메뉴 건너뛰기




Volumn 69, Issue , 2013, Pages 209-272

Bacterial cell-envelope glycoconjugates

Author keywords

Archaea; Bacteria; Glycoprotein; Secondary cell wall polymers; Surface layer

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; GLYCOCONJUGATE; MEMBRANE PROTEIN; O ANTIGEN; SIALIC ACID; TRISACCHARIDE;

EID: 84888167777     PISSN: 00652318     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-408093-5.00006-X     Document Type: Chapter
Times cited : (40)

References (265)
  • 1
    • 0002172016 scopus 로고
    • The carbohydrates of glycoproteins
    • John Wiley & Sons, New York, V. Ginsburg, P.W. Robbins (Eds.)
    • Kobata A. The carbohydrates of glycoproteins. Biology of Carbohydrates 1984, Vol. 2:87-161. John Wiley & Sons, New York. V. Ginsburg, P.W. Robbins (Eds.).
    • (1984) Biology of Carbohydrates , vol.2 , pp. 87-161
    • Kobata, A.1
  • 2
    • 0021744087 scopus 로고
    • Spatial conformation of glycans and glycoproteins
    • Montreuil J. Spatial conformation of glycans and glycoproteins. Biol. Cell 1984, 51:115-131.
    • (1984) Biol. Cell , vol.51 , pp. 115-131
    • Montreuil, J.1
  • 3
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 1985, 54:631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 4
    • 0004106191 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler (Eds.)
    • Essentials of Glycobiology 2009, 784. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 2nd ed. A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler (Eds.).
    • (2009) Essentials of Glycobiology , pp. 784
  • 5
    • 0026343404 scopus 로고
    • Bacterial surface layer glycoproteins
    • Messner P., Sleytr U.B. Bacterial surface layer glycoproteins. Glycobiology 1991, 1:545-551.
    • (1991) Glycobiology , vol.1 , pp. 545-551
    • Messner, P.1    Sleytr, U.B.2
  • 8
    • 0345059167 scopus 로고    scopus 로고
    • Sweet new world: Glycoproteins in bacterial pathogens
    • Schmidt M.A., Riley L.W., Benz I. Sweet new world: Glycoproteins in bacterial pathogens. Trends Microbiol. 2003, 11:554-561.
    • (2003) Trends Microbiol. , vol.11 , pp. 554-561
    • Schmidt, M.A.1    Riley, L.W.2    Benz, I.3
  • 9
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski M., Wren B.W. Protein glycosylation in bacterial mucosal pathogens. Nat. Rev. Microbiol. 2005, 3:225-237.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 225-237
    • Szymanski, M.1    Wren, B.W.2
  • 10
    • 84886267132 scopus 로고    scopus 로고
    • Eubacteria and Archaea
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler (Eds.)
    • Esko J.D., Doering T.L., Raetz C.R.H. Eubacteria and Archaea. Essentials of Glycobiology 2009, 293-299. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 2nd ed. A. Varki, R.D. Cummings, J.D. Esko, H.H. Freeze, P. Stanley, C.R. Bertozzi, G.W. Hart, M.E. Etzler (Eds.).
    • (2009) Essentials of Glycobiology , pp. 293-299
    • Esko, J.D.1    Doering, T.L.2    Raetz, C.R.H.3
  • 11
    • 70349392087 scopus 로고    scopus 로고
    • Prokaryotic protein glycosylation is rapidly expanding from "curiosity" to "ubiquity"
    • Messner P. Prokaryotic protein glycosylation is rapidly expanding from "curiosity" to "ubiquity". ChemBioChem 2009, 13:2151-2154.
    • (2009) ChemBioChem , vol.13 , pp. 2151-2154
    • Messner, P.1
  • 12
    • 79951966895 scopus 로고    scopus 로고
    • Analogies and homologies in lipopolysaccharide and glycoprotein biosynthesis in bacteria
    • Hug I., Feldman M.F. Analogies and homologies in lipopolysaccharide and glycoprotein biosynthesis in bacteria. Glycobiology 2011, 21:138-151.
    • (2011) Glycobiology , vol.21 , pp. 138-151
    • Hug, I.1    Feldman, M.F.2
  • 13
    • 84871292768 scopus 로고    scopus 로고
    • The Bacillus subtilis endospore: Assembly and functions of the multilayered coat
    • McKenney P.T., Driks A., Eichenberger P. The Bacillus subtilis endospore: Assembly and functions of the multilayered coat. Nat. Rev. Microbiol. 2013, 11:33-44.
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 33-44
    • McKenney, P.T.1    Driks, A.2    Eichenberger, P.3
  • 14
    • 0013002180 scopus 로고
    • Glycoproteins as cell surface structural components
    • Mescher M.F. Glycoproteins as cell surface structural components. Trends Biochem. Sci. 1981, 6:97-99.
    • (1981) Trends Biochem. Sci. , vol.6 , pp. 97-99
    • Mescher, M.F.1
  • 15
    • 0024346543 scopus 로고
    • Structure and biosynthesis of prokaryotic glycoproteins
    • Lechner J., Wieland F. Structure and biosynthesis of prokaryotic glycoproteins. Annu. Rev. Biochem. 1989, 58:173-194.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 173-194
    • Lechner, J.1    Wieland, F.2
  • 16
    • 77956818765 scopus 로고
    • Bacterial glycoproteins
    • Elsevier, Amsterdam, J. Montreuil, J.F.G. Vliegenthart, H. Schachter (Eds.)
    • Sumper M., Wieland F.T. Bacterial glycoproteins. Glycoproteins 1995, 455-473. Elsevier, Amsterdam. J. Montreuil, J.F.G. Vliegenthart, H. Schachter (Eds.).
    • (1995) Glycoproteins , pp. 455-473
    • Sumper, M.1    Wieland, F.T.2
  • 17
    • 24944463449 scopus 로고    scopus 로고
    • Posttranslational protein modification in Archaea
    • Eichler J., Adams M.W.W. Posttranslational protein modification in Archaea. Microbiol. Mol. Biol. Rev. 2005, 69:393-425.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 393-425
    • Eichler, J.1    Adams, M.W.W.2
  • 19
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides-All of the theories are correct
    • Varki A. Biological roles of oligosaccharides-All of the theories are correct. Glycobiology 1993, 3:97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 20
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro R. Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 2002, 12:43R-56R.
    • (2002) Glycobiology , vol.12
    • Spiro, R.1
  • 21
    • 5444247077 scopus 로고    scopus 로고
    • Structure, function and pathology of O-mannosyl glycans
    • Endo T. Structure, function and pathology of O-mannosyl glycans. Glycoconj. J. 2004, 21:3-7.
    • (2004) Glycoconj. J. , vol.21 , pp. 3-7
    • Endo, T.1
  • 22
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems
    • Weerapana E., Imperiali B. Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems. Glycobiology 2006, 16:91R-101R.
    • (2006) Glycobiology , vol.16
    • Weerapana, E.1    Imperiali, B.2
  • 23
    • 0017278612 scopus 로고
    • Purification and characterization of a prokaryotic glycoprotein from the cell envelope of Halobacterium salinarium
    • Mescher M.F., Strominger J.L. Purification and characterization of a prokaryotic glycoprotein from the cell envelope of Halobacterium salinarium. J. Biol. Chem. 1976, 251:2005-2014.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2005-2014
    • Mescher, M.F.1    Strominger, J.L.2
  • 24
    • 0017066835 scopus 로고
    • Chemical characterization of the regularly arrayed surface layers of Clostridium thermosaccharolyticum and Clostridium thermohydrosulfuricum
    • Sleytr U.B., Thorne K.J.I. Chemical characterization of the regularly arrayed surface layers of Clostridium thermosaccharolyticum and Clostridium thermohydrosulfuricum. J. Bacteriol. 1976, 126:377-383.
    • (1976) J. Bacteriol. , vol.126 , pp. 377-383
    • Sleytr, U.B.1    Thorne, K.J.I.2
  • 25
    • 0001263941 scopus 로고
    • Cell envelopes of archaebacteria
    • Academic Press, New York, C.R. Woese, R.S. Wolfe (Eds.) The Bacteria
    • Kandler O., König H. Cell envelopes of archaebacteria. Archaebacteria 1985, Vol. VIII:413-457. Academic Press, New York. C.R. Woese, R.S. Wolfe (Eds.).
    • (1985) Archaebacteria , vol.VIII , pp. 413-457
    • Kandler, O.1    König, H.2
  • 26
    • 0023235232 scopus 로고
    • Halobacterial glycoprotein biosynthesis
    • Sumper M. Halobacterial glycoprotein biosynthesis. Biochim. Biophys. Acta 1987, 906:69-79.
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 69-79
    • Sumper, M.1
  • 28
    • 0021099776 scopus 로고
    • Purification and some properties of the endogenous, autolytic N-acetylmuramoylhydrolase of Streptococcus faecium, a bacterial glycoenzyme
    • Kawamura T., Shockman G.D. Purification and some properties of the endogenous, autolytic N-acetylmuramoylhydrolase of Streptococcus faecium, a bacterial glycoenzyme. J. Biol. Chem. 1983, 258:9514-9521.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9514-9521
    • Kawamura, T.1    Shockman, G.D.2
  • 29
    • 0032783142 scopus 로고    scopus 로고
    • Identification of a glycoprotein produced by enterotoxigenic Escherichia coli
    • Lindenthal C., Elsinghorst E.A. Identification of a glycoprotein produced by enterotoxigenic Escherichia coli. Infect. Immun. 1999, 67:4084-4091.
    • (1999) Infect. Immun. , vol.67 , pp. 4084-4091
    • Lindenthal, C.1    Elsinghorst, E.A.2
  • 30
    • 33646757219 scopus 로고    scopus 로고
    • Flagellar glycosylation-A new component of the motility repertoire?
    • Logan S.M. Flagellar glycosylation-A new component of the motility repertoire?. Microbiology 2006, 152:1249-1262.
    • (2006) Microbiology , vol.152 , pp. 1249-1262
    • Logan, S.M.1
  • 31
    • 0022337274 scopus 로고
    • Halobacterial flagellins are sulfated glycoproteins
    • Wieland F., Paul G., Sumper M. Halobacterial flagellins are sulfated glycoproteins. J. Biol. Chem. 1985, 260:15180-15185.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15180-15185
    • Wieland, F.1    Paul, G.2    Sumper, M.3
  • 32
    • 0028783792 scopus 로고
    • Glycosylation of the flagellin of the polar flagellum of Azospirillum brasilense, a Gram-negative nitrogen-fixing bacterium
    • Moens S., Michiels K., Vanderleyden J. Glycosylation of the flagellin of the polar flagellum of Azospirillum brasilense, a Gram-negative nitrogen-fixing bacterium. Microbiology 1995, 141:2651-2657.
    • (1995) Microbiology , vol.141 , pp. 2651-2657
    • Moens, S.1    Michiels, K.2    Vanderleyden, J.3
  • 33
    • 0035860764 scopus 로고    scopus 로고
    • Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin
    • Thibault P., Logan S.M., Kelly J.F., Brisson J.-R., Ewing C.P., Trust T.J., Guerry P. Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin. J. Biol. Chem. 2001, 276:34862-34870.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34862-34870
    • Thibault, P.1    Logan, S.M.2    Kelly, J.F.3    Brisson, J.-R.4    Ewing, C.P.5    Trust, T.J.6    Guerry, P.7
  • 34
    • 0037560879 scopus 로고    scopus 로고
    • Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori
    • Schirm M., Soo E.C., Aubry A.J., Austin J., Thibault P., Logan S.M. Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori. Mol. Microbiol. 2003, 48:1579-1592.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1579-1592
    • Schirm, M.1    Soo, E.C.2    Aubry, A.J.3    Austin, J.4    Thibault, P.5    Logan, S.M.6
  • 35
    • 28544452605 scopus 로고    scopus 로고
    • Identification of unusual bacterial glycosylation by tandem mass spectrometry analyses of intact proteins
    • Schirm M., Schoenhofen I.C., Logan S.M., Waldron K.C., Thibault P. Identification of unusual bacterial glycosylation by tandem mass spectrometry analyses of intact proteins. Anal. Chem. 2005, 77:7774-7782.
    • (2005) Anal. Chem. , vol.77 , pp. 7774-7782
    • Schirm, M.1    Schoenhofen, I.C.2    Logan, S.M.3    Waldron, K.C.4    Thibault, P.5
  • 36
    • 33644850378 scopus 로고    scopus 로고
    • Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: Enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways
    • Schoenhofen C., McNally D.J., Vinogradov E., Whitfield D., Young N.M., Dick S., Wakarchuk W.W., Brisson J.-R., Logan S.M. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: Enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J. Biol. Chem. 2006, 281:723-732.
    • (2006) J. Biol. Chem. , vol.281 , pp. 723-732
    • Schoenhofen, C.1    McNally, D.J.2    Vinogradov, E.3    Whitfield, D.4    Young, N.M.5    Dick, S.6    Wakarchuk, W.W.7    Brisson, J.-R.8    Logan, S.M.9
  • 37
    • 66249092413 scopus 로고    scopus 로고
    • The CMP-legionaminic acid pathway in Campylobacter: Biosynthesis involving novel GDP-linked precursors
    • Schoenhofen C., Vinogradov E., Whitfield D.M., Brisson J.-R., Logan S.M. The CMP-legionaminic acid pathway in Campylobacter: Biosynthesis involving novel GDP-linked precursors. Glycobiology 2009, 19:715-725.
    • (2009) Glycobiology , vol.19 , pp. 715-725
    • Schoenhofen, C.1    Vinogradov, E.2    Whitfield, D.M.3    Brisson, J.-R.4    Logan, S.M.5
  • 38
    • 0035854812 scopus 로고    scopus 로고
    • Structural characterization of the Pseudomonas aeruginosa 1244 pilin glycan
    • Castric P., Cassels F.J., Carlson R.W. Structural characterization of the Pseudomonas aeruginosa 1244 pilin glycan. J. Biol. Chem. 2001, 276:26479-26485.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26479-26485
    • Castric, P.1    Cassels, F.J.2    Carlson, R.W.3
  • 39
    • 0028199696 scopus 로고
    • The structure of the O-specific chain of Legionella pneumophila serogroup 1 lipopolysaccharide
    • Knirel Y.A., Rietschel E.T., Marre R., Zähringer U. The structure of the O-specific chain of Legionella pneumophila serogroup 1 lipopolysaccharide. Eur. J. Biochem. 1994, 221:239-245.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 239-245
    • Knirel, Y.A.1    Rietschel, E.T.2    Marre, R.3    Zähringer, U.4
  • 41
    • 0035543161 scopus 로고    scopus 로고
    • The rkp-3 gene region of Sinorhizobium meliloti RM41 contains strain-specific genes that determine K antigen structure
    • Kiss E., Kereszt A., Barta F., Stephens S., Reuhs B.L., Kondorosi Á., Putnoky P. The rkp-3 gene region of Sinorhizobium meliloti RM41 contains strain-specific genes that determine K antigen structure. Mol. Plant-Microbe Interact. 2001, 14:1395-1403.
    • (2001) Mol. Plant-Microbe Interact. , vol.14 , pp. 1395-1403
    • Kiss, E.1    Kereszt, A.2    Barta, F.3    Stephens, S.4    Reuhs, B.L.5    Kondorosi, Á.6    Putnoky, P.7
  • 42
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • Szymanski M., Yao R., Ewing C.P., Trust T.J., Guerry P. Evidence for a system of general protein glycosylation in Campylobacter jejuni. Mol. Microbiol. 1999, 32:1022-1030.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1022-1030
    • Szymanski, M.1    Yao, R.2    Ewing, C.P.3    Trust, T.J.4    Guerry, P.5
  • 43
    • 0036428656 scopus 로고    scopus 로고
    • Structural heterogeneity of carbohydrate modifications affects serospecificity of Campylobacter flagellins
    • Logan S.M., Kelly J.F., Thibault P., Ewing C.P., Guerry P. Structural heterogeneity of carbohydrate modifications affects serospecificity of Campylobacter flagellins. Mol. Microbiol. 2002, 46:587-597.
    • (2002) Mol. Microbiol. , vol.46 , pp. 587-597
    • Logan, S.M.1    Kelly, J.F.2    Thibault, P.3    Ewing, C.P.4    Guerry, P.5
  • 44
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab R.M. How bacteria assemble flagella. Annu. Rev. Microbiol. 2003, 57:77-100.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 46
    • 0037033113 scopus 로고    scopus 로고
    • Studies on the function of oligosaccharyl transferase subunits. Stt3p is directly involved in the glycosylation process
    • Yan Q., Lennarz W.J. Studies on the function of oligosaccharyl transferase subunits. Stt3p is directly involved in the glycosylation process. J. Biol. Chem. 2002, 277:47692-47700.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47692-47700
    • Yan, Q.1    Lennarz, W.J.2
  • 51
    • 77956531782 scopus 로고    scopus 로고
    • Glycomimicry: Display of the GM3 sugar epitope on Escherichia coli and Salmonella enterica sv Typhimurium
    • Ilg K., Yavuz E., Maffioli C., Priem B., Aebi M. Glycomimicry: Display of the GM3 sugar epitope on Escherichia coli and Salmonella enterica sv Typhimurium. Glycobiology 2010, 20:1289-1297.
    • (2010) Glycobiology , vol.20 , pp. 1289-1297
    • Ilg, K.1    Yavuz, E.2    Maffioli, C.3    Priem, B.4    Aebi, M.5
  • 52
    • 79959191882 scopus 로고    scopus 로고
    • X-ray structure of a bacterial oligosaccharyltransferase
    • Lizak C., Gerber S., Numao S., Aebi M., Locher K.P. X-ray structure of a bacterial oligosaccharyltransferase. Nature 2011, 474:350-355.
    • (2011) Nature , vol.474 , pp. 350-355
    • Lizak, C.1    Gerber, S.2    Numao, S.3    Aebi, M.4    Locher, K.P.5
  • 55
    • 36549029858 scopus 로고    scopus 로고
    • Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation
    • Faridmoayer A., Fentabil M.A., Mills D.C., Klassen J.S., Feldman M.F. Functional characterization of bacterial oligosaccharyltransferases involved in O-linked protein glycosylation. J. Bacteriol. 2007, 189:8088-8098.
    • (2007) J. Bacteriol. , vol.189 , pp. 8088-8098
    • Faridmoayer, A.1    Fentabil, M.A.2    Mills, D.C.3    Klassen, J.S.4    Feldman, M.F.5
  • 56
    • 79958061550 scopus 로고    scopus 로고
    • Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N'-diacetylbacillosamine
    • Hartley M.D., Morrison M.J., Aas F.E., Børud B., Koomey M., Imperiali B. Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N'-diacetylbacillosamine. Biochemistry 2011, 50:4936-4948.
    • (2011) Biochemistry , vol.50 , pp. 4936-4948
    • Hartley, M.D.1    Morrison, M.J.2    Aas, F.E.3    Børud, B.4    Koomey, M.5    Imperiali, B.6
  • 57
    • 0037387036 scopus 로고    scopus 로고
    • Bacterial glycoproteins: Functions, biosynthesis and applications
    • Upreti R.K., Kumar M., Shankar V. Bacterial glycoproteins: Functions, biosynthesis and applications. Proteomics 2003, 3:363-379.
    • (2003) Proteomics , vol.3 , pp. 363-379
    • Upreti, R.K.1    Kumar, M.2    Shankar, V.3
  • 58
    • 1942540043 scopus 로고    scopus 로고
    • Prokaryotic glycoproteins: Unexplored but important
    • Messner P. Prokaryotic glycoproteins: Unexplored but important. J. Bacteriol. 2004, 186:2517-2519.
    • (2004) J. Bacteriol. , vol.186 , pp. 2517-2519
    • Messner, P.1
  • 59
    • 50249135417 scopus 로고    scopus 로고
    • Campylobacter sugars sticking out
    • Guerry P., Szymanski C.M. Campylobacter sugars sticking out. Trends Microbiol. 2008, 16:428-435.
    • (2008) Trends Microbiol. , vol.16 , pp. 428-435
    • Guerry, P.1    Szymanski, C.M.2
  • 60
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria: Sweeter than ever
    • Nothaft H., Szymanski C.M. Protein glycosylation in bacteria: Sweeter than ever. Nat. Rev. Microbiol. 2010, 8:765-778.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 61
    • 77952556110 scopus 로고    scopus 로고
    • Genetic, structural, and antigenic analyses of glycan diversity in the O-linked protein glycosylation systems of human Neisseria species
    • Børud B., Aas F.E., Vik Å., Winther-Larsen H.C., Egge-Jacobsen W., Koomey M. Genetic, structural, and antigenic analyses of glycan diversity in the O-linked protein glycosylation systems of human Neisseria species. J. Bacteriol. 2010, 192:2816-2829.
    • (2010) J. Bacteriol. , vol.192 , pp. 2816-2829
    • Børud, B.1    Aas, F.E.2    Vik, Å.3    Winther-Larsen, H.C.4    Egge-Jacobsen, W.5    Koomey, M.6
  • 62
    • 80054801695 scopus 로고    scopus 로고
    • Exploiting bacterial glycosylation machineries for the synthesis of a Lewis antigen-containing glycoprotein
    • Hug I., Zheng B., Reiz B., Whittal R.M., Fentabil A., Klassen J.S., Feldman M.F. Exploiting bacterial glycosylation machineries for the synthesis of a Lewis antigen-containing glycoprotein. J. Biol. Chem. 2011, 286:37887-37894.
    • (2011) J. Biol. Chem. , vol.286 , pp. 37887-37894
    • Hug, I.1    Zheng, B.2    Reiz, B.3    Whittal, R.M.4    Fentabil, A.5    Klassen, J.S.6    Feldman, M.F.7
  • 64
    • 0343097375 scopus 로고
    • On the cell wall structure of Spirillum serpens
    • Murray R.G.E. On the cell wall structure of Spirillum serpens. Can. J. Microbiol. 1963, 9:381-392.
    • (1963) Can. J. Microbiol. , vol.9 , pp. 381-392
    • Murray, R.G.E.1
  • 65
    • 0013978487 scopus 로고
    • Moiré patterns in electron micrographs of a bacterial membrane
    • Glauert M. Moiré patterns in electron micrographs of a bacterial membrane. J. Cell Sci. 1966, 1:425-428.
    • (1966) J. Cell Sci. , vol.1 , pp. 425-428
    • Glauert, M.1
  • 66
    • 0016564906 scopus 로고
    • Cell envelopes with regularly arranged surface subunits in Acinetobacter and related bacteria
    • Thornley M.J. Cell envelopes with regularly arranged surface subunits in Acinetobacter and related bacteria. CRC Crit. Rev. Microbiol. 1975, 4:65-100.
    • (1975) CRC Crit. Rev. Microbiol. , vol.4 , pp. 65-100
    • Thornley, M.J.1
  • 67
    • 0018195592 scopus 로고
    • Regular arrays of macromolecules on bacterial cell walls: Structure, chemistry, assembly and function
    • Sleytr U.B. Regular arrays of macromolecules on bacterial cell walls: Structure, chemistry, assembly and function. Int. Rev. Cytol. 1978, 53:1-64.
    • (1978) Int. Rev. Cytol. , vol.53 , pp. 1-64
    • Sleytr, U.B.1
  • 68
    • 0019395615 scopus 로고
    • Ultrastructure, chemistry, and function of the bacterial wall
    • Beveridge T.J. Ultrastructure, chemistry, and function of the bacterial wall. Int. Rev. Cytol. 1981, 72:229-317.
    • (1981) Int. Rev. Cytol. , vol.72 , pp. 229-317
    • Beveridge, T.J.1
  • 69
    • 0003423980 scopus 로고    scopus 로고
    • Crystalline surface layers on eubacteria and archaeobacteria
    • R.G. Landes/Academic Press, Austin, TX, U.B. Sleytr, P. Messner, D. Pum, M. Sára (Eds.)
    • Sleytr U.B., Messner P., Pum D., Sára M. Crystalline surface layers on eubacteria and archaeobacteria. Crystalline Bacterial Cell Surface Proteins 1996, 211-225. R.G. Landes/Academic Press, Austin, TX. U.B. Sleytr, P. Messner, D. Pum, M. Sára (Eds.).
    • (1996) Crystalline Bacterial Cell Surface Proteins , pp. 211-225
    • Sleytr, U.B.1    Messner, P.2    Pum, D.3    Sára, M.4
  • 70
    • 0032464347 scopus 로고    scopus 로고
    • Structural research on surface layers: A focus on stability, surface layer homology domains, and surface layer-cell wall interactions
    • Engelhardt H., Peters J. Structural research on surface layers: A focus on stability, surface layer homology domains, and surface layer-cell wall interactions. J. Struct. Biol. 1998, 124:276-302.
    • (1998) J. Struct. Biol. , vol.124 , pp. 276-302
    • Engelhardt, H.1    Peters, J.2
  • 71
  • 73
    • 85019933067 scopus 로고    scopus 로고
    • Crystalline cell surface layers (S layers)
    • Academic Press/Elsevier, San Diego, CA, M. Schaechter (Ed.)
    • Sleytr U.B., Messner P. Crystalline cell surface layers (S layers). Encyclopedia of Microbiology 2009, Vol. 1:89-98. Academic Press/Elsevier, San Diego, CA. 3rd ed. M. Schaechter (Ed.).
    • (2009) Encyclopedia of Microbiology , vol.1 , pp. 89-98
    • Sleytr, U.B.1    Messner, P.2
  • 74
    • 84900086602 scopus 로고    scopus 로고
    • Occurrence, structure, chemistry, genetics, morphogenesis, and functions of S-layers
    • Springer, Berlin, H. König, H. Claus, A. Varma (Eds.)
    • Messner P., Schäffer C., Egelseer E.-M., Sleytr U.B. Occurrence, structure, chemistry, genetics, morphogenesis, and functions of S-layers. Prokaryotic Cell Wall Compounds-Structure and Biochemistry 2010, 53-109. Springer, Berlin. H. König, H. Claus, A. Varma (Eds.).
    • (2010) Prokaryotic Cell Wall Compounds-Structure and Biochemistry , pp. 53-109
    • Messner, P.1    Schäffer, C.2    Egelseer, E.-M.3    Sleytr, U.B.4
  • 75
    • 77956795061 scopus 로고
    • Cell envelopes of archaea: Structure and chemistry
    • Elsevier, Amsterdam, M. Kates, D.J. Kushner, A.T. Matheson (Eds.)
    • Kandler O., König H. Cell envelopes of archaea: Structure and chemistry. The Biochemistry of Archaea (Archaebacteria) 1993, 223-259. Elsevier, Amsterdam. M. Kates, D.J. Kushner, A.T. Matheson (Eds.).
    • (1993) The Biochemistry of Archaea (Archaebacteria) , pp. 223-259
    • Kandler, O.1    König, H.2
  • 78
    • 0024523934 scopus 로고
    • Principles of organization in eubacterial and archaebacterial surface proteins
    • Baumeister W., Wildhaber I., Phipps B.M. Principles of organization in eubacterial and archaebacterial surface proteins. Can. J. Microbiol. 1989, 35:215-227.
    • (1989) Can. J. Microbiol. , vol.35 , pp. 215-227
    • Baumeister, W.1    Wildhaber, I.2    Phipps, B.M.3
  • 79
    • 0002734640 scopus 로고
    • Self-assembly of crystalline bacterial cell surface layers
    • CRC Press, Boca Raton, FL, H. Plattner (Ed.)
    • Sleytr U.B., Messner P. Self-assembly of crystalline bacterial cell surface layers. Electron Microscopy of Subcellular Dynamics 1989, 13-31. CRC Press, Boca Raton, FL. H. Plattner (Ed.).
    • (1989) Electron Microscopy of Subcellular Dynamics , pp. 13-31
    • Sleytr, U.B.1    Messner, P.2
  • 80
    • 0033583512 scopus 로고    scopus 로고
    • Crystalline bacterial cell surface layers (S-layers): From supramolecular cell structure to biomimetics and nanotechnology
    • Sleytr U.B., Messner P., Pum D., Sára M. Crystalline bacterial cell surface layers (S-layers): From supramolecular cell structure to biomimetics and nanotechnology. Angew. Chem. Int. Ed. Engl. 1999, 38:1034-1054.
    • (1999) Angew. Chem. Int. Ed. Engl. , vol.38 , pp. 1034-1054
    • Sleytr, U.B.1    Messner, P.2    Pum, D.3    Sára, M.4
  • 81
    • 0030058166 scopus 로고    scopus 로고
    • Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans monitored by atomic force microscopy
    • Müller J., Baumeister W., Engel A. Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans monitored by atomic force microscopy. J. Bacteriol. 1996, 178:3025-3030.
    • (1996) J. Bacteriol. , vol.178 , pp. 3025-3030
    • Müller, J.1    Baumeister, W.2    Engel, A.3
  • 82
    • 0035239182 scopus 로고    scopus 로고
    • Application of atomic force microscopy to microbial surfaces: From reconstituted cell surface layers to living cells
    • Dufrêne Y.F. Application of atomic force microscopy to microbial surfaces: From reconstituted cell surface layers to living cells. Micron 2001, 32:153-165.
    • (2001) Micron , vol.32 , pp. 153-165
    • Dufrêne, Y.F.1
  • 83
    • 80054683180 scopus 로고    scopus 로고
    • S-layer protein lattices studied by scanning force microscopy
    • Wiley-VCH, Weinheim, Germany, C.S.S.R. Kumar (Ed.) Nanomaterial for the Life Sciences
    • Pum D., Tang J., Hinterdorfer P., Toca-Herrera J.-L., Sleytr U.B. S-layer protein lattices studied by scanning force microscopy. Biomimetic and Bioinspired Nanomaterials 2010, Vol. 7:459-510. Wiley-VCH, Weinheim, Germany. C.S.S.R. Kumar (Ed.).
    • (2010) Biomimetic and Bioinspired Nanomaterials , vol.7 , pp. 459-510
    • Pum, D.1    Tang, J.2    Hinterdorfer, P.3    Toca-Herrera, J.-L.4    Sleytr, U.B.5
  • 85
    • 27944466452 scopus 로고    scopus 로고
    • Crystalline bacterial cell surface layers (S-layers): A versatile self-assembly system
    • Taylor & Francis, Boca Raton, FL, A. Ciferri (Ed.)
    • Sleytr U.B., Sára M., Pum D., Schuster B. Crystalline bacterial cell surface layers (S-layers): A versatile self-assembly system. Supramolecular Polymers 2005, 583-616. Taylor & Francis, Boca Raton, FL. 2nd ed. A. Ciferri (Ed.).
    • (2005) Supramolecular Polymers , pp. 583-616
    • Sleytr, U.B.1    Sára, M.2    Pum, D.3    Schuster, B.4
  • 87
    • 2242485596 scopus 로고    scopus 로고
    • The first biantennary bacterial secondary cell wall polymer from bacteria and its influence on S-layer glycoprotein assembly
    • Steindl C., Schäffer C., Wugeditsch T., Graninger M., Matecko I., Müller N., Messner P. The first biantennary bacterial secondary cell wall polymer from bacteria and its influence on S-layer glycoprotein assembly. Biochem. J. 2002, 368:483-494.
    • (2002) Biochem. J. , vol.368 , pp. 483-494
    • Steindl, C.1    Schäffer, C.2    Wugeditsch, T.3    Graninger, M.4    Matecko, I.5    Müller, N.6    Messner, P.7
  • 88
    • 0034998889 scopus 로고    scopus 로고
    • Analysis of the structure-function relationship of the S-layer protein SbsC of Bacillus stearothermophilus ATCC 12980 by producing truncated forms
    • Jarosch M., Egelseer E.M., Huber C., Moll D., Mattanovich D., Sleytr U.B., Sára M. Analysis of the structure-function relationship of the S-layer protein SbsC of Bacillus stearothermophilus ATCC 12980 by producing truncated forms. Microbiology 2001, 147:1353-1363.
    • (2001) Microbiology , vol.147 , pp. 1353-1363
    • Jarosch, M.1    Egelseer, E.M.2    Huber, C.3    Moll, D.4    Mattanovich, D.5    Sleytr, U.B.6    Sára, M.7
  • 89
    • 1242339692 scopus 로고    scopus 로고
    • Biophysical characterization of the entire bacterial surface layer protein SbsB and its two distinct functional domains
    • Rünzler D., Huber C., Moll D., Köhler G., Sára M. Biophysical characterization of the entire bacterial surface layer protein SbsB and its two distinct functional domains. J. Biol. Chem. 2004, 279:5207-5215.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5207-5215
    • Rünzler, D.1    Huber, C.2    Moll, D.3    Köhler, G.4    Sára, M.5
  • 90
    • 48149095082 scopus 로고    scopus 로고
    • The structure and binding behavior of the bacterial cell surface layer protein SbsC
    • Pavkov T., Egelseer E.M., Tesarz M., Svergun D.I., Sleytr U.B., Keller W. The structure and binding behavior of the bacterial cell surface layer protein SbsC. Structure 2008, 16:1226-1237.
    • (2008) Structure , vol.16 , pp. 1226-1237
    • Pavkov, T.1    Egelseer, E.M.2    Tesarz, M.3    Svergun, D.I.4    Sleytr, U.B.5    Keller, W.6
  • 94
    • 39349116630 scopus 로고    scopus 로고
    • Structure prediction of an S-layer protein by the mean force method
    • Horejs C., Pum D., Sleytr U.B., Tscheliessnig R. Structure prediction of an S-layer protein by the mean force method. J. Chem. Phys. 2008, 128:065106.
    • (2008) J. Chem. Phys. , vol.128 , pp. 065106
    • Horejs, C.1    Pum, D.2    Sleytr, U.B.3    Tscheliessnig, R.4
  • 95
    • 79953321225 scopus 로고    scopus 로고
    • Monte Carlo study of the molecular mechanisms of surface-layer protein self-assembly
    • Horejs C., Mitra M.K., Pum D., Sleytr U.B., Muthukumar M. Monte Carlo study of the molecular mechanisms of surface-layer protein self-assembly. J. Chem. Phys. 2011, 134:125103.
    • (2011) J. Chem. Phys. , vol.134 , pp. 125103
    • Horejs, C.1    Mitra, M.K.2    Pum, D.3    Sleytr, U.B.4    Muthukumar, M.5
  • 97
    • 0030867822 scopus 로고    scopus 로고
    • Basic and applied S-layer research: An overview
    • Sleytr U.B. Basic and applied S-layer research: An overview. FEMS Microbiol. Rev. 1997, 20:5-12.
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 5-12
    • Sleytr, U.B.1
  • 99
    • 35148873213 scopus 로고    scopus 로고
    • Are S-layers exoskeletons? The basic function of protein surface layers revisited
    • Engelhardt H. Are S-layers exoskeletons? The basic function of protein surface layers revisited. J. Struct. Biol. 2007, 160:115-124.
    • (2007) J. Struct. Biol. , vol.160 , pp. 115-124
    • Engelhardt, H.1
  • 101
    • 0029876584 scopus 로고    scopus 로고
    • Dynamics in oxygen-induced changes in S-layer protein synthesis from Bacillus stearothermophilus PV72 and the S-layer-deficient variant T5 in continuous culture and studies of the cell wall composition
    • Sára M., Kuen B., Mayer H.F., Mandl F., Schuster K.C., Sleytr U.B. Dynamics in oxygen-induced changes in S-layer protein synthesis from Bacillus stearothermophilus PV72 and the S-layer-deficient variant T5 in continuous culture and studies of the cell wall composition. J. Bacteriol. 1996, 178:2108-2117.
    • (1996) J. Bacteriol. , vol.178 , pp. 2108-2117
    • Sára, M.1    Kuen, B.2    Mayer, H.F.3    Mandl, F.4    Schuster, K.C.5    Sleytr, U.B.6
  • 102
    • 0030700288 scopus 로고    scopus 로고
    • Molecular mechanisms of Campylobacter fetus surface layer protein expression
    • Dworkin J., Blaser M.J. Molecular mechanisms of Campylobacter fetus surface layer protein expression. Mol. Microbiol. 1997, 26:433-440.
    • (1997) Mol. Microbiol. , vol.26 , pp. 433-440
    • Dworkin, J.1    Blaser, M.J.2
  • 103
    • 0032138208 scopus 로고    scopus 로고
    • Campylobacter fetus-Emerging infection and model system for bacterial pathogenesis at mucosal surfaces
    • Blaser M.J. Campylobacter fetus-Emerging infection and model system for bacterial pathogenesis at mucosal surfaces. Clin. Infect. Dis. 1998, 27:256-258.
    • (1998) Clin. Infect. Dis. , vol.27 , pp. 256-258
    • Blaser, M.J.1
  • 104
    • 0035117468 scopus 로고    scopus 로고
    • S-layer variation in Bacillus stearothermophilus PV72 is based on DNA rearrangements between the chromosome and the naturally occurring megaplasmids
    • Scholz H.C., Riedmann E., Witte A., Lubitz W., Kuen B. S-layer variation in Bacillus stearothermophilus PV72 is based on DNA rearrangements between the chromosome and the naturally occurring megaplasmids. J. Bacteriol. 2001, 183:1672-1679.
    • (2001) J. Bacteriol. , vol.183 , pp. 1672-1679
    • Scholz, H.C.1    Riedmann, E.2    Witte, A.3    Lubitz, W.4    Kuen, B.5
  • 105
    • 0036955885 scopus 로고    scopus 로고
    • Isolation of three new surface layer protein genes (slp) from Lactobacillus brevis ATCC 14869 and characterization of the change in their expression under aerated and anaerobic conditions
    • Jakava-Viljanen M., Åvall-Jääskeläinen S., Messner P., Sleytr U.B., Palva A. Isolation of three new surface layer protein genes (slp) from Lactobacillus brevis ATCC 14869 and characterization of the change in their expression under aerated and anaerobic conditions. J. Bacteriol. 2002, 184:6786-6795.
    • (2002) J. Bacteriol. , vol.184 , pp. 6786-6795
    • Jakava-Viljanen, M.1    Åvall-Jääskeläinen, S.2    Messner, P.3    Sleytr, U.B.4    Palva, A.5
  • 106
    • 80055084408 scopus 로고    scopus 로고
    • Characterization and scope of S-layer protein O-glycosylation in Tannerella forsythia
    • Posch G., Pabst M., Brecker L., Altmann F., Messner P., Schäffer C. Characterization and scope of S-layer protein O-glycosylation in Tannerella forsythia. J. Biol. Chem. 2011, 286:38714-38724.
    • (2011) J. Biol. Chem. , vol.286 , pp. 38714-38724
    • Posch, G.1    Pabst, M.2    Brecker, L.3    Altmann, F.4    Messner, P.5    Schäffer, C.6
  • 107
    • 33646452547 scopus 로고    scopus 로고
    • Analyzing the dynamic bacterial glycome with a lectin microarray approach
    • Hsu K.-L., Pilobello K.T., Mahal L.K. Analyzing the dynamic bacterial glycome with a lectin microarray approach. Nat. Chem. Biol. 2006, 2:153-157.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 153-157
    • Hsu, K.-L.1    Pilobello, K.T.2    Mahal, L.K.3
  • 108
    • 33947428014 scopus 로고    scopus 로고
    • Loss of adherence ability to human gingival epithelial cells in S-layer protein-deficient mutants of Tannerella forsythensis
    • Sakakibara J., Nagano K., Murakami Y., Higuchi N., Nakamura H., Shimozato K., Yoshimura F. Loss of adherence ability to human gingival epithelial cells in S-layer protein-deficient mutants of Tannerella forsythensis. Microbiology 2007, 153:866-876.
    • (2007) Microbiology , vol.153 , pp. 866-876
    • Sakakibara, J.1    Nagano, K.2    Murakami, Y.3    Higuchi, N.4    Nakamura, H.5    Shimozato, K.6    Yoshimura, F.7
  • 109
    • 84874067867 scopus 로고    scopus 로고
    • A bacterial glycan core linked to surface (S)-layer proteins modulates host immunity through Th17 suppression
    • Settem R.P., Honma K., Nakajima T., Phansopa C., Roy S., Stafford G.P., Sharma A. A bacterial glycan core linked to surface (S)-layer proteins modulates host immunity through Th17 suppression. Mucosal Immunol. 2013, 6:415-426.
    • (2013) Mucosal Immunol. , vol.6 , pp. 415-426
    • Settem, R.P.1    Honma, K.2    Nakajima, T.3    Phansopa, C.4    Roy, S.5    Stafford, G.P.6    Sharma, A.7
  • 110
    • 0034839334 scopus 로고    scopus 로고
    • Glycobiology of surface layer proteins
    • Schäffer C., Messner P. Glycobiology of surface layer proteins. Biochimie 2001, 83:591-599.
    • (2001) Biochimie , vol.83 , pp. 591-599
    • Schäffer, C.1    Messner, P.2
  • 112
    • 77956846877 scopus 로고    scopus 로고
    • S-layer glycoproteins and flagellins: Reporters of archaeal posttranslational modifications
    • Jarrell F., Jones G.M., Kandiba L., Nair D.B., Eichler J. S-layer glycoproteins and flagellins: Reporters of archaeal posttranslational modifications. Archaea 2010, 2010:612948.
    • (2010) Archaea , vol.2010 , pp. 612948
    • Jarrell, F.1    Jones, G.M.2    Kandiba, L.3    Nair, D.B.4    Eichler, J.5
  • 114
    • 84857911456 scopus 로고    scopus 로고
    • Protein glycosylation as an adaptive response in Archaea: Growth at different salt concentrations leads to alterations in Haloferax volcanii S-layer glycoprotein N-glycosylation
    • Guan Z., Naparstek S., Calo D., Eichler J. Protein glycosylation as an adaptive response in Archaea: Growth at different salt concentrations leads to alterations in Haloferax volcanii S-layer glycoprotein N-glycosylation. Environ. Microbiol. 2012, 14:743-753.
    • (2012) Environ. Microbiol. , vol.14 , pp. 743-753
    • Guan, Z.1    Naparstek, S.2    Calo, D.3    Eichler, J.4
  • 115
    • 4444231397 scopus 로고    scopus 로고
    • Surface layer glycoproteins: An example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology
    • Schäffer C., Messner P. Surface layer glycoproteins: An example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology. Glycobiology 2004, 14:31R-42R.
    • (2004) Glycobiology , vol.14
    • Schäffer, C.1    Messner, P.2
  • 117
    • 0021261426 scopus 로고
    • Paracrystalline cell wall surface layers of different Bacillus stearothermophilus strains
    • Messner P., Hollaus F., Sleytr U.B. Paracrystalline cell wall surface layers of different Bacillus stearothermophilus strains. Int. J. Syst. Bacteriol. 1984, 34:202-210.
    • (1984) Int. J. Syst. Bacteriol. , vol.34 , pp. 202-210
    • Messner, P.1    Hollaus, F.2    Sleytr, U.B.3
  • 119
    • 9944226719 scopus 로고    scopus 로고
    • Classification of two isolates from locations in Austria and Yellowstone National Park as Geobacillus tepidamans sp. nov
    • Schäffer C., Franck W.L., Scheberl A., Kosma P., McDermott T.R., Messner P. Classification of two isolates from locations in Austria and Yellowstone National Park as Geobacillus tepidamans sp. nov. Int. J. Syst. Evol. Microbiol. 2004, 54:2361-2368.
    • (2004) Int. J. Syst. Evol. Microbiol. , vol.54 , pp. 2361-2368
    • Schäffer, C.1    Franck, W.L.2    Scheberl, A.3    Kosma, P.4    McDermott, T.R.5    Messner, P.6
  • 120
    • 84864130913 scopus 로고    scopus 로고
    • Taxonomic revision of the genus Geobacillus: emendation of Geobacillus, G. stearothermophilus, G. jurassicus, G. toebii, G. thermodenitrificans and G. thermoglucosidans (nom. corrig., formerly 'thermoglucosidasius')
    • transfer of Bacillus thermantarcticus to the genus as G. thermantarcticus comb. nov.; proposal of Caldibacillus debilis gen. nov., comb. nov.; transfer of G. tepidamans to Anoxybacillus as A. tepidamans comb. nov.; and proposal of Anoxybacillus caldiproteolyticus sp. nov., Int. J. Syst. Evol. Microbiol.
    • A. Coorevits, A. E. Dinsdale, G. Halket, L. Lebbe, P. De Vos, A. van Landschoot, and N. A. Logan. Taxonomic revision of the genus Geobacillus: emendation of Geobacillus, G. stearothermophilus, G. jurassicus, G. toebii, G. thermodenitrificans and G. thermoglucosidans (nom. corrig., formerly 'thermoglucosidasius'); transfer of Bacillus thermantarcticus to the genus as G. thermantarcticus comb. nov.; proposal of Caldibacillus debilis gen. nov., comb. nov.; transfer of G. tepidamans to Anoxybacillus as A. tepidamans comb. nov.; and proposal of Anoxybacillus caldiproteolyticus sp. nov., Int. J. Syst. Evol. Microbiol., 62 (2012) 1470-1485.
    • (2012) , vol.62 , pp. 1470-1485
    • Coorevits, A.1    Dinsdale, A.E.2    Halket, G.3    Lebbe, L.4    De Vos, P.5    van Landschoot, A.6    Logan, N.A.7
  • 125
    • 84862310736 scopus 로고    scopus 로고
    • Synthesis of lipopolysaccharide O-antigens by ABC transporter-dependent pathways
    • Greenfield K., Whitfield C. Synthesis of lipopolysaccharide O-antigens by ABC transporter-dependent pathways. Carbohydr. Res. 2012, 356:12-24.
    • (2012) Carbohydr. Res. , vol.356 , pp. 12-24
    • Greenfield, K.1    Whitfield, C.2
  • 126
    • 33645210489 scopus 로고    scopus 로고
    • Identification and characterization of the genes encoding a unique surface (S-) layer of Tannerella forsythia
    • Lee S.-W., Sabet M., Um H.-S., Yang J., Kim H.C., Zhu W. Identification and characterization of the genes encoding a unique surface (S-) layer of Tannerella forsythia. Gene 2006, 371:102-111.
    • (2006) Gene , vol.371 , pp. 102-111
    • Lee, S.-W.1    Sabet, M.2    Um, H.-S.3    Yang, J.4    Kim, H.C.5    Zhu, W.6
  • 127
    • 64249095086 scopus 로고    scopus 로고
    • A general O-glycosylation system important to the physiology of a major human intestinal symbiont
    • Fletcher M., Coyne M.J., Villa O.F., Chatzidaki-Livanis M., Comstock L.E. A general O-glycosylation system important to the physiology of a major human intestinal symbiont. Cell 2009, 137:321-331.
    • (2009) Cell , vol.137 , pp. 321-331
    • Fletcher, M.1    Coyne, M.J.2    Villa, O.F.3    Chatzidaki-Livanis, M.4    Comstock, L.E.5
  • 129
    • 0002276033 scopus 로고    scopus 로고
    • Surface layer glycoproteins of Bacteria and Archaea
    • Kluwer Academic/Plenum Publishers, New York, R.J. Doyle (Ed.)
    • Messner P., Schäffer C. Surface layer glycoproteins of Bacteria and Archaea. Glycomicrobiology 2000, 93-125. Kluwer Academic/Plenum Publishers, New York. R.J. Doyle (Ed.).
    • (2000) Glycomicrobiology , pp. 93-125
    • Messner, P.1    Schäffer, C.2
  • 130
    • 77952791624 scopus 로고    scopus 로고
    • Protein tyrosine O-glycosylation-Insights into a rather unexplored prokaryotic glycosylation system
    • Zarschler K., Janesch B., Pabst M., Altmann F., Messner P., Schäffer C. Protein tyrosine O-glycosylation-Insights into a rather unexplored prokaryotic glycosylation system. Glycobiology 2010, 20:787-798.
    • (2010) Glycobiology , vol.20 , pp. 787-798
    • Zarschler, K.1    Janesch, B.2    Pabst, M.3    Altmann, F.4    Messner, P.5    Schäffer, C.6
  • 131
    • 0037155265 scopus 로고    scopus 로고
    • The surface layer (S-layer) glycoprotein of Geobacillus stearothermophilus NRS 2004/3a. Analysis of its glycosylation
    • Schäffer C., Wugeditsch T., Kählig H., Scheberl A., Zayni S., Messner P. The surface layer (S-layer) glycoprotein of Geobacillus stearothermophilus NRS 2004/3a. Analysis of its glycosylation. J. Biol. Chem. 2002, 277:6230-6239.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6230-6239
    • Schäffer, C.1    Wugeditsch, T.2    Kählig, H.3    Scheberl, A.4    Zayni, S.5    Messner, P.6
  • 133
    • 0029566235 scopus 로고
    • Glycan structure of a heptose-containing S-layer glycoprotein of Bacillus thermoaerophilus
    • Kosma P., Wugeditsch T., Christian R., Zayni S., Messner P. Glycan structure of a heptose-containing S-layer glycoprotein of Bacillus thermoaerophilus. Glycobiology 1995, 5:791-796.
    • (1995) Glycobiology , vol.5 , pp. 791-796
    • Kosma, P.1    Wugeditsch, T.2    Christian, R.3    Zayni, S.4    Messner, P.5
  • 134
    • 0026019504 scopus 로고
    • Chemical characterization of the regularly arranged surface layer glycoprotein of Bacillus alvei CCM 2051
    • Altman E., Brisson J.-R., Messner P., Sleytr U.B. Chemical characterization of the regularly arranged surface layer glycoprotein of Bacillus alvei CCM 2051. Biochem. Cell Biol. 1991, 69:72-78.
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 72-78
    • Altman, E.1    Brisson, J.-R.2    Messner, P.3    Sleytr, U.B.4
  • 135
    • 0028986366 scopus 로고
    • Similarity of "core" structures in two different glycans of tyrosine-linked eubacterial S-layer glycoproteins
    • Messner P., Christian R., Neuninger C., Schulz G. Similarity of "core" structures in two different glycans of tyrosine-linked eubacterial S-layer glycoproteins. J. Bacteriol. 1995, 177:2188-2193.
    • (1995) J. Bacteriol. , vol.177 , pp. 2188-2193
    • Messner, P.1    Christian, R.2    Neuninger, C.3    Schulz, G.4
  • 136
    • 0028321691 scopus 로고
    • Primary structure of the O-glycosidically linked glycan chain of the crystalline surface layer glycoprotein of Thermoanaerobacter thermohydrosulfuricus L111-69. Galactosyl tyrosine as a novel linkage unit
    • Bock K., Schuster-Kolbe J., Altman E., Allmaier G., Stahl B., Christian R., Sleytr U.B., Messner P. Primary structure of the O-glycosidically linked glycan chain of the crystalline surface layer glycoprotein of Thermoanaerobacter thermohydrosulfuricus L111-69. Galactosyl tyrosine as a novel linkage unit. J. Biol. Chem. 1994, 269:7137-7144.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7137-7144
    • Bock, K.1    Schuster-Kolbe, J.2    Altman, E.3    Allmaier, G.4    Stahl, B.5    Christian, R.6    Sleytr, U.B.7    Messner, P.8
  • 138
    • 0025156038 scopus 로고
    • Chemical characterization of the regularly arranged surface layer glycoprotein of Clostridium thermosaccharolyticum D120-70
    • Altman E., Brisson J.-R., Messner P., Sleytr U.B. Chemical characterization of the regularly arranged surface layer glycoprotein of Clostridium thermosaccharolyticum D120-70. Eur. J. Biochem. 1990, 188:73-82.
    • (1990) Eur. J. Biochem. , vol.188 , pp. 73-82
    • Altman, E.1    Brisson, J.-R.2    Messner, P.3    Sleytr, U.B.4
  • 139
    • 0033865696 scopus 로고    scopus 로고
    • A novel type of carbohydrate-protein linkage region in the tyrosine-bound S-layer glycan of Thermoanaerobacterium thermosaccharolyticum D120-70
    • Schäffer C., Dietrich K., Unger B., Scheberl A., Rainey F.A., Kählig H., Messner P. A novel type of carbohydrate-protein linkage region in the tyrosine-bound S-layer glycan of Thermoanaerobacterium thermosaccharolyticum D120-70. Eur. J. Biochem. 2000, 267:5482-5492.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5482-5492
    • Schäffer, C.1    Dietrich, K.2    Unger, B.3    Scheberl, A.4    Rainey, F.A.5    Kählig, H.6    Messner, P.7
  • 140
    • 0027529226 scopus 로고
    • Complete structure of the tyrosine-linked saccharide moiety from the surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70
    • Christian R., Schulz G., Schuster-Kolbe J., Allmaier G., Schmid E.R., Sleytr U.B., Messner P. Complete structure of the tyrosine-linked saccharide moiety from the surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70. J. Bacteriol. 1993, 175:1250-1256.
    • (1993) J. Bacteriol. , vol.175 , pp. 1250-1256
    • Christian, R.1    Schulz, G.2    Schuster-Kolbe, J.3    Allmaier, G.4    Schmid, E.R.5    Sleytr, U.B.6    Messner, P.7
  • 142
    • 0025649761 scopus 로고
    • Components of bacterial polysaccharides
    • Lindberg B. Components of bacterial polysaccharides. Adv. Carbohydr. Chem. Biochem. 1990, 48:279-318.
    • (1990) Adv. Carbohydr. Chem. Biochem. , vol.48 , pp. 279-318
    • Lindberg, B.1
  • 143
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R., Hermjakob H., Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1999, 1473:4-8.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 145
    • 0026740469 scopus 로고
    • Structure of the glycan chain from the surface layer glycoprotein of Clostridium thermohydrosulfuricus L77-66
    • Altman E., Brisson J.-R., Gagné S.M., Kolbe J., Messner P., Sleytr U.B. Structure of the glycan chain from the surface layer glycoprotein of Clostridium thermohydrosulfuricus L77-66. Biochim. Biophys. Acta 1992, 1117:71-77.
    • (1992) Biochim. Biophys. Acta , vol.1117 , pp. 71-77
    • Altman, E.1    Brisson, J.-R.2    Gagné, S.M.3    Kolbe, J.4    Messner, P.5    Sleytr, U.B.6
  • 146
    • 0028967813 scopus 로고
    • Characterization of the glycan structure of a major glycopeptide from the surface layer glycoprotein of Clostridium thermosaccharolyticum E207-71
    • Altman E., Schäffer C., Brisson J.-R., Messner P. Characterization of the glycan structure of a major glycopeptide from the surface layer glycoprotein of Clostridium thermosaccharolyticum E207-71. Eur. J. Biochem. 1995, 229:308-315.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 308-315
    • Altman, E.1    Schäffer, C.2    Brisson, J.-R.3    Messner, P.4
  • 147
    • 65449158090 scopus 로고    scopus 로고
    • Biochemical and structural analysis of bacterial O-antigen chain length regulator proteins reveals a conserved quaternary structure
    • Larue K., Kimber M.S., Ford R., Whitfield C. Biochemical and structural analysis of bacterial O-antigen chain length regulator proteins reveals a conserved quaternary structure. J. Biol. Chem. 2009, 284:7395-7403.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7395-7403
    • Larue, K.1    Kimber, M.S.2    Ford, R.3    Whitfield, C.4
  • 150
    • 84874113719 scopus 로고    scopus 로고
    • Extreme sweetness: Protein glycosylation in archaea
    • Eichler J. Extreme sweetness: Protein glycosylation in archaea. Nat. Rev. Microbiol. 2013, 11:151-156.
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 151-156
    • Eichler, J.1
  • 152
    • 84863773950 scopus 로고    scopus 로고
    • AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein
    • Kaminski L., Guan Z., Abu-Qarn M., Konrad Z., Eichler J. AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein. Biochim. Biophys. Acta 2012, 1820:1664-1670.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 1664-1670
    • Kaminski, L.1    Guan, Z.2    Abu-Qarn, M.3    Konrad, Z.4    Eichler, J.5
  • 153
    • 84870715118 scopus 로고    scopus 로고
    • AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase
    • Cohen-Rosenzweig C., Yurist-Doutsch S., Eichler J. AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase. J. Bacteriol. 2012, 194:6909-6916.
    • (2012) J. Bacteriol. , vol.194 , pp. 6909-6916
    • Cohen-Rosenzweig, C.1    Yurist-Doutsch, S.2    Eichler, J.3
  • 154
    • 84871985639 scopus 로고    scopus 로고
    • Lipid modification gives rise to two distinct Haloferax volcanii S-layer glycoprotein populations
    • Kandiba L., Guan Z., Eichler J. Lipid modification gives rise to two distinct Haloferax volcanii S-layer glycoprotein populations. Biochim. Biophys. Acta 2013, 1828:938-943.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 938-943
    • Kandiba, L.1    Guan, Z.2    Eichler, J.3
  • 155
    • 79960108098 scopus 로고    scopus 로고
    • Glyco-engineering in Archaea: Differential N-glycosylation of the S-layer glycoprotein in a transformed Haloferax volcanii strain
    • Calo D., Guan Z., Eichler J. Glyco-engineering in Archaea: Differential N-glycosylation of the S-layer glycoprotein in a transformed Haloferax volcanii strain. Microb. Biotechnol. 2011, 4:461-470.
    • (2011) Microb. Biotechnol. , vol.4 , pp. 461-470
    • Calo, D.1    Guan, Z.2    Eichler, J.3
  • 156
    • 20444488776 scopus 로고    scopus 로고
    • Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae
    • Voisin S., Houliston R.S., Kelly J., Brisson J.-R., Watson D., Bardy S.L., Jarrell K.F., Logan S.M. Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae. J. Biol. Chem. 2005, 280:16586-16593.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16586-16593
    • Voisin, S.1    Houliston, R.S.2    Kelly, J.3    Brisson, J.-R.4    Watson, D.5    Bardy, S.L.6    Jarrell, K.F.7    Logan, S.M.8
  • 157
    • 58149483373 scopus 로고    scopus 로고
    • AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltae
    • Chaban B., Logan S.M., Kelly J.F., Jarrell K.F. AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltae. J. Bacteriol. 2009, 191:187-195.
    • (2009) J. Bacteriol. , vol.191 , pp. 187-195
    • Chaban, B.1    Logan, S.M.2    Kelly, J.F.3    Jarrell, K.F.4
  • 158
    • 79958134297 scopus 로고    scopus 로고
    • Biosynthesis and role of N-linked glycosylation in cell surface structures of Archaea with a focus on flagella and S layers
    • Jarrell K.F., Jones G.M., Nair D.B. Biosynthesis and role of N-linked glycosylation in cell surface structures of Archaea with a focus on flagella and S layers. Int. J. Microbiol. 2010, 2010:470138.
    • (2010) Int. J. Microbiol. , vol.2010 , pp. 470138
    • Jarrell, K.F.1    Jones, G.M.2    Nair, D.B.3
  • 159
    • 65349147066 scopus 로고    scopus 로고
    • Identification of genes involved in the assembly and attachment of a novel flagellin N-linked tetrasaccharide important for motility in the archaeon Methanococcus maripaludis
    • VanDyke D.J., Wu J., Logan S.M., Kelly J.F., Mizuno S., Aizawa S.-I., Jarrell K.F. Identification of genes involved in the assembly and attachment of a novel flagellin N-linked tetrasaccharide important for motility in the archaeon Methanococcus maripaludis. Mol. Microbiol. 2009, 72:633-644.
    • (2009) Mol. Microbiol. , vol.72 , pp. 633-644
    • VanDyke, D.J.1    Wu, J.2    Logan, S.M.3    Kelly, J.F.4    Mizuno, S.5    Aizawa, S.-I.6    Jarrell, K.F.7
  • 160
    • 84861398049 scopus 로고    scopus 로고
    • Identification of genes involved in the acetamidino group modification of the flagellin N-linked glycan of Methanococcus maripaludis
    • Jones G.M., Wu J., Ding Y., Uchida K., Aizawa S.-I., Robotham A., Logan S.M., Kelly J., Jarrell K.F. Identification of genes involved in the acetamidino group modification of the flagellin N-linked glycan of Methanococcus maripaludis. J. Bacteriol. 2012, 194:2693-2702.
    • (2012) J. Bacteriol. , vol.194 , pp. 2693-2702
    • Jones, G.M.1    Wu, J.2    Ding, Y.3    Uchida, K.4    Aizawa, S.-I.5    Robotham, A.6    Logan, S.M.7    Kelly, J.8    Jarrell, K.F.9
  • 161
    • 78249283543 scopus 로고    scopus 로고
    • The S-layer glycoprotein of the crenarchaeote Sulfolobus acidocaldarius is glycosylated at multiple sites with chitobiose-linked N-glycans
    • Peyfoon E., Meyer B., Hitchen P.G., Panico M., Morris H.R., Haslam S.M., Albers S.-V., Dell A. The S-layer glycoprotein of the crenarchaeote Sulfolobus acidocaldarius is glycosylated at multiple sites with chitobiose-linked N-glycans. Archaea 2010, 2010:754101.
    • (2010) Archaea , vol.2010 , pp. 754101
    • Peyfoon, E.1    Meyer, B.2    Hitchen, P.G.3    Panico, M.4    Morris, H.R.5    Haslam, S.M.6    Albers, S.-V.7    Dell, A.8
  • 162
    • 0033625671 scopus 로고    scopus 로고
    • 558/566 from the archaeon Sulfolobus acidocaldarius has a unique Asn-linked highly branched hexasaccharide chain containing 6-sulfoquinovose
    • 558/566 from the archaeon Sulfolobus acidocaldarius has a unique Asn-linked highly branched hexasaccharide chain containing 6-sulfoquinovose. Eur. J. Biochem. 2000, 267:4144-4149.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4144-4149
    • Zähringer, U.1    Moll, H.2    Hettmann, T.3    Knirel, Y.A.4    Schäfer, G.5
  • 164
    • 80051795191 scopus 로고    scopus 로고
    • The thermoacidophilic archaeon Sulfolobus acidocaldarius contains an unusually short, highly reduced dolichyl phosphate
    • Guan Z., Meyer B.H., Albers S.-V., Eichler J. The thermoacidophilic archaeon Sulfolobus acidocaldarius contains an unusually short, highly reduced dolichyl phosphate. Biochim. Biophys. Acta 2011, 1811:607-616.
    • (2011) Biochim. Biophys. Acta , vol.1811 , pp. 607-616
    • Guan, Z.1    Meyer, B.H.2    Albers, S.-V.3    Eichler, J.4
  • 165
    • 0034283014 scopus 로고    scopus 로고
    • Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation
    • Mesnage S., Fontaine T., Mignot T., Delepierre M., Mock M., Fouet A. Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation. EMBO J. 2000, 19:4473-4484.
    • (2000) EMBO J. , vol.19 , pp. 4473-4484
    • Mesnage, S.1    Fontaine, T.2    Mignot, T.3    Delepierre, M.4    Mock, M.5    Fouet, A.6
  • 166
    • 0035253107 scopus 로고    scopus 로고
    • Conserved anchoring mechanisms between crystalline cell surface S-layer proteins and secondary cell wall polymers in Gram-positive bacteria
    • Sára M. Conserved anchoring mechanisms between crystalline cell surface S-layer proteins and secondary cell wall polymers in Gram-positive bacteria. Trends Microbiol. 2001, 9:47-49.
    • (2001) Trends Microbiol. , vol.9 , pp. 47-49
    • Sára, M.1
  • 167
    • 15844394070 scopus 로고    scopus 로고
    • The structure of secondary cell wall polymers: How Gram-positive bacteria stick their cell walls together
    • Schäffer C., Messner P. The structure of secondary cell wall polymers: How Gram-positive bacteria stick their cell walls together. Microbiology 2005, 151:643-651.
    • (2005) Microbiology , vol.151 , pp. 643-651
    • Schäffer, C.1    Messner, P.2
  • 169
    • 0025118463 scopus 로고
    • Characterization of Aeromonas salmonicida variants with altered cell surfaces and their use in studying surface protein assembly
    • Griffiths S.G., Lynch W.H. Characterization of Aeromonas salmonicida variants with altered cell surfaces and their use in studying surface protein assembly. Arch. Microbiol. 1990, 154:308-312.
    • (1990) Arch. Microbiol. , vol.154 , pp. 308-312
    • Griffiths, S.G.1    Lynch, W.H.2
  • 170
    • 0002474503 scopus 로고
    • Cell wall structure, synthesis and turnover
    • American Society for Microbiology, Washington, DC, A. Sonenshein, J.A. Hoch, R. Losick (Eds.)
    • Archibald A.R., Hancock I.C., Harwood C.R. Cell wall structure, synthesis and turnover. Bacillus subtilis and Other Gram-Positive Bacteria 1993, 381-410. American Society for Microbiology, Washington, DC. A. Sonenshein, J.A. Hoch, R. Losick (Eds.).
    • (1993) Bacillus subtilis and Other Gram-Positive Bacteria , pp. 381-410
    • Archibald, A.R.1    Hancock, I.C.2    Harwood, C.R.3
  • 171
    • 0013483403 scopus 로고
    • Biosynthesis of the bacterial envelope polymers teichoic acid and teichuronic acid
    • Plenum Press, New York, NY, A.N. Martonosi (Ed.)
    • Hancock I.C., Baddiley J. Biosynthesis of the bacterial envelope polymers teichoic acid and teichuronic acid. The Enzymes of Biological Membranes 1985, Vol. 2:279-307. Plenum Press, New York, NY. 2nd ed. A.N. Martonosi (Ed.).
    • (1985) The Enzymes of Biological Membranes , vol.2 , pp. 279-307
    • Hancock, I.C.1    Baddiley, J.2
  • 172
    • 0024844303 scopus 로고
    • Linkage units in cell walls of Gram-positive bacteria
    • Araki Y., Ito E. Linkage units in cell walls of Gram-positive bacteria. CRC Crit. Rev. Microbiol. 1989, 17:121-135.
    • (1989) CRC Crit. Rev. Microbiol. , vol.17 , pp. 121-135
    • Araki, Y.1    Ito, E.2
  • 174
    • 77956835710 scopus 로고
    • Teichoic acid synthesis in Bacillus subtilis: Genetic organisation and biological roles
    • Elsevier, Amsterdam, J.-M. Ghuysen, R. Hakenbeck (Eds.)
    • Pooley H.M., Karamata D. Teichoic acid synthesis in Bacillus subtilis: Genetic organisation and biological roles. Bacterial Cell Wall 1994, 187-198. Elsevier, Amsterdam. J.-M. Ghuysen, R. Hakenbeck (Eds.).
    • (1994) Bacterial Cell Wall , pp. 187-198
    • Pooley, H.M.1    Karamata, D.2
  • 175
    • 2442511062 scopus 로고    scopus 로고
    • Binding to pyruvylated compounds as an ancestral mechanism to anchor the outer envelope in primitive bacteria
    • Cava F., de Pedro M.A., Schwarz H., Henne A., Berenguer J. Binding to pyruvylated compounds as an ancestral mechanism to anchor the outer envelope in primitive bacteria. Mol. Microbiol. 2004, 52:677-690.
    • (2004) Mol. Microbiol. , vol.52 , pp. 677-690
    • Cava, F.1    de Pedro, M.A.2    Schwarz, H.3    Henne, A.4    Berenguer, J.5
  • 176
    • 84882044752 scopus 로고    scopus 로고
    • Surface layer glycoproteins and secondary cell wall polymers
    • Academic Press-Elsevier, San Diego, CA, A.P. Moran, P.J. Brennan, O. Holst, M. von Itzstein (Eds.)
    • Messner P., Egelseer E.M., Sleytr U.B., Schäffer C. Surface layer glycoproteins and secondary cell wall polymers. Microbial Glycobiology: Structures, Relevance and Applications 2009, 109-128. Academic Press-Elsevier, San Diego, CA. A.P. Moran, P.J. Brennan, O. Holst, M. von Itzstein (Eds.).
    • (2009) Microbial Glycobiology: Structures, Relevance and Applications , pp. 109-128
    • Messner, P.1    Egelseer, E.M.2    Sleytr, U.B.3    Schäffer, C.4
  • 177
    • 0034442553 scopus 로고    scopus 로고
    • A pyrophosphate bridge links the pyruvate-containing secondary cell wall polymer of Paenibacillus alvei CCM 2051 to muramic acid
    • Schäffer C., Müller N., Mandal P.K., Christian R., Zayni S., Messner P. A pyrophosphate bridge links the pyruvate-containing secondary cell wall polymer of Paenibacillus alvei CCM 2051 to muramic acid. Glycoconj. J. 2000, 17:681-690.
    • (2000) Glycoconj. J. , vol.17 , pp. 681-690
    • Schäffer, C.1    Müller, N.2    Mandal, P.K.3    Christian, R.4    Zayni, S.5    Messner, P.6
  • 178
    • 0032786249 scopus 로고    scopus 로고
    • Structural and functional analyses of the secondary cell wall polymer of Bacillus sphaericus CCM 2177 that serves as an S-layer-specific anchor
    • Ilk N., Kosma P., Puchberger M., Egelseer E.M., Mayer H.F., Sleytr U.B., Sára M. Structural and functional analyses of the secondary cell wall polymer of Bacillus sphaericus CCM 2177 that serves as an S-layer-specific anchor. J. Bacteriol. 1999, 181:7643-7646.
    • (1999) J. Bacteriol. , vol.181 , pp. 7643-7646
    • Ilk, N.1    Kosma, P.2    Puchberger, M.3    Egelseer, E.M.4    Mayer, H.F.5    Sleytr, U.B.6    Sára, M.7
  • 179
    • 0342288081 scopus 로고    scopus 로고
    • Isolation and characterization of an amino sugar-rich glycopeptide from the surface layer glycoprotein of Thermoanaerobacterium thermosaccharolyticum E207-71
    • Altman E., Schäffer C., Brisson J.-R., Messner P. Isolation and characterization of an amino sugar-rich glycopeptide from the surface layer glycoprotein of Thermoanaerobacterium thermosaccharolyticum E207-71. Carbohydr. Res. 1996, 295:245-253.
    • (1996) Carbohydr. Res. , vol.295 , pp. 245-253
    • Altman, E.1    Schäffer, C.2    Brisson, J.-R.3    Messner, P.4
  • 180
    • 0023445575 scopus 로고
    • Isolation and structure determination of a diacetamidodideoxyuronic acid-containing glycan chain from the S-layer glycoprotein of Bacillus stearothermophilus NRS 2004/3a
    • Messner P., Sleytr U.B., Christian R., Schulz G., Unger F.M. Isolation and structure determination of a diacetamidodideoxyuronic acid-containing glycan chain from the S-layer glycoprotein of Bacillus stearothermophilus NRS 2004/3a. Carbohydr. Res. 1987, 168:211-218.
    • (1987) Carbohydr. Res. , vol.168 , pp. 211-218
    • Messner, P.1    Sleytr, U.B.2    Christian, R.3    Schulz, G.4    Unger, F.M.5
  • 181
    • 0032799160 scopus 로고    scopus 로고
    • The diacetamidodideoxuronic-acid-containing glycan chain of Bacillus stearothermophilus NRS 2004/3a represents the secondary cell wall polymer of wild-type B. stearothermophilus strains
    • Schäffer C., Kählig H., Christian R., Schulz G., Zayni S., Messner P. The diacetamidodideoxuronic-acid-containing glycan chain of Bacillus stearothermophilus NRS 2004/3a represents the secondary cell wall polymer of wild-type B. stearothermophilus strains. Microbiology 1999, 145:1575-1583.
    • (1999) Microbiology , vol.145 , pp. 1575-1583
    • Schäffer, C.1    Kählig, H.2    Christian, R.3    Schulz, G.4    Zayni, S.5    Messner, P.6
  • 183
    • 43349104162 scopus 로고    scopus 로고
    • Structural characterization of the acid-degraded secondary cell wall polysaccharide of Geobacillus stearothermophilus PV72/p2
    • Corrigendum: Carbohydr. Res., 373 (2013) 52
    • Petersen B.O., Sára M., Mader C., Mayer H.F., Sleytr U.B., Pabst M., Puchberger M., Hofinger A., Duus J.Ø., Kosma P. Structural characterization of the acid-degraded secondary cell wall polysaccharide of Geobacillus stearothermophilus PV72/p2. Carbohydr. Res. 2008, 343:1346-1358. Corrigendum: Carbohydr. Res., 373 (2013) 52.
    • (2008) Carbohydr. Res. , vol.343 , pp. 1346-1358
    • Petersen, B.O.1    Sára, M.2    Mader, C.3    Mayer, H.F.4    Sleytr, U.B.5    Pabst, M.6    Puchberger, M.7    Hofinger, A.8    Duus, J.Ø.9    Kosma, P.10
  • 184
    • 84866342410 scopus 로고    scopus 로고
    • Surface-layer (S-layer) proteins Sap and EA1 govern the binding of the S-layer-associated protein BslO at the cell septa of Bacillus anthracis
    • Kern V.J., Kern J.W., Theriot J.A., Schneewind O., Missiakis D. Surface-layer (S-layer) proteins Sap and EA1 govern the binding of the S-layer-associated protein BslO at the cell septa of Bacillus anthracis. J. Bacteriol. 2012, 194:3833-3840.
    • (2012) J. Bacteriol. , vol.194 , pp. 3833-3840
    • Kern, V.J.1    Kern, J.W.2    Theriot, J.A.3    Schneewind, O.4    Missiakis, D.5
  • 185
    • 77955551189 scopus 로고    scopus 로고
    • Bacillus anthracis surface-layer proteins assemble by binding to the secondary cell wall polysaccharide in a manner that requires csaB and tagO
    • Kern J., Ryan C., Faull K., Schneewind O. Bacillus anthracis surface-layer proteins assemble by binding to the secondary cell wall polysaccharide in a manner that requires csaB and tagO. J. Mol. Biol. 2010, 401:757-775.
    • (2010) J. Mol. Biol. , vol.401 , pp. 757-775
    • Kern, J.1    Ryan, C.2    Faull, K.3    Schneewind, O.4
  • 187
    • 65849118867 scopus 로고    scopus 로고
    • Secondary cell wall polysaccharides of Bacillus anthracis are antigens that contain specific epitopes which cross-react with three pathogenic Bacillus cereus strains that caused severe disease, and other epitopes common to all the Bacillus cereus strains tested
    • Leoff C., Saile E., Rauvolfova J., Quinn C.P., Hoffmaster A., Zhong W., Mehta A.S., Boons G.-J., Carlson R.W., Kannenberg E.L. Secondary cell wall polysaccharides of Bacillus anthracis are antigens that contain specific epitopes which cross-react with three pathogenic Bacillus cereus strains that caused severe disease, and other epitopes common to all the Bacillus cereus strains tested. Glycobiology 2009, 19:665-673.
    • (2009) Glycobiology , vol.19 , pp. 665-673
    • Leoff, C.1    Saile, E.2    Rauvolfova, J.3    Quinn, C.P.4    Hoffmaster, A.5    Zhong, W.6    Mehta, A.S.7    Boons, G.-J.8    Carlson, R.W.9    Kannenberg, E.L.10
  • 188
    • 0037158695 scopus 로고    scopus 로고
    • A bacteriolytic agent that detects and kills Bacillus anthracis
    • Schuch R., Nelson D., Fischetti V.A. A bacteriolytic agent that detects and kills Bacillus anthracis. Nature 2002, 418:884-889.
    • (2002) Nature , vol.418 , pp. 884-889
    • Schuch, R.1    Nelson, D.2    Fischetti, V.A.3
  • 189
    • 84866511605 scopus 로고    scopus 로고
    • Endolysins of Bacillus anthracis bacteriophages recognize unique carbohydrate epitopes of vegetative cell wall polysaccharides with high affinity and selectivity
    • Mo K.-F., Li X., Li H., Low L.Y., Quinn C.P., Boons G.-J. Endolysins of Bacillus anthracis bacteriophages recognize unique carbohydrate epitopes of vegetative cell wall polysaccharides with high affinity and selectivity. J. Am. Chem. Soc. 2012, 134:15556-15562.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15556-15562
    • Mo, K.-F.1    Li, X.2    Li, H.3    Low, L.Y.4    Quinn, C.P.5    Boons, G.-J.6
  • 190
    • 84863209055 scopus 로고    scopus 로고
    • Localization and structural analysis of a conserved pyruvylated epitope in Bacillus anthracis secondary cell wall polysaccharides and characterization of the galactose-deficient wall polysaccharide from avirulent B. anthracis CDC 684
    • Forsberg L.S., Abshire T.G., Friedlander A., Quinn C.P., Kannenberg E.L., Carlson R.W. Localization and structural analysis of a conserved pyruvylated epitope in Bacillus anthracis secondary cell wall polysaccharides and characterization of the galactose-deficient wall polysaccharide from avirulent B. anthracis CDC 684. Glycobiology 2012, 22:1103-1117.
    • (2012) Glycobiology , vol.22 , pp. 1103-1117
    • Forsberg, L.S.1    Abshire, T.G.2    Friedlander, A.3    Quinn, C.P.4    Kannenberg, E.L.5    Carlson, R.W.6
  • 191
    • 79958777474 scopus 로고    scopus 로고
    • Secondary cell wall polysaccharides from Bacillus cereus strains G9241, 03BB87 and 03BB102 causing fatal pneumonia share similar glycosyl structures with polysaccharides from Bacillus anthracis
    • Forsberg L.S., Choudhury B., Leoff C., Marston C.K., Hoffmaster A.R., Saile E., Quinn C.P., Kannenberg E.L., Carlson R.W. Secondary cell wall polysaccharides from Bacillus cereus strains G9241, 03BB87 and 03BB102 causing fatal pneumonia share similar glycosyl structures with polysaccharides from Bacillus anthracis. Glycobiology 2011, 21:934-948.
    • (2011) Glycobiology , vol.21 , pp. 934-948
    • Forsberg, L.S.1    Choudhury, B.2    Leoff, C.3    Marston, C.K.4    Hoffmaster, A.R.5    Saile, E.6    Quinn, C.P.7    Kannenberg, E.L.8    Carlson, R.W.9
  • 192
    • 57649158622 scopus 로고    scopus 로고
    • Structural elucidation of the nonclassical secondary cell wall polysaccharide from Bacillus cereus ATCC 10987
    • Leoff C., Choudhury B., Saile E., Quinn C.P., Carlson R.W., Kannenberg E.L. Structural elucidation of the nonclassical secondary cell wall polysaccharide from Bacillus cereus ATCC 10987. J. Biol. Chem. 2008, 283:29812-29821.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29812-29821
    • Leoff, C.1    Choudhury, B.2    Saile, E.3    Quinn, C.P.4    Carlson, R.W.5    Kannenberg, E.L.6
  • 193
    • 80052419372 scopus 로고    scopus 로고
    • Environmental and bio-film dependent changes in a Bacillus cereus secondary cell wall polysaccharide
    • Candela T., Maes E., Garénaux E., Rombouts Y., Krzewinski F., Gohar M., Guérardel Y. Environmental and bio-film dependent changes in a Bacillus cereus secondary cell wall polysaccharide. J. Biol. Chem. 2011, 286:31250-31262.
    • (2011) J. Biol. Chem. , vol.286 , pp. 31250-31262
    • Candela, T.1    Maes, E.2    Garénaux, E.3    Rombouts, Y.4    Krzewinski, F.5    Gohar, M.6    Guérardel, Y.7
  • 194
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • Navarre W.W., Schneewind O. Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope. Microbiol. Mol. Biol. Rev. 1999, 63:174-229.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 195
    • 0017128465 scopus 로고
    • Self-assembly of the hexagonally and tetragonally arranged subunits of bacterial surface layers and their reattachment to cell walls
    • Sleytr U.B. Self-assembly of the hexagonally and tetragonally arranged subunits of bacterial surface layers and their reattachment to cell walls. J. Ultrastruct. Res. 1976, 55:360-377.
    • (1976) J. Ultrastruct. Res. , vol.55 , pp. 360-377
    • Sleytr, U.B.1
  • 196
    • 0022250181 scopus 로고
    • Reassembly of a regularly arranged protein in the cell wall of Lactobacillus buchneri and its reattachment to cell walls: Chemical modification studies
    • Masuda K., Kawata T. Reassembly of a regularly arranged protein in the cell wall of Lactobacillus buchneri and its reattachment to cell walls: Chemical modification studies. Microbiol. Immunol. 1985, 29:927-938.
    • (1985) Microbiol. Immunol. , vol.29 , pp. 927-938
    • Masuda, K.1    Kawata, T.2
  • 197
    • 0027502582 scopus 로고
    • Organization of a Clostridium thermocellum gene cluster encoding the cellulosomal scaffolding protein CipA and a protein possibly involved in attachment of the cellulosome to the cell surface
    • Fujino T., Béguin P., Aubert J.P. Organization of a Clostridium thermocellum gene cluster encoding the cellulosomal scaffolding protein CipA and a protein possibly involved in attachment of the cellulosome to the cell surface. J. Bacteriol. 1993, 175:1891-1899.
    • (1993) J. Bacteriol. , vol.175 , pp. 1891-1899
    • Fujino, T.1    Béguin, P.2    Aubert, J.P.3
  • 198
    • 0028262129 scopus 로고
    • Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis
    • Lupas A., Engelhardt H., Peters J., Santarius U., Volker S., Baumeister W. Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis. J. Bacteriol. 1994, 176:1224-1233.
    • (1994) J. Bacteriol. , vol.176 , pp. 1224-1233
    • Lupas, A.1    Engelhardt, H.2    Peters, J.3    Santarius, U.4    Volker, S.5    Baumeister, W.6
  • 199
    • 4143139469 scopus 로고    scopus 로고
    • The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides
    • Bayer E.A., Belaich J.-P., Shoham Y., Lamed R. The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides. Annu. Rev. Microbiol. 2004, 58:521-554.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 521-554
    • Bayer, E.A.1    Belaich, J.-P.2    Shoham, Y.3    Lamed, R.4
  • 200
    • 0029967418 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding a large S-layer-associated endoxylanase from Thermoanaerobacterium sp. strain JW/SL-YS 485 in Escherichia coli
    • Liu S.-Y., Gherardini F.C., Matuschek M., Bahl H., Wiegel J. Cloning, sequencing, and expression of the gene encoding a large S-layer-associated endoxylanase from Thermoanaerobacterium sp. strain JW/SL-YS 485 in Escherichia coli. J. Bacteriol. 1996, 178:1539-1547.
    • (1996) J. Bacteriol. , vol.178 , pp. 1539-1547
    • Liu, S.-Y.1    Gherardini, F.C.2    Matuschek, M.3    Bahl, H.4    Wiegel, J.5
  • 201
    • 0030978176 scopus 로고    scopus 로고
    • Molecular characterization of the Bacillus anthracis S-layer component: Evidence that it is the major cell-associated antigen
    • Mesnage S., Tosi-Couture E., Mock M., Gounon P., Fouet A. Molecular characterization of the Bacillus anthracis S-layer component: Evidence that it is the major cell-associated antigen. Mol. Microbiol. 1997, 23:1147-1155.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1147-1155
    • Mesnage, S.1    Tosi-Couture, E.2    Mock, M.3    Gounon, P.4    Fouet, A.5
  • 202
    • 0032824061 scopus 로고    scopus 로고
    • The S-layer homology domain as a means for anchoring heterologous proteins on the cell surface of Bacillus anthracis
    • Mesnage S., Tosi-Couture E., Mock M., Fouet A. The S-layer homology domain as a means for anchoring heterologous proteins on the cell surface of Bacillus anthracis. J. Appl. Microbiol. 1999, 87:256-260.
    • (1999) J. Appl. Microbiol. , vol.87 , pp. 256-260
    • Mesnage, S.1    Tosi-Couture, E.2    Mock, M.3    Fouet, A.4
  • 203
    • 33645965876 scopus 로고    scopus 로고
    • Mutagenesis of conserved charged amino acids in SLH domains of Thermoanaerobacterium thermosulfurigenes EM1 affects attachment to cell wall sacculi
    • May A., Pusztahelyi T., Hoffmann N., Fischer R.J., Bahl H. Mutagenesis of conserved charged amino acids in SLH domains of Thermoanaerobacterium thermosulfurigenes EM1 affects attachment to cell wall sacculi. Arch. Microbiol. 2006, 185:263-269.
    • (2006) Arch. Microbiol. , vol.185 , pp. 263-269
    • May, A.1    Pusztahelyi, T.2    Hoffmann, N.3    Fischer, R.J.4    Bahl, H.5
  • 204
    • 79960383869 scopus 로고    scopus 로고
    • Structure of surface layer homology (SLH) domains from Bacillus anthracis surface array protein
    • Kern J., Wilton R., Zhang R., Binkowski T.A., Joachimiak A., Schneewind O. Structure of surface layer homology (SLH) domains from Bacillus anthracis surface array protein. J. Biol. Chem. 2011, 286:26042-26049.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26042-26049
    • Kern, J.1    Wilton, R.2    Zhang, R.3    Binkowski, T.A.4    Joachimiak, A.5    Schneewind, O.6
  • 205
    • 0031010863 scopus 로고    scopus 로고
    • Evidence for the N-terminal part of the S-layer protein from Bacillus stearothermophilus PV72/p2 recognizes a secondary cell wall polymer
    • Ries W., Hotzy C., Schocher I., Sleytr U.B., Sára M. Evidence for the N-terminal part of the S-layer protein from Bacillus stearothermophilus PV72/p2 recognizes a secondary cell wall polymer. J. Bacteriol. 1997, 179:3892-3898.
    • (1997) J. Bacteriol. , vol.179 , pp. 3892-3898
    • Ries, W.1    Hotzy, C.2    Schocher, I.3    Sleytr, U.B.4    Sára, M.5
  • 206
    • 0032415871 scopus 로고    scopus 로고
    • Identification of two binding domains, one for peptidoglycan and another for a secondary cell wall polymer on the N-terminal part of the S-layer protein SbsB from Bacillus stearothermophilus PV72/p2
    • Sára M., Egelseer E.M., Dekitsch C., Sleytr U.B. Identification of two binding domains, one for peptidoglycan and another for a secondary cell wall polymer on the N-terminal part of the S-layer protein SbsB from Bacillus stearothermophilus PV72/p2. J. Bacteriol. 1998, 180:6780-6783.
    • (1998) J. Bacteriol. , vol.180 , pp. 6780-6783
    • Sára, M.1    Egelseer, E.M.2    Dekitsch, C.3    Sleytr, U.B.4
  • 207
    • 0031038990 scopus 로고    scopus 로고
    • Molecular characterization of the Bacillus stearothermophilus PV72 S-layer gene sbsB induced by oxidative stress
    • Kuen B., Koch A., Asenbauer E., Sára M., Lubitz W. Molecular characterization of the Bacillus stearothermophilus PV72 S-layer gene sbsB induced by oxidative stress. J. Bacteriol. 1997, 179:1664-1670.
    • (1997) J. Bacteriol. , vol.179 , pp. 1664-1670
    • Kuen, B.1    Koch, A.2    Asenbauer, E.3    Sára, M.4    Lubitz, W.5
  • 208
    • 0035847002 scopus 로고    scopus 로고
    • The S-layer protein of Lactobacillus acidophilus ATCC 4356: Identification and characterisation of domains responsible for S-protein assembly and cell wall binding
    • Smit E., Oling F., Demel R., Martinez B., Pouwels P.H. The S-layer protein of Lactobacillus acidophilus ATCC 4356: Identification and characterisation of domains responsible for S-protein assembly and cell wall binding. J. Mol. Biol. 2001, 305:245-257.
    • (2001) J. Mol. Biol. , vol.305 , pp. 245-257
    • Smit, E.1    Oling, F.2    Demel, R.3    Martinez, B.4    Pouwels, P.H.5
  • 209
    • 0036430117 scopus 로고    scopus 로고
    • Domains in the S-layer protein CbsA of Lactobacillus crispatus involved in adherence to collagens, laminin and lipoteichoic acids and in self-assembly
    • Antikainen J., Anton L., Sillanpää L.J., Korhonen T.K. Domains in the S-layer protein CbsA of Lactobacillus crispatus involved in adherence to collagens, laminin and lipoteichoic acids and in self-assembly. Mol. Microbiol. 2002, 46:381-394.
    • (2002) Mol. Microbiol. , vol.46 , pp. 381-394
    • Antikainen, J.1    Anton, L.2    Sillanpää, L.J.3    Korhonen, T.K.4
  • 211
    • 0031941002 scopus 로고    scopus 로고
    • The S-layer proteins of two Bacillus stearothermophilus wild-type strains are bound via their N-terminal region to a secondary cell wall polymer of identical chemical composition
    • Egelseer E., Leitner K., Jarosch M., Hotzy C., Zayni S., Sleytr U.B., Sára M. The S-layer proteins of two Bacillus stearothermophilus wild-type strains are bound via their N-terminal region to a secondary cell wall polymer of identical chemical composition. J. Bacteriol. 1998, 180:1488-1495.
    • (1998) J. Bacteriol. , vol.180 , pp. 1488-1495
    • Egelseer, E.1    Leitner, K.2    Jarosch, M.3    Hotzy, C.4    Zayni, S.5    Sleytr, U.B.6    Sára, M.7
  • 214
    • 0032766054 scopus 로고    scopus 로고
    • Structural heterogeneity in the core oligosaccharide of the S-layer glycoprotein from Aneurinibacillus thermoaerophilus DSM 10155
    • Wugeditsch T., Zachara N.E., Puchberger M., Kosma P., Gooley A.A., Messner P. Structural heterogeneity in the core oligosaccharide of the S-layer glycoprotein from Aneurinibacillus thermoaerophilus DSM 10155. Glycobiology 1999, 9:787-795.
    • (1999) Glycobiology , vol.9 , pp. 787-795
    • Wugeditsch, T.1    Zachara, N.E.2    Puchberger, M.3    Kosma, P.4    Gooley, A.A.5    Messner, P.6
  • 215
    • 0013271569 scopus 로고
    • Carbon-13 nuclear magnetic resonance data for oligosaccharides
    • Bock K., Pedersen C., Pedersen H. Carbon-13 nuclear magnetic resonance data for oligosaccharides. Adv. Carbohydr. Chem. Biochem. 1984, 42:193-225.
    • (1984) Adv. Carbohydr. Chem. Biochem. , vol.42 , pp. 193-225
    • Bock, K.1    Pedersen, C.2    Pedersen, H.3
  • 219
    • 0026594002 scopus 로고
    • Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70
    • Messner P., Christian R., Kolbe J., Schulz G., Sleytr U.B. Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70. J. Bacteriol. 1992, 174:2236-2240.
    • (1992) J. Bacteriol. , vol.174 , pp. 2236-2240
    • Messner, P.1    Christian, R.2    Kolbe, J.3    Schulz, G.4    Sleytr, U.B.5
  • 220
    • 0028931702 scopus 로고
    • Accurate determination of the molecular weight of the major surface layer protein isolated from Clostridium thermosaccharolyticum by time-of-flight mass spectrometry
    • Allmaier G., Schäffer C., Messner P., Rapp U., Mayer-Posner F.J. Accurate determination of the molecular weight of the major surface layer protein isolated from Clostridium thermosaccharolyticum by time-of-flight mass spectrometry. J. Bacteriol. 1995, 177:1402-1404.
    • (1995) J. Bacteriol. , vol.177 , pp. 1402-1404
    • Allmaier, G.1    Schäffer, C.2    Messner, P.3    Rapp, U.4    Mayer-Posner, F.J.5
  • 221
    • 34248203257 scopus 로고    scopus 로고
    • Sequencing of O-glycopeptides derived from a S-layer glycoprotein of Geobacillus stearothermophilus NRS 2004/3a containing up to 51 monosaccharide residues at a single glycosylation site by Fourier transform ion cyclotron resonance infrared multiphoton dissociation mass spectrometry
    • Bindila L., Steiner K., Schäffer C., Messner P., Mormann M., Peter-Katalinić J. Sequencing of O-glycopeptides derived from a S-layer glycoprotein of Geobacillus stearothermophilus NRS 2004/3a containing up to 51 monosaccharide residues at a single glycosylation site by Fourier transform ion cyclotron resonance infrared multiphoton dissociation mass spectrometry. Anal. Chem. 2007, 79:3271-3279.
    • (2007) Anal. Chem. , vol.79 , pp. 3271-3279
    • Bindila, L.1    Steiner, K.2    Schäffer, C.3    Messner, P.4    Mormann, M.5    Peter-Katalinić, J.6
  • 222
    • 34147139297 scopus 로고    scopus 로고
    • Functional characterization of the initiation enzyme of S-layer glycoprotein glycan biosynthesis in Geobacillus stearothermophilus NRS 2004/3a
    • Steiner K., Novotny R., Patel K., Vinogradov E., Whitfield C., Valvano M.A., Messner P., Schäffer C. Functional characterization of the initiation enzyme of S-layer glycoprotein glycan biosynthesis in Geobacillus stearothermophilus NRS 2004/3a. J. Bacteriol. 2007, 189:2590-2598.
    • (2007) J. Bacteriol. , vol.189 , pp. 2590-2598
    • Steiner, K.1    Novotny, R.2    Patel, K.3    Vinogradov, E.4    Whitfield, C.5    Valvano, M.A.6    Messner, P.7    Schäffer, C.8
  • 224
    • 0035894307 scopus 로고    scopus 로고
    • Microscale nonreductive release of O-linked glycans for subsequent analysis through MALDI mass spectrometry and capillary electrophoresis
    • Huang Y., Mechref Y., Novotny M.V. Microscale nonreductive release of O-linked glycans for subsequent analysis through MALDI mass spectrometry and capillary electrophoresis. Anal. Chem. 2001, 73:6063-6069.
    • (2001) Anal. Chem. , vol.73 , pp. 6063-6069
    • Huang, Y.1    Mechref, Y.2    Novotny, M.V.3
  • 225
    • 0020671471 scopus 로고
    • Crystalline surface layers on bacteria
    • Sleytr U.B., Messner P. Crystalline surface layers on bacteria. Annu. Rev. Microbiol. 1983, 37:311-339.
    • (1983) Annu. Rev. Microbiol. , vol.37 , pp. 311-339
    • Sleytr, U.B.1    Messner, P.2
  • 226
    • 1942537159 scopus 로고    scopus 로고
    • S-Layer glycan-specific loci on the chromosome of Geobacillus stearothermophilus NRS 2004/3a and dTDP-l-rhamnose biosynthesis potential of Geobacillus stearothermophilus strains
    • Novotny R., Schäffer C., Strauss J., Messner P. S-Layer glycan-specific loci on the chromosome of Geobacillus stearothermophilus NRS 2004/3a and dTDP-l-rhamnose biosynthesis potential of Geobacillus stearothermophilus strains. Microbiology 2004, 150:953-965.
    • (2004) Microbiology , vol.150 , pp. 953-965
    • Novotny, R.1    Schäffer, C.2    Strauss, J.3    Messner, P.4
  • 228
    • 15844409901 scopus 로고    scopus 로고
    • Genetic organization of chromosomal S-layer glycan biosynthesis loci of Bacillaceae
    • Novotny R., Pföstl A., Messner P., Schäffer C. Genetic organization of chromosomal S-layer glycan biosynthesis loci of Bacillaceae. Glycoconj. J. 2004, 20:435-447.
    • (2004) Glycoconj. J. , vol.20 , pp. 435-447
    • Novotny, R.1    Pföstl, A.2    Messner, P.3    Schäffer, C.4
  • 229
    • 0026593942 scopus 로고
    • Molecular analysis of a Salmonella enterica group E1 rfb gene cluster: O antigen and the genetic basis of the major polymorphism
    • Wang L., Romana L.K., Reeves P.R. Molecular analysis of a Salmonella enterica group E1 rfb gene cluster: O antigen and the genetic basis of the major polymorphism. Genetics 1992, 130:429-443.
    • (1992) Genetics , vol.130 , pp. 429-443
    • Wang, L.1    Romana, L.K.2    Reeves, P.R.3
  • 230
    • 0034877216 scopus 로고    scopus 로고
    • Structural and genetic analyses of O polysaccharide from Actinobacillus actinomycetemcomitans serotype f
    • Kaplan J.B., Perry M.B., MacLean L.L., Furgang D., Wilson M.E., Fine D.H. Structural and genetic analyses of O polysaccharide from Actinobacillus actinomycetemcomitans serotype f. Infect. Immun. 2001, 69:5375-5384.
    • (2001) Infect. Immun. , vol.69 , pp. 5375-5384
    • Kaplan, J.B.1    Perry, M.B.2    MacLean, L.L.3    Furgang, D.4    Wilson, M.E.5    Fine, D.H.6
  • 231
    • 0036322431 scopus 로고    scopus 로고
    • Homologs of the Rml enzymes from Salmonella enterica are responsible for dTDP-β-l-rhamnose biosynthesis in the Gram-positive thermophile Aneurinibacillus thermoaerophilus DSM 10155
    • Graninger M., Kneidinger B., Bruno K., Scheberl A., Messner P. Homologs of the Rml enzymes from Salmonella enterica are responsible for dTDP-β-l-rhamnose biosynthesis in the Gram-positive thermophile Aneurinibacillus thermoaerophilus DSM 10155. Appl. Environ. Microbiol. 2002, 68:3708-3715.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3708-3715
    • Graninger, M.1    Kneidinger, B.2    Bruno, K.3    Scheberl, A.4    Messner, P.5
  • 236
    • 0035038011 scopus 로고    scopus 로고
    • Drug targeting Mycobacterium tuberculosis cell wall synthesis: Genetics of dTDP-rhamnose synthetic enzymes and development of a microtiter plate-based screen for inhibitors of conversion of dTDP-glucose to dTDP-rhamnose
    • Ma Y., Stern R.J., Scherman M.S., Vissa V.D., Yan W., Cox Jones V., Zhang F., Franzblau S.G., Lewis W.H., McNeil M.R. Drug targeting Mycobacterium tuberculosis cell wall synthesis: Genetics of dTDP-rhamnose synthetic enzymes and development of a microtiter plate-based screen for inhibitors of conversion of dTDP-glucose to dTDP-rhamnose. Antimicrob. Agents Chemother. 2001, 45:1407-1416.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1407-1416
    • Ma, Y.1    Stern, R.J.2    Scherman, M.S.3    Vissa, V.D.4    Yan, W.5    Cox Jones, V.6    Zhang, F.7    Franzblau, S.G.8    Lewis, W.H.9    McNeil, M.R.10
  • 238
    • 0031932581 scopus 로고    scopus 로고
    • Synthesis of Escherichia coli O9a polysaccharide requires the participation of two domains of WbdA, a mannosyltransferase encoded within the wb* gene cluster
    • Kido N., Sugiyama T., Yokochi T., Kobayashi H., Okawa Y. Synthesis of Escherichia coli O9a polysaccharide requires the participation of two domains of WbdA, a mannosyltransferase encoded within the wb* gene cluster. Mol. Microbiol. 1998, 27:1213-1221.
    • (1998) Mol. Microbiol. , vol.27 , pp. 1213-1221
    • Kido, N.1    Sugiyama, T.2    Yokochi, T.3    Kobayashi, H.4    Okawa, Y.5
  • 239
    • 4143132365 scopus 로고    scopus 로고
    • Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter
    • Clarke B.R., Cuthbertson L., Whitfield C. Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter. J. Biol. Chem. 2004, 279:35709-35718.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35709-35718
    • Clarke, B.R.1    Cuthbertson, L.2    Whitfield, C.3
  • 241
    • 0029864188 scopus 로고    scopus 로고
    • C-terminal half of Salmonella enterica WbaP (RfbP) is the galactosyl-1-phosphate transferase domain catalyzing the first step of O-antigen synthesis
    • Wang L., Liu D., Reeves P.R. C-terminal half of Salmonella enterica WbaP (RfbP) is the galactosyl-1-phosphate transferase domain catalyzing the first step of O-antigen synthesis. J. Bacteriol. 1996, 178:2598-2604.
    • (1996) J. Bacteriol. , vol.178 , pp. 2598-2604
    • Wang, L.1    Liu, D.2    Reeves, P.R.3
  • 242
    • 77349090654 scopus 로고    scopus 로고
    • Structural basis of substrate binding in WsaF, a rhamnosyltransferase from Geobacillus stearothermophilus
    • Steiner K., Hagelueken G., Messner P., Schäffer C., Naismith J.H. Structural basis of substrate binding in WsaF, a rhamnosyltransferase from Geobacillus stearothermophilus. J. Mol. Biol. 2010, 397:436-447.
    • (2010) J. Mol. Biol. , vol.397 , pp. 436-447
    • Steiner, K.1    Hagelueken, G.2    Messner, P.3    Schäffer, C.4    Naismith, J.H.5
  • 243
    • 0027946244 scopus 로고
    • Identification of an ATP-binding cassette transport system required for translocation of lipopolysaccharide O-antigen side-chains across the cytoplasmic membrane of Klebsiella pneumoniae serotype O1
    • Bronner D., Clarke B.R., Whitfield C. Identification of an ATP-binding cassette transport system required for translocation of lipopolysaccharide O-antigen side-chains across the cytoplasmic membrane of Klebsiella pneumoniae serotype O1. Mol. Microbiol. 1994, 14:505-519.
    • (1994) Mol. Microbiol. , vol.14 , pp. 505-519
    • Bronner, D.1    Clarke, B.R.2    Whitfield, C.3
  • 244
    • 24044542300 scopus 로고    scopus 로고
    • The C-terminal domain of the nucleotide-binding domain protein Wzt determines substrate specificity in the ATP-binding cassette transporter for the lipopolysaccharide O-antigens in Escherichia coli serotypes O8 and O9a
    • Cuthbertson L., Powers J., Whitfield C. The C-terminal domain of the nucleotide-binding domain protein Wzt determines substrate specificity in the ATP-binding cassette transporter for the lipopolysaccharide O-antigens in Escherichia coli serotypes O8 and O9a. J. Biol. Chem. 2005, 280:30310-30319.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30310-30319
    • Cuthbertson, L.1    Powers, J.2    Whitfield, C.3
  • 245
    • 37649017952 scopus 로고    scopus 로고
    • Substrate binding by a bacterial ABC transporter involved in polysaccharide export
    • Cuthbertson L., Kimber M.S., Whitfield C. Substrate binding by a bacterial ABC transporter involved in polysaccharide export. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:19529-19534.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 19529-19534
    • Cuthbertson, L.1    Kimber, M.S.2    Whitfield, C.3
  • 247
    • 77955775676 scopus 로고    scopus 로고
    • Cell surface display of chimeric glycoproteins via the S-layer of Paenibacillus alvei
    • Zarschler K., Janesch B., Kainz B., Ristl R., Messner P., Schäffer C. Cell surface display of chimeric glycoproteins via the S-layer of Paenibacillus alvei. Carbohydr. Res. 2010, 345:1422-1431.
    • (2010) Carbohydr. Res. , vol.345 , pp. 1422-1431
    • Zarschler, K.1    Janesch, B.2    Kainz, B.3    Ristl, R.4    Messner, P.5    Schäffer, C.6
  • 248
    • 27744454625 scopus 로고    scopus 로고
    • The TagB protein in Bacillus subtilis 168 is an intracellular peripheral membrane protein that can incorporate glycerol phosphate onto a membrane-bound acceptor in vitro
    • Bhavsar A.P., Truant R., Brown E.D. The TagB protein in Bacillus subtilis 168 is an intracellular peripheral membrane protein that can incorporate glycerol phosphate onto a membrane-bound acceptor in vitro. J. Biol. Chem. 2005, 280:36691-36700.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36691-36700
    • Bhavsar, A.P.1    Truant, R.2    Brown, E.D.3
  • 250
    • 33645049557 scopus 로고    scopus 로고
    • Protein cell surface display in Gram-positive bacteria: From single protein to macromolecular protein structure
    • Desvaux M., Dumas E., Chafsey I., Hébraud M. Protein cell surface display in Gram-positive bacteria: From single protein to macromolecular protein structure. FEMS Microbiol. Lett. 2006, 256:1-15.
    • (2006) FEMS Microbiol. Lett. , vol.256 , pp. 1-15
    • Desvaux, M.1    Dumas, E.2    Chafsey, I.3    Hébraud, M.4
  • 251
    • 0021939769 scopus 로고
    • Structure of the linkage units between ribitol teichoic acids and peptidoglycan
    • Kojima N., Arakai Y., Ito E. Structure of the linkage units between ribitol teichoic acids and peptidoglycan. J. Bacteriol. 1985, 161:299-306.
    • (1985) J. Bacteriol. , vol.161 , pp. 299-306
    • Kojima, N.1    Arakai, Y.2    Ito, E.3
  • 252
    • 37549030896 scopus 로고    scopus 로고
    • Cell wall carbohydrate compositions of strains from Bacillus cereus group of species correlate with phylogenetic relatedness
    • Leoff C., Saile E., Sue D., Wilkins P.P., Quinn C.P., Carlson R.W., Kannenberg E.L. Cell wall carbohydrate compositions of strains from Bacillus cereus group of species correlate with phylogenetic relatedness. J. Bacteriol. 2008, 190:112-121.
    • (2008) J. Bacteriol. , vol.190 , pp. 112-121
    • Leoff, C.1    Saile, E.2    Sue, D.3    Wilkins, P.P.4    Quinn, C.P.5    Carlson, R.W.6    Kannenberg, E.L.7
  • 253
    • 79953157865 scopus 로고    scopus 로고
    • O-Acetylation of peptidoglycan is required for proper cell separation and S-layer anchoring in Bacillus anthracis
    • Laaberki M.-H., Pfeffer J., Clarke A.J., Dworkin J. O-Acetylation of peptidoglycan is required for proper cell separation and S-layer anchoring in Bacillus anthracis. J. Biol. Chem. 2010, 286:5278-5288.
    • (2010) J. Biol. Chem. , vol.286 , pp. 5278-5288
    • Laaberki, M.-H.1    Pfeffer, J.2    Clarke, A.J.3    Dworkin, J.4
  • 254
    • 84873559319 scopus 로고    scopus 로고
    • Bacillus anthracis acetyl-transferases PatA1 and PatA2 modify the secondary cell wall polysaccharide and affect the assembly of S-layer proteins
    • Lunderberg J.M., Nguyen-Mau S.-M., Richter G.S., Wang Y.-T., Dworkin J., Missiakas D.M., Schneewind O. Bacillus anthracis acetyl-transferases PatA1 and PatA2 modify the secondary cell wall polysaccharide and affect the assembly of S-layer proteins. J. Bacteriol. 2013, 195:977-989.
    • (2013) J. Bacteriol. , vol.195 , pp. 977-989
    • Lunderberg, J.M.1    Nguyen-Mau, S.-M.2    Richter, G.S.3    Wang, Y.-T.4    Dworkin, J.5    Missiakas, D.M.6    Schneewind, O.7
  • 256
    • 34548792373 scopus 로고    scopus 로고
    • Novel biocatalysts based on S-layer self-assembly of Geobacillus stearothermophilus NRS 2004/3a: A nanobiotechnological approach
    • Schäffer C., Novotny R., Küpcü S., Zayni S., Scheberl A., Friedmann J., Sleytr U.B., Messner P. Novel biocatalysts based on S-layer self-assembly of Geobacillus stearothermophilus NRS 2004/3a: A nanobiotechnological approach. Small 2007, 3:1549-1559.
    • (2007) Small , vol.3 , pp. 1549-1559
    • Schäffer, C.1    Novotny, R.2    Küpcü, S.3    Zayni, S.4    Scheberl, A.5    Friedmann, J.6    Sleytr, U.B.7    Messner, P.8
  • 257
    • 55349125699 scopus 로고    scopus 로고
    • Recombinant glycans on an S-layer self-assembly protein: A new dimension for nanopatterned biomaterials
    • Steiner K., Hanreich A., Kainz B., Hitchen P.G., Dell A., Messner P., Schäffer C. Recombinant glycans on an S-layer self-assembly protein: A new dimension for nanopatterned biomaterials. Small 2008, 4:1728-1740.
    • (2008) Small , vol.4 , pp. 1728-1740
    • Steiner, K.1    Hanreich, A.2    Kainz, B.3    Hitchen, P.G.4    Dell, A.5    Messner, P.6    Schäffer, C.7
  • 258
    • 0035179085 scopus 로고    scopus 로고
    • Chemical and biological strategies for engineering cell surface glycosylation
    • Saxon E., Bertozzi C.R. Chemical and biological strategies for engineering cell surface glycosylation. Annu. Rev. Cell Dev. Biol. 2001, 17:1-23.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 1-23
    • Saxon, E.1    Bertozzi, C.R.2
  • 260
    • 79952797070 scopus 로고    scopus 로고
    • Theoretical and experimental characterization of the scope of protein O-glycosylation in Bacteroides fragilis
    • Fletcher C.M., Coyne M.J., Comstock L.E. Theoretical and experimental characterization of the scope of protein O-glycosylation in Bacteroides fragilis. J. Biol. Chem. 2011, 286:3219-3226.
    • (2011) J. Biol. Chem. , vol.286 , pp. 3219-3226
    • Fletcher, C.M.1    Coyne, M.J.2    Comstock, L.E.3
  • 263
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp S., Mimura Y., Jefferis R., Huber R., Sondermann P. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J. Mol. Biol. 2003, 325:979-989.
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 264
    • 0035081693 scopus 로고    scopus 로고
    • The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: Properties of a series of truncated glycoforms
    • Mimura Y., Church S., Ghirlando R., Ashton P.R., Dong S., Goodall M., Lund J., Jefferis R. The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: Properties of a series of truncated glycoforms. Mol. Immunol. 2000, 37:697-706.
    • (2000) Mol. Immunol. , vol.37 , pp. 697-706
    • Mimura, Y.1    Church, S.2    Ghirlando, R.3    Ashton, P.R.4    Dong, S.5    Goodall, M.6    Lund, J.7    Jefferis, R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.