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Volumn 12, Issue 3, 2014, Pages 211-222

Biogenesis and functions of bacterial S-layers

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALS; ARCHAEA; BACTERIA; CELL WALL; GENETIC VARIATION; HUMANS; MEMBRANE GLYCOPROTEINS; MODELS, BIOLOGICAL; MULTIGENE FAMILY; PROTEIN STRUCTURE, TERTIARY;

EID: 84894065666     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro3213     Document Type: Review
Times cited : (260)

References (121)
  • 1
    • 0033984760 scopus 로고    scopus 로고
    • S-layer proteins
    • Sara, M. & Sleytr, U. B. S-layer proteins. J. Bacteriol. 182, 859-868 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 859-868
    • Sara, M.1    Sleytr, U.B.2
  • 4
    • 0017135609 scopus 로고
    • Ultrastructure of the cell walls of two closely related Clostridia that possess different regular arrays of surface subunits
    • Sleytr, U. B. & Glauert, A. M. Ultrastructure of the cell walls of two closely related Clostridia that possess different regular arrays of surface subunits. J. Bacteriol. 126, 869-882 (1976).
    • (1976) J. Bacteriol. , vol.126 , pp. 869-882
    • Sleytr, U.B.1    Glauert, A.M.2
  • 5
    • 33846273815 scopus 로고    scopus 로고
    • S-layers as a tool kit for nanobiotechnological applications
    • Sleytr, U. B. et al. S-layers as a tool kit for nanobiotechnological applications. FEMS Microbiol. Lett. 267, 131-144 (2007).
    • (2007) FEMS Microbiol. Lett. , vol.267 , pp. 131-144
    • Sleytr, U.B.1
  • 6
    • 84877117946 scopus 로고    scopus 로고
    • Nanotechnology with S-layer proteins
    • Schuster, B. & Sleytr, U. B. Nanotechnology with S-layer proteins. Methods Mol. Biol. 996, 153-175 (2013).
    • (2013) Methods Mol. Biol. , vol.996 , pp. 153-175
    • Schuster, B.1    Sleytr, U.B.2
  • 7
    • 0037673494 scopus 로고    scopus 로고
    • Structure and genotypic plasticity of the Campylobacter fetus sap locus
    • Tu, Z. C., Wassenaar, T. M., Thompson, S. A. & Blaser, M. J. Structure and genotypic plasticity of the Campylobacter fetus sap locus. Mol. Microbiol. 48, 685-698 (2003).
    • (2003) Mol. Microbiol. , vol.48 , pp. 685-698
    • Tu, Z.C.1    Wassenaar, T.M.2    Thompson, S.A.3    Blaser, M.J.4
  • 8
    • 0031028714 scopus 로고    scopus 로고
    • Nested DNA inversion as a paradigm of programmed gene rearrangement
    • Dworkin, J. & Blaser, M. J. Nested DNA inversion as a paradigm of programmed gene rearrangement. Proc. Natl Acad. Sci. USA 94, 985-990 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 985-990
    • Dworkin, J.1    Blaser, M.J.2
  • 9
    • 0027240586 scopus 로고
    • Rearrangement of sapA homologs with conserved and variable regions in Campylobacter fetus
    • Tummuru, M. K. & Blaser, M. J. Rearrangement of sapA homologs with conserved and variable regions in Campylobacter fetus. Proc. Natl Acad. Sci. USA 90, 7265-7269 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7265-7269
    • Tummuru, M.K.1    Blaser, M.J.2
  • 10
    • 0029030845 scopus 로고
    • Segmental conservation of sapA sequences in type B Campylobacter fetus cells
    • Dworkin, J., Tummuru, M. K. & Blaser, M. J. Segmental conservation of sapA sequences in type B Campylobacter fetus cells. J. Biol. Chem. 270, 15093-15101 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 15093-15101
    • Dworkin, J.1    Tummuru, M.K.2    Blaser, M.J.3
  • 11
    • 29744441162 scopus 로고    scopus 로고
    • Sequence and phylogenetic analysis of the gene for surface layer protein, slpA, from 14 PCR ribotypes of Clostridium difficile
    • Eidhin, D., Ryan, A., Doyle, R., Walsh, J. B. & Kelleher, D. Sequence and phylogenetic analysis of the gene for surface layer protein, slpA, from 14 PCR ribotypes of Clostridium difficile. J. Med. Microbiol. 55, 69-83 (2006).
    • (2006) J. Med. Microbiol. , vol.55 , pp. 69-83
    • Eidhin, D.1    Ryan, A.2    Doyle, R.3    Walsh, J.B.4    Kelleher, D.5
  • 12
    • 0036302998 scopus 로고    scopus 로고
    • Patterns of sequence conservation in the S-layer proteins and related sequences in Clostridium difficile
    • Calabi, E. & Fairweather, N. Patterns of sequence conservation in the S-layer proteins and related sequences in Clostridium difficile. J. Bacteriol. 184, 3886-3897 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 3886-3897
    • Calabi, E.1    Fairweather, N.2
  • 13
    • 84876072545 scopus 로고    scopus 로고
    • Recombinational switching of the Clostridium difficile S-layer and a novel glycosylation gene cluster revealed by large-scale whole-genome sequencing
    • Dingle, K. E. et al. Recombinational switching of the Clostridium difficile S-layer and a novel glycosylation gene cluster revealed by large-scale whole-genome sequencing. J. Infect. Dis. 207, 675-686 (2013).
    • (2013) J. Infect. Dis. , vol.207 , pp. 675-686
    • Dingle, K.E.1
  • 14
    • 70350376366 scopus 로고    scopus 로고
    • A novel genetic switch controls phase variable expression of CwpV, a Clostridium difficile cell wall protein
    • Emerson, J. et al. A novel genetic switch controls phase variable expression of CwpV, a Clostridium difficile cell wall protein. Mol. Microbiol. 74, 541-556 (2009).
    • (2009) Mol. Microbiol. , vol.74 , pp. 541-556
    • Emerson, J.1
  • 15
    • 79955766239 scopus 로고    scopus 로고
    • The Clostridium difficile cell wall protein CwpV is antigenically variable between strains, but exhibits conserved aggregation-promoting function
    • Reynolds, C. B., Emerson, J. E., de la Riva, L., Fagan, R. P. & Fairweather, N. F. The Clostridium difficile cell wall protein CwpV is antigenically variable between strains, but exhibits conserved aggregation-promoting function. PLoS Pathog. 7, e1002024 (2011).
    • (2011) PLoS Pathog. , vol.7
    • Reynolds, C.B.1    Emerson, J.E.2    De La Riva, L.3    Fagan, R.P.4    Fairweather, N.F.5
  • 16
    • 41049113518 scopus 로고    scopus 로고
    • BslA a pXO1-encoded adhesin of Bacillus anthracis
    • Kern, J. W. & Schneewind, O. BslA, a pXO1-encoded adhesin of Bacillus anthracis. Mol. Microbiol. 68, 504-515 (2008).
    • (2008) Mol. Microbiol. , vol.68 , pp. 504-515
    • Kern, J.W.1    Schneewind, O.2
  • 17
    • 0036267952 scopus 로고    scopus 로고
    • Developmental switch of S-layer protein synthesis in Bacillus anthracis
    • Mignot, T., Mesnage, S., Couture-Tosi, E., Mock, M. & Fouet, A. Developmental switch of S-layer protein synthesis in Bacillus anthracis. Mol. Microbiol. 43, 1615-1627 (2002).
    • (2002) Mol. Microbiol. , vol.43 , pp. 1615-1627
    • Mignot, T.1    Mesnage, S.2    Couture-Tosi, E.3    Mock, M.4    Fouet, A.5
  • 18
    • 84873020808 scopus 로고    scopus 로고
    • Bacillus cereus G9241 S-layer assembly contributes to the pathogenesis of anthrax-like disease in mice
    • Wang, Y. T., Oh, S. Y., Hendrickx, A. P., Lunderberg, J. M. & Schneewind, O. Bacillus cereus G9241 S-layer assembly contributes to the pathogenesis of anthrax-like disease in mice. J. Bacteriol. 195, 596-605 (2012).
    • (2012) J. Bacteriol. , vol.195 , pp. 596-605
    • Wang, Y.T.1    Oh, S.Y.2    Hendrickx, A.P.3    Lunderberg, J.M.4    Schneewind, O.5
  • 19
    • 79960394068 scopus 로고    scopus 로고
    • A proposed nomenclature for cell wall proteins of Clostridium difficile
    • Fagan, R. P. et al. A proposed nomenclature for cell wall proteins of Clostridium difficile. J. Med. Microbiol. 60, 1225-1228 (2011).
    • (2011) J. Med. Microbiol. , vol.60 , pp. 1225-1228
    • Fagan, R.P.1
  • 20
    • 0037418012 scopus 로고    scopus 로고
    • The genome sequence of Clostridium tetani, the causative agent of tetanus disease
    • Bruggemann, H. et al. The genome sequence of Clostridium tetani, the causative agent of tetanus disease. Proc. Natl Acad. Sci. USA 100, 1316-1321 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1316-1321
    • Bruggemann, H.1
  • 21
    • 34347395377 scopus 로고    scopus 로고
    • Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes
    • Sebaihia, M. et al. Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes. Genome Res. 17, 1082-1092 (2007).
    • (2007) Genome Res. , vol.17 , pp. 1082-1092
    • Sebaihia, M.1
  • 22
    • 0031748720 scopus 로고    scopus 로고
    • The Caulobacter crescentus paracrystalline S-layer protein is secreted by an ABC transporter (type I) secretion apparatus
    • Awram, P. & Smit, J. The Caulobacter crescentus paracrystalline S-layer protein is secreted by an ABC transporter (type I) secretion apparatus. J. Bacteriol. 180, 3062-3069 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 3062-3069
    • Awram, P.1    Smit, J.2
  • 23
    • 0031780199 scopus 로고    scopus 로고
    • Serratia marcescens S-layer protein is secreted extracellularly via an ATP-binding cassette exporter, the Lip system
    • Kawai, E., Akatsuka, H., Idei, A., Shibatani, T. & Omori, K. Serratia marcescens S-layer protein is secreted extracellularly via an ATP-binding cassette exporter, the Lip system. Mol. Microbiol. 27, 941-952 (1998).
    • (1998) Mol. Microbiol. , vol.27 , pp. 941-952
    • Kawai, E.1    Akatsuka, H.2    Idei, A.3    Shibatani, T.4    Omori, K.5
  • 24
    • 0032425549 scopus 로고    scopus 로고
    • Campylobacter fetus surface layer proteins are transported by a type i secretion system
    • Thompson, S. A. et al. Campylobacter fetus surface layer proteins are transported by a type I secretion system. J. Bacteriol. 180, 6450-6458 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 6450-6458
    • Thompson, S.A.1
  • 25
    • 0029047349 scopus 로고
    • Molecular analysis of an A-protein secretion mutant of Aeromonas salmonicida reveals a surface layer-specific protein secretion pathway
    • Noonan, B. & Trust, T. J. Molecular analysis of an A-protein secretion mutant of Aeromonas salmonicida reveals a surface layer-specific protein secretion pathway. J. Mol. Biol. 248, 316-327 (1995).
    • (1995) J. Mol. Biol. , vol.248 , pp. 316-327
    • Noonan, B.1    Trust, T.J.2
  • 26
    • 0029076831 scopus 로고
    • A specific PulD homolog is required for the secretion of paracrystalline surface array subunits in Aeromonas hydrophila
    • Thomas, S. R. & Trust, T. J. A specific PulD homolog is required for the secretion of paracrystalline surface array subunits in Aeromonas hydrophila. J. Bacteriol. 177, 3932-3939 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 3932-3939
    • Thomas, S.R.1    Trust, T.J.2
  • 28
    • 79961004324 scopus 로고    scopus 로고
    • Clostridium difficile has two parallel and essential Sec secretion systems
    • Fagan, R. P. & Fairweather, N. F. Clostridium difficile has two parallel and essential Sec secretion systems. J. Biol. Chem. 286, 27483-27493 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 27483-27493
    • Fagan, R.P.1    Fairweather, N.F.2
  • 29
    • 0035212925 scopus 로고    scopus 로고
    • Two nonredundant SecA homologues function in Mycobacteria
    • Braunstein, M., Brown, A. M., Kurtz, S. & Jacobs, W. R. Jr. Two nonredundant SecA homologues function in Mycobacteria. J. Bacteriol. 183, 6979-6990 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 6979-6990
    • Braunstein, M.1    Brown, A.M.2    Kurtz, S.3    Jacobs Jr., W.R.4
  • 30
    • 84867893593 scopus 로고    scopus 로고
    • Emerging themes in SecA2-mediated protein export
    • Feltcher, M. E. & Braunstein, M. Emerging themes in SecA2-mediated protein export. Nature Rev. Microbiol. 10, 779-789 (2012).
    • (2012) Nature Rev. Microbiol. , vol.10 , pp. 779-789
    • Feltcher, M.E.1    Braunstein, M.2
  • 31
    • 0034965222 scopus 로고    scopus 로고
    • Identification of lipopolysaccharide O antigen synthesis genes required for attachment of the S-layer of Caulobacter crescentus
    • Awram, P. & Smit, J. Identification of lipopolysaccharide O antigen synthesis genes required for attachment of the S-layer of Caulobacter crescentus. Microbiology 147, 1451-1460 (2001).
    • (2001) Microbiology , vol.147 , pp. 1451-1460
    • Awram, P.1    Smit, J.2
  • 32
    • 33947130584 scopus 로고    scopus 로고
    • S-layer anchoring and localization of an S-layer-associated protease in Caulobacter crescentus
    • Ford, M. J., Nomellini, J. F. & Smit, J. S-layer anchoring and localization of an S-layer-associated protease in Caulobacter crescentus. J. Bacteriol. 189, 2226-2237 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 2226-2237
    • Ford, M.J.1    Nomellini, J.F.2    Smit, J.3
  • 33
    • 0026565859 scopus 로고
    • Reattachment of surface array proteins to Campylobacter fetus cells
    • Yang, L. Y., Pei, Z. H., Fujimoto, S. & Blaser, M. J. Reattachment of surface array proteins to Campylobacter fetus cells. J. Bacteriol. 174, 1258-1267 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 1258-1267
    • Yang, L.Y.1    Pei, Z.H.2    Fujimoto, S.3    Blaser, M.J.4
  • 34
    • 0028946548 scopus 로고
    • A lipopolysaccharide-binding domain of the Campylobacter fetus S-layer protein resides within the conserved N terminus of a family of silent and divergent homologs
    • Dworkin, J., Tummuru, M. K. & Blaser, M. J. A lipopolysaccharide- binding domain of the Campylobacter fetus S-layer protein resides within the conserved N terminus of a family of silent and divergent homologs. J. Bacteriol. 177, 1734-1741 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 1734-1741
    • Dworkin, J.1    Tummuru, M.K.2    Blaser, M.J.3
  • 35
    • 0025248414 scopus 로고
    • Conserved structures of cell wall protein genes among protein-producing Bacillus brevis strains
    • Ebisu, S. et al. Conserved structures of cell wall protein genes among protein-producing Bacillus brevis strains. J. Bacteriol. 172, 1312-1320 (1990).
    • (1990) J. Bacteriol. , vol.172 , pp. 1312-1320
    • Ebisu, S.1
  • 36
    • 0024720358 scopus 로고
    • Cloning and sequencing of the gene encoding a 125-kilodalton surface-layer protein from Bacillus sphaericus 2362 and of a related cryptic gene
    • Bowditch, R. D., Baumann, P. & Yousten, A. A. Cloning and sequencing of the gene encoding a 125-kilodalton surface-layer protein from Bacillus sphaericus 2362 and of a related cryptic gene. J. Bacteriol. 171, 4178-4188 (1989).
    • (1989) J. Bacteriol. , vol.171 , pp. 4178-4188
    • Bowditch, R.D.1    Baumann, P.2    Yousten, A.A.3
  • 37
    • 0026539739 scopus 로고
    • Sequence of the S-layer gene of Thermus thermophilus HB8 and functionality of its promoter in Escherichia coli
    • Faraldo, M. M., de Pedro, M. A. & Berenguer, J. Sequence of the S-layer gene of Thermus thermophilus HB8 and functionality of its promoter in Escherichia coli. J. Bacteriol. 174, 7458-7462 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 7458-7462
    • Faraldo, M.M.1    De Pedro, M.A.2    Berenguer, J.3
  • 38
    • 0028337633 scopus 로고
    • Sequence analysis of the sbsA gene encoding the 130-kDa surface-layer protein of Bacillus stearothermophilus strain PV72
    • Kuen, B., Sleytr, U. B. & Lubitz, W. Sequence analysis of the sbsA gene encoding the 130-kDa surface-layer protein of Bacillus stearothermophilus strain PV72. Gene 145, 115-120 (1994).
    • (1994) Gene , vol.145 , pp. 115-120
    • Kuen, B.1    Sleytr, U.B.2    Lubitz, W.3
  • 39
    • 0031983981 scopus 로고    scopus 로고
    • Identification of a region responsible for binding to the cell wall within the S-layer protein of Clostridium thermocellum
    • Lemaire, M., Miras, I., Gounon, P. & Beguin, P. Identification of a region responsible for binding to the cell wall within the S-layer protein of Clostridium thermocellum. Microbiology 144, 211-217 (1998).
    • (1998) Microbiology , vol.144 , pp. 211-217
    • Lemaire, M.1    Miras, I.2    Gounon, P.3    Beguin, P.4
  • 40
    • 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. et al. Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation. EMBO J. 19, 4473-4484 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4473-4484
    • Mesnage, S.1
  • 41
    • 0028966264 scopus 로고
    • Characterization of the Bacillus anthracis S-layer: Cloning and sequencing of the structural gene
    • Etienne-Toumelin, I., Sirard, J. C., Duflot, E., Mock, M. & Fouet, A. Characterization of the Bacillus anthracis S-layer: cloning and sequencing of the structural gene. J. Bacteriol. 177, 614-620 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 614-620
    • Etienne-Toumelin, I.1    Sirard, J.C.2    Duflot, E.3    Mock, M.4    Fouet, A.5
  • 42
    • 0030978176 scopus 로고    scopus 로고
    • Molecular characterization of the Bacillus anthracis main 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 main S-layer component: evidence that it is the major cell-associated antigen. Mol. Microbiol. 23, 1147-1155 (1997).
    • (1997) Mol. Microbiol. , vol.23 , pp. 1147-1155
    • Mesnage, S.1    Tosi-Couture, E.2    Mock, M.3    Gounon, P.4    Fouet, A.5
  • 43
    • 79960383869 scopus 로고    scopus 로고
    • Structure of the SLH domains from Bacillus anthracis surface array protein
    • Kern, J. et al. Structure of the SLH domains from Bacillus anthracis surface array protein. J. Biol. Chem. 286, 26042-26049 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 26042-26049
    • Kern, J.1
  • 44
    • 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
    • Sara, M. et al. 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. 178, 2108-2117 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 2108-2117
    • Sara, M.1
  • 45
    • 0033975875 scopus 로고    scopus 로고
    • S-layer gene sbsC of Bacillus stearothermophilus ATCC 12980: Molecular characterization and heterologous expression in Escherichia coli
    • Jarosch, M., Egelseer, E. M., Mattanovich, D., Sleytr, U. B. & Sara, M. S-layer gene sbsC of Bacillus stearothermophilus ATCC 12980: molecular characterization and heterologous expression in Escherichia coli. Microbiology 146, 273-281 (2000).
    • (2000) Microbiology , vol.146 , pp. 273-281
    • Jarosch, M.1    Egelseer, E.M.2    Mattanovich, D.3    Sleytr, U.B.4    Sara, M.5
  • 46
    • 0036136957 scopus 로고    scopus 로고
    • Characterization of an S-layer glycoprotein produced in the course of S-layer variation of Bacillus stearothermophilus ATCC 12980 and sequencing and cloning of the sbsD gene encoding the protein moiety
    • Egelseer, E. M. et al. Characterization of an S-layer glycoprotein produced in the course of S-layer variation of Bacillus stearothermophilus ATCC 12980 and sequencing and cloning of the sbsD gene encoding the protein moiety. Arch. Microbiol. 177, 70-80 (2001).
    • (2001) Arch. Microbiol. , vol.177 , pp. 70-80
    • Egelseer, E.M.1
  • 47
    • 0037155265 scopus 로고    scopus 로고
    • The surface layer (S-layer) glycoprotein of Geobacillus stearothermophilus NRS 2004/3a. Analysis of its glycosylation
    • Schaffer, C. et al. The surface layer (S-layer) glycoprotein of Geobacillus stearothermophilus NRS 2004/3a. Analysis of its glycosylation. J. Biol. Chem. 277, 6230-6239 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 6230-6239
    • Schaffer, C.1
  • 48
    • 1542346915 scopus 로고    scopus 로고
    • Interaction of the crystalline bacterial cell surface layer protein SbsB and the secondary cell wall polymer of Geobacillus stearothermophilus PV72 assessed by real-time surface plasmon resonance biosensor technology
    • Mader, C., Huber, C., Moll, D., Sleytr, U. B. & Sara, M. Interaction of the crystalline bacterial cell surface layer protein SbsB and the secondary cell wall polymer of Geobacillus stearothermophilus PV72 assessed by real-time surface plasmon resonance biosensor technology. J. Bacteriol. 186, 1758-1768 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 1758-1768
    • Mader, C.1    Huber, C.2    Moll, D.3    Sleytr, U.B.4    Sara, M.5
  • 49
    • 0032799160 scopus 로고    scopus 로고
    • The diacetamidodideoxyuronic-acid-containing glycan chain of Bacillus stearothermophilus NRS 2004/3a represents the secondary cell-wall polymer of wild-type B. Stearothermophilus strains
    • Schaffer, C. et al. The diacetamidodideoxyuronic-acid-containing glycan chain of Bacillus stearothermophilus NRS 2004/3a represents the secondary cell-wall polymer of wild-type B. stearothermophilus strains. Microbiology 145, 1575-1583 (1999).
    • (1999) Microbiology , vol.145 , pp. 1575-1583
    • Schaffer, C.1
  • 50
    • 34948870365 scopus 로고    scopus 로고
    • High-affinity interaction between the S-layer protein SbsC and the secondary cell wall polymer of Geobacillus stearothermophilus ATCC 12980 determined by surface plasmon resonance technology
    • Ferner-Ortner, J., Mader, C., Ilk, N., Sleytr, U. B. & Egelseer, E. M. High-affinity interaction between the S-layer protein SbsC and the secondary cell wall polymer of Geobacillus stearothermophilus ATCC 12980 determined by surface plasmon resonance technology. J. Bacteriol. 189, 7154-7158 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 7154-7158
    • Ferner-Ortner, J.1    Mader, C.2    Ilk, N.3    Sleytr, U.B.4    Egelseer, E.M.5
  • 51
    • 0026694316 scopus 로고
    • Molecular cloning and sequencing of the upstream region of the major Bacillus subtilis autolysin gene: A modifier protein exhibiting sequence homology to the major autolysin and the spoIID product
    • Kuroda, A., Rashid, M. H. & Sekiguchi, J. Molecular cloning and sequencing of the upstream region of the major Bacillus subtilis autolysin gene: a modifier protein exhibiting sequence homology to the major autolysin and the spoIID product. J. Gen. Microbiol. 138, 1067-1076 (1992).
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1067-1076
    • Kuroda, A.1    Rashid, M.H.2    Sekiguchi, J.3
  • 52
    • 0025011966 scopus 로고
    • Cloning sequencing and genetic mapping of a Bacillus subtilis cell wall hydrolase gene
    • Kuroda, A. & Sekiguchi, J. Cloning, sequencing and genetic mapping of a Bacillus subtilis cell wall hydrolase gene. J. Gen. Microbiol. 136, 2209-2216 (1990).
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 2209-2216
    • Kuroda, A.1    Sekiguchi, J.2
  • 53
    • 41349086881 scopus 로고    scopus 로고
    • Comparative genomics of Clostridia: Link between the ecological niche and cell surface properties
    • Bruggemann, H. & Gottschalk, G. Comparative genomics of Clostridia: link between the ecological niche and cell surface properties. Ann. NY Acad. Sci. 1125, 73-81 (2008).
    • (2008) Ann. NY Acad. Sci. , vol.1125 , pp. 73-81
    • Bruggemann, H.1    Gottschalk, G.2
  • 54
    • 40949089662 scopus 로고    scopus 로고
    • Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions
    • Weidenmaier, C. & Peschel, A. Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions. Nature Rev. Microbiol. 6, 276-287 (2008).
    • (2008) Nature Rev. Microbiol. , vol.6 , pp. 276-287
    • Weidenmaier, C.1    Peschel, A.2
  • 55
    • 48149095082 scopus 로고    scopus 로고
    • The structure and binding behavior of the bacterial cell surface layer protein SbsC
    • Pavkov, T. et al. The structure and binding behavior of the bacterial cell surface layer protein SbsC. Structure 16, 1226-1237 (2008).
    • (2008) Structure , vol.16 , pp. 1226-1237
    • Pavkov, T.1
  • 56
    • 1242339692 scopus 로고    scopus 로고
    • Biophysical characterization of the entire bacterial surface layer protein SbsB and its two distinct functional domains
    • Runzler, D., Huber, C., Moll, D., Kohler, G. & Sara, M. Biophysical characterization of the entire bacterial surface layer protein SbsB and its two distinct functional domains. J Biol Chem, 7, 5207-5215 (2003).
    • (2003) J Biol Chem , vol.7 , pp. 5207-5215
    • Runzler, D.1    Huber, C.2    Moll, D.3    Kohler, G.4    Sara, M.5
  • 57
    • 0035212204 scopus 로고    scopus 로고
    • Distribution of S-layers on the surface of Bacillus cereus strains: Phylogenetic origin and ecological pressure
    • Mignot, T. et al. Distribution of S-layers on the surface of Bacillus cereus strains: phylogenetic origin and ecological pressure. Environ. Microbiol. 3, 493-501 (2001).
    • (2001) Environ. Microbiol. , vol.3 , pp. 493-501
    • Mignot, T.1
  • 58
    • 84863497306 scopus 로고    scopus 로고
    • 2+ triggered S-layer assembly
    • Baranova, E. et al. SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly. Nature 487, 119-122 (2012).
    • (2012) Nature , vol.487 , pp. 119-122
    • Baranova, E.1
  • 59
    • 0016123083 scopus 로고
    • Protein and carbohydrate composition of the cell envelope of Halobacterium salinarium
    • Mescher, M. F., Strominger, J. L. & Watson, S. W. Protein and carbohydrate composition of the cell envelope of Halobacterium salinarium. J. Bacteriol. 120, 945-954 (1974).
    • (1974) J. Bacteriol. , vol.120 , pp. 945-954
    • Mescher, M.F.1    Strominger, J.L.2    Watson, S.W.3
  • 60
    • 80052285877 scopus 로고    scopus 로고
    • The S-layer glycome-adding to the sugar coat of bacteria
    • Ristl, R. et al. The S-layer glycome-adding to the sugar coat of bacteria. Int J. Microbiol 2011, 127870 (2011).
    • (2011) Int J. Microbiol , vol.2011 , pp. 127870
    • Ristl, R.1
  • 62
    • 53249147141 scopus 로고    scopus 로고
    • Not just for eukarya anymore: Protein glycosylation in bacteria and archaea
    • Abu-Qarn, M., Eichler, J. & Sharon, N. Not just for eukarya anymore: protein glycosylation in bacteria and archaea. Curr. Opin. Struct. Biol. 18, 544-550 (2008).
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 544-550
    • Abu-Qarn, M.1    Eichler, J.2    Sharon, N.3
  • 63
    • 0036067107 scopus 로고    scopus 로고
    • Never say never again: Protein glycosylation in pathogenic bacteria
    • Benz, I. & Schmidt, M. A. Never say never again: protein glycosylation in pathogenic bacteria. Mol. Microbiol. 45, 267-276 (2002).
    • (2002) Mol. Microbiol. , vol.45 , pp. 267-276
    • Benz, I.1    Schmidt, M.A.2
  • 65
    • 51049100438 scopus 로고    scopus 로고
    • Molecular basis of S-layer glycoprotein glycan biosynthesis in Geobacillus stearothermophilus
    • Steiner, K. et al. Molecular basis of S-layer glycoprotein glycan biosynthesis in Geobacillus stearothermophilus. J. Biol. Chem. 283, 21120-21133 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 21120-21133
    • Steiner, K.1
  • 66
    • 66249118703 scopus 로고    scopus 로고
    • Construction of a gene knockout system for application in Paenibacillus alvei CCM 2051T, exemplified by the S-layer glycan biosynthesis initiation enzyme WsfP
    • Zarschler, K., Janesch, B., Zayni, S., Schaffer, C. & Messner, P. Construction of a gene knockout system for application in Paenibacillus alvei CCM 2051T, exemplified by the S-layer glycan biosynthesis initiation enzyme WsfP. Appl. Environ. Microbiol. 75, 3077-3085 (2009).
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 3077-3085
    • Zarschler, K.1    Janesch, B.2    Zayni, S.3    Schaffer, C.4    Messner, P.5
  • 67
    • 80055084408 scopus 로고    scopus 로고
    • Characterization and scope of S-layer protein O-glycosylation in Tannerella forsythia
    • Posch, G. et al. Characterization and scope of S-layer protein O-glycosylation in Tannerella forsythia. J. Biol. Chem. 286, 38714-38724 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 38714-38724
    • Posch, G.1
  • 68
    • 62149118280 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the S-layer proteins from Clostridium difficile demonstrates the absence of glycosylation
    • Qazi, O. et al. Mass spectrometric analysis of the S-layer proteins from Clostridium difficile demonstrates the absence of glycosylation. J. Mass Spectrom. 44, 368-374 (2009).
    • (2009) J. Mass Spectrom. , vol.44 , pp. 368-374
    • Qazi, O.1
  • 69
    • 0030610711 scopus 로고    scopus 로고
    • Functions of S-layers
    • Beveridge, T. J. et al. Functions of S-layers. FEMS Microbiol. Rev. 20, 99-149 (1997).
    • (1997) FEMS Microbiol. Rev. , vol.20 , pp. 99-149
    • Beveridge, T.J.1
  • 70
    • 84874105332 scopus 로고    scopus 로고
    • Characterization of a S-layer protein from Lactobacillus crispatus K313 and the domains responsible for binding to cell wall and adherence to collagen
    • Sun, Z. et al. Characterization of a S-layer protein from Lactobacillus crispatus K313 and the domains responsible for binding to cell wall and adherence to collagen. Appl. Microbiol. Biotechnol. 97, 1941-1952 (2013).
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 1941-1952
    • Sun, Z.1
  • 71
    • 0033754371 scopus 로고    scopus 로고
    • Characterization of the collagen-binding S-layer protein CbsA of Lactobacillus crispatus
    • Sillanpaa, J. et al. Characterization of the collagen-binding S-layer protein CbsA of Lactobacillus crispatus. J. Bacteriol. 182, 6440-6450 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 6440-6450
    • Sillanpaa, J.1
  • 72
    • 0029025393 scopus 로고
    • A collagen-binding S-layer protein in Lactobacillus crispatus
    • Toba, T. et al. A collagen-binding S-layer protein in Lactobacillus crispatus. Appl. Environ. Microbiol. 61, 2467-2471 (1995).
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2467-2471
    • Toba, T.1
  • 73
    • 33750033868 scopus 로고    scopus 로고
    • Surface layer proteins from Clostridium difficile induce inflammatory and regulatory cytokines in human monocytes and dendritic cells
    • Ausiello, C. M. et al. Surface layer proteins from Clostridium difficile induce inflammatory and regulatory cytokines in human monocytes and dendritic cells. Microbes Infect. 8, 2640-2646 (2006).
    • (2006) Microbes Infect. , vol.8 , pp. 2640-2646
    • Ausiello, C.M.1
  • 74
    • 79959828804 scopus 로고    scopus 로고
    • A role for TLR4 in Clostridium difficile infection and the recognition of surface layer proteins
    • Ryan, A. et al. A role for TLR4 in Clostridium difficile infection and the recognition of surface layer proteins. PLoS Pathog 7, e1002076 (2011).
    • (2011) PLoS Pathog , vol.7
    • Ryan, A.1
  • 75
    • 0036785598 scopus 로고    scopus 로고
    • Binding of Clostridium difficile surface layer proteins to gastrointestinal tissues
    • Calabi, E., Calabi, F., Phillips, A. D. & Fairweather, N. Binding of Clostridium difficile surface layer proteins to gastrointestinal tissues. Infect. Immun. 70, 5770-5778 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 5770-5778
    • Calabi, E.1    Calabi, F.2    Phillips, A.D.3    Fairweather, N.4
  • 76
    • 84880647378 scopus 로고    scopus 로고
    • Improved bacterial mutagenesis by high-frequency allele exchange, demonstrated in Clostridium difficile and Streptococcus suis
    • Faulds-Pain, A. & Wren, B. W. Improved bacterial mutagenesis by high-frequency allele exchange, demonstrated in Clostridium difficile and Streptococcus suis. Appl. Environ. Microbiol. 79, 4768-4771 (2013).
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 4768-4771
    • Faulds-Pain, A.1    Wren, B.W.2
  • 77
    • 84863792386 scopus 로고    scopus 로고
    • Precise manipulation of the Clostridium difficile chromosome reveals a lack of association between tcdC genotype and toxin production
    • Cartman, S. T., Kelly, M. L., Heeg, D., Heap, J. T. & Minton, N. P. Precise manipulation of the Clostridium difficile chromosome reveals a lack of association between tcdC genotype and toxin production. Appl. Environ. Microbiol. 78, 4683-4690 (2012).
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 4683-4690
    • Cartman, S.T.1    Kelly, M.L.2    Heeg, D.3    Heap, J.T.4    Minton, N.P.5
  • 78
    • 84860362257 scopus 로고    scopus 로고
    • Integration of DNA into bacterial chromosomes from plasmids without a counter-selection marker
    • Heap, J. T. et al. Integration of DNA into bacterial chromosomes from plasmids without a counter-selection marker. Nucleic Acids Res. 40, e59 (2012).
    • (2012) Nucleic Acids Res. , vol.40
    • Heap, J.T.1
  • 79
    • 74349118819 scopus 로고    scopus 로고
    • BslA the S-layer adhesin of B. Anthracis, is a virulence factor for anthrax pathogenesis
    • Kern, J. & Schneewind, O. BslA, the S-layer adhesin of B. anthracis, is a virulence factor for anthrax pathogenesis. Mol. Microbiol. 75, 324-332 (2010).
    • (2010) Mol. Microbiol. , vol.75 , pp. 324-332
    • Kern, J.1    Schneewind, O.2
  • 80
    • 77954358807 scopus 로고    scopus 로고
    • A Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdC
    • Tarlovsky, Y. et al. A Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdC. J. Bacteriol. 192, 3503-3511 (2010).
    • (2010) J. Bacteriol. , vol.192 , pp. 3503-3511
    • Tarlovsky, Y.1
  • 81
    • 0033970122 scopus 로고    scopus 로고
    • Roles of the surface layer proteins of Campylobacter fetus subsp. Fetus in ovine abortion
    • Grogono-Thomas, R., Dworkin, J., Blaser, M. J. & Newell, D. G. Roles of the surface layer proteins of Campylobacter fetus subsp. fetus in ovine abortion. Infect. Immun. 68, 1687-1691 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 1687-1691
    • Grogono-Thomas, R.1    Dworkin, J.2    Blaser, M.J.3    Newell, D.G.4
  • 82
    • 0028950818 scopus 로고
    • Protein shift and antigenic variation in the S-layer of Campylobacter fetus subsp. Venerealis during bovine infection accompanied by genomic rearrangement of sapA homologs
    • Garcia, M. M. et al. Protein shift and antigenic variation in the S-layer of Campylobacter fetus subsp. venerealis during bovine infection accompanied by genomic rearrangement of sapA homologs. J. Bacteriol. 177, 1976-1980 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 1976-1980
    • Garcia, M.M.1
  • 83
    • 0027258077 scopus 로고
    • Shift in S-layer protein expression responsible for antigenic variation in Campylobacter fetus
    • Wang, E., Garcia, M. M., Blake, M. S., Pei, Z. & Blaser, M. J. Shift in S-layer protein expression responsible for antigenic variation in Campylobacter fetus. J. Bacteriol. 175, 4979-4984 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 4979-4984
    • Wang, E.1    Garcia, M.M.2    Blake, M.S.3    Pei, Z.4    Blaser, M.J.5
  • 84
    • 0027507214 scopus 로고
    • Pathogenesis of Campylobacter fetus infections: Critical role of high-molecular-weight S-layer proteins in virulence
    • Blaser, M. J. & Pei, Z. Pathogenesis of Campylobacter fetus infections: critical role of high-molecular-weight S-layer proteins in virulence. J. Infect. Dis. 167, 372-377 (1993).
    • (1993) J. Infect. Dis. , vol.167 , pp. 372-377
    • Blaser, M.J.1    Pei, Z.2
  • 85
    • 0023099751 scopus 로고
    • Pathogenesis of Campylobacter fetus infections: Serum resistance associated with high-molecular-weight surface proteins
    • Blaser, M. J. et al. Pathogenesis of Campylobacter fetus infections: serum resistance associated with high-molecular-weight surface proteins. J. Infect. Dis. 155, 696-706 (1987).
    • (1987) J. Infect. Dis. , vol.155 , pp. 696-706
    • Blaser, M.J.1
  • 86
    • 0023947952 scopus 로고
    • Pathogenesis of Campylobacter fetus infections. Failure of encapsulated Campylobacter fetus to bind C3b explains serum and phagocytosis resistance
    • Blaser, M. J., Smith, P. F., Repine, J. E. & Joiner, K. A. Pathogenesis of Campylobacter fetus infections. Failure of encapsulated Campylobacter fetus to bind C3b explains serum and phagocytosis resistance. J. Clin. Invest. 81, 1434-1444 (1988).
    • (1988) J. Clin. Invest. , vol.81 , pp. 1434-1444
    • Blaser, M.J.1    Smith, P.F.2    Repine, J.E.3    Joiner, K.A.4
  • 87
    • 20444376499 scopus 로고    scopus 로고
    • Mechanisms underlying Campylobacter fetus pathogenesis in humans: Surface-layer protein variation in relapsing infections
    • Tu, Z. C., Gaudreau, C. & Blaser, M. J. Mechanisms underlying Campylobacter fetus pathogenesis in humans: surface-layer protein variation in relapsing infections. J. Infect. Dis. 191, 2082-2089 (2005).
    • (2005) J. Infect. Dis. , vol.191 , pp. 2082-2089
    • Tu, Z.C.1    Gaudreau, C.2    Blaser, M.J.3
  • 88
    • 77953616099 scopus 로고    scopus 로고
    • Periodontitis: A polymicrobial disruption of host homeostasis
    • Darveau, R. P. Periodontitis: a polymicrobial disruption of host homeostasis. Nature Rev. Microbiol. 8, 481-490 (2010).
    • (2010) Nature Rev. Microbiol. , vol.8 , pp. 481-490
    • Darveau, R.P.1
  • 90
    • 0347513213 scopus 로고    scopus 로고
    • The surface (S-) layer is a virulence factor of Bacteroides forsythus
    • Sabet, M., Lee, S. W., Nauman, R. K., Sims, T. & Um, H. S. The surface (S-) layer is a virulence factor of Bacteroides forsythus. Microbiology 149, 3617-3627 (2003).
    • (2003) Microbiology , vol.149 , pp. 3617-3627
    • Sabet, M.1    Lee, S.W.2    Nauman, R.K.3    Sims, T.4    Um, H.S.5
  • 91
    • 0033813567 scopus 로고    scopus 로고
    • Localization of major, high molecular weight proteins in Bacteroides forsythus
    • Higuchi, N. et al. Localization of major, high molecular weight proteins in Bacteroides forsythus. Microbiol. Immunol. 44, 777-780 (2000).
    • (2000) Microbiol. Immunol. , vol.44 , pp. 777-780
    • Higuchi, N.1
  • 92
    • 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. et al. Loss of adherence ability to human gingival epithelial cells in S-layer protein-deficient mutants of Tannerella forsythensis. Microbiology 153, 866-876 (2007).
    • (2007) Microbiology , vol.153 , pp. 866-876
    • Sakakibara, J.1
  • 93
    • 33645210489 scopus 로고    scopus 로고
    • Identification and characterization of the genes encoding a unique surface (S-) layer of Tannerella forsythia
    • Lee, S. W. et al. Identification and characterization of the genes encoding a unique surface (S-) layer of Tannerella forsythia. Gene 371, 102-111 (2006).
    • (2006) Gene , vol.371 , pp. 102-111
    • Lee, S.W.1
  • 94
    • 34047275924 scopus 로고    scopus 로고
    • Role of a Tannerella forsythia exopolysaccharide synthesis operon in biofilm development
    • Honma, K., Inagaki, S., Okuda, K., Kuramitsu, H. K. & Sharma, A. Role of a Tannerella forsythia exopolysaccharide synthesis operon in biofilm development. Microb. Pathog. 42, 156-166 (2007).
    • (2007) Microb. Pathog. , vol.42 , pp. 156-166
    • Honma, K.1    Inagaki, S.2    Okuda, K.3    Kuramitsu, H.K.4    Sharma, A.5
  • 95
    • 77956130622 scopus 로고    scopus 로고
    • A quantitative proteomic analysis of biofilm adaptation by the periodontal pathogen Tannerella forsythia
    • Pham, T. K. et al. A quantitative proteomic analysis of biofilm adaptation by the periodontal pathogen Tannerella forsythia. Proteomics 10, 3130-3141 (2010).
    • (2010) Proteomics , vol.10 , pp. 3130-3141
    • Pham, T.K.1
  • 96
    • 70349547205 scopus 로고    scopus 로고
    • Predatory lifestyle of Bdellovibrio bacteriovorus
    • Sockett, R. E. Predatory lifestyle of Bdellovibrio bacteriovorus. Annu. Rev. Microbiol. 63, 523-539 (2009).
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 523-539
    • Sockett, R.E.1
  • 97
    • 0025731018 scopus 로고
    • Effect of paracrystalline protein surface layers on predation by Bdellovibrio bacteriovorus
    • Koval, S. F. & Hynes, S. H. Effect of paracrystalline protein surface layers on predation by Bdellovibrio bacteriovorus. J. Bacteriol. 173, 2244-2249 (1991).
    • (1991) J. Bacteriol. , vol.173 , pp. 2244-2249
    • Koval, S.F.1    Hynes, S.H.2
  • 98
    • 0023406967 scopus 로고
    • Molecular sieving through S layers of Bacillus stearothermophilus strains
    • Sara, M. & Sleytr, U. B. Molecular sieving through S layers of Bacillus stearothermophilus strains. J. Bacteriol. 169, 4092-4098 (1987).
    • (1987) J. Bacteriol. , vol.169 , pp. 4092-4098
    • Sara, M.1    Sleytr, U.B.2
  • 99
    • 33748780908 scopus 로고    scopus 로고
    • Involvement of the S-layer proteins Hpi and SlpA in the maintenance of cell envelope integrity in Deinococcus radiodurans R1
    • Rothfuss, H., Lara, J. C., Schmid, A. K. & Lidstrom, M. E. Involvement of the S-layer proteins Hpi and SlpA in the maintenance of cell envelope integrity in Deinococcus radiodurans R1. Microbiology 152, 2779-2787 (2006).
    • (2006) Microbiology , vol.152 , pp. 2779-2787
    • Rothfuss, H.1    Lara, J.C.2    Schmid, A.K.3    Lidstrom, M.E.4
  • 100
    • 71749087319 scopus 로고    scopus 로고
    • Cwp84, a surface-associated cysteine protease, plays a role in the maturation of the surface layer of Clostridium difficile
    • Kirby, J. M. et al. Cwp84, a surface-associated cysteine protease, plays a role in the maturation of the surface layer of Clostridium difficile. J. Biol. Chem. 284, 34666-34673 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 34666-34673
    • Kirby, J.M.1
  • 101
    • 79959365481 scopus 로고    scopus 로고
    • Roles of cysteine proteases Cwp84 and Cwp13 in biogenesis of the cell wall of Clostridium difficile
    • de la Riva, L., Willing, S. E., Tate, E. W. & Fairweather, N. F. Roles of cysteine proteases Cwp84 and Cwp13 in biogenesis of the cell wall of Clostridium difficile. J. Bacteriol. 193, 3276-3285 (2011).
    • (2011) J. Bacteriol. , vol.193 , pp. 3276-3285
    • De La Riva, L.1    Willing, S.E.2    Tate, E.W.3    Fairweather, N.F.4
  • 102
    • 33750431733 scopus 로고    scopus 로고
    • Characterization of CidR-mediated regulation in Bacillus anthracis reveals a previously undetected role of S-layer proteins as murein hydrolases
    • Ahn, J. S., Chandramohan, L., Liou, L. E. & Bayles, K. W. Characterization of CidR-mediated regulation in Bacillus anthracis reveals a previously undetected role of S-layer proteins as murein hydrolases. Mol. Microbiol. 62, 1158-1169 (2006).
    • (2006) Mol. Microbiol. , vol.62 , pp. 1158-1169
    • Ahn, J.S.1    Chandramohan, L.2    Liou, L.E.3    Bayles, K.W.4
  • 103
    • 79959537294 scopus 로고    scopus 로고
    • The SLH-domain protein BslO is a determinant of Bacillus anthracis chain length
    • Anderson, V. J., Kern, J. W., McCool, J. W., Schneewind, O. & Missiakas, D. The SLH-domain protein BslO is a determinant of Bacillus anthracis chain length. Mol. Microbiol. 81, 192-205 (2011).
    • (2011) Mol. Microbiol. , vol.81 , pp. 192-205
    • Anderson, V.J.1    Kern, J.W.2    McCool, J.W.3    Schneewind, O.4    Missiakas, D.5
  • 104
    • 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. & Missiakas, 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. 194, 3833-3840 (2012).
    • (2012) J. Bacteriol. , vol.194 , pp. 3833-3840
    • Kern, V.J.1    Kern, J.W.2    Theriot, J.A.3    Schneewind, O.4    Missiakas, D.5
  • 105
    • 80051695335 scopus 로고    scopus 로고
    • Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links
    • Peltier, J. et al. Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links. J. Biol. Chem. 286, 29053-29062 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 29053-29062
    • Peltier, J.1
  • 106
    • 0029900080 scopus 로고    scopus 로고
    • An abundant cell-surface polypeptide is required for swimming by the nonflagellated marine cyanobacterium Synechococcus
    • Brahamsha, B. An abundant cell-surface polypeptide is required for swimming by the nonflagellated marine cyanobacterium Synechococcus. Proc. Natl Acad. Sci. USA 93, 6504-6509 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6504-6509
    • Brahamsha, B.1
  • 107
    • 33846622119 scopus 로고    scopus 로고
    • SwmB a 1.12-megadalton protein that is required for nonflagellar swimming motility in Synechococcus
    • McCarren, J. & Brahamsha, B. SwmB, a 1.12-megadalton protein that is required for nonflagellar swimming motility in Synechococcus. J. Bacteriol. 189, 1158-1162 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 1158-1162
    • McCarren, J.1    Brahamsha, B.2
  • 108
    • 63449134020 scopus 로고    scopus 로고
    • Swimming motility mutants of marine Synechococcus affected in production and localization of the S-layer protein SwmA
    • McCarren, J. & Brahamsha, B. Swimming motility mutants of marine Synechococcus affected in production and localization of the S-layer protein SwmA. J. Bacteriol. 191, 1111-1114 (2009).
    • (2009) J. Bacteriol. , vol.191 , pp. 1111-1114
    • McCarren, J.1    Brahamsha, B.2
  • 109
    • 36048936428 scopus 로고    scopus 로고
    • 7Å projection map of the S-layer protein sbpA obtained with trehalose-embedded monolayer crystals
    • Norville, J. E. et al. 7Å projection map of the S-layer protein sbpA obtained with trehalose-embedded monolayer crystals. J. Struct. Biol. 160, 313-323 (2007).
    • (2007) J. Struct. Biol. , vol.160 , pp. 313-323
    • Norville, J.E.1
  • 110
    • 0001732638 scopus 로고
    • A macromolecular mono-layer in the cell wall of Spirillum spec
    • Houwink, A. L. A macromolecular mono-layer in the cell wall of Spirillum spec. Biochim. Biophys. Acta 10, 360-366 (1953).
    • (1953) Biochim. Biophys. Acta , vol.10 , pp. 360-366
    • Houwink, A.L.1
  • 111
    • 34347256383 scopus 로고    scopus 로고
    • Freeze-fracture electron microscopy
    • Severs, N. J. Freeze-fracture electron microscopy. Nature Protoc. 2, 547-576 (2007).
    • (2007) Nature Protoc. , vol.2 , pp. 547-576
    • Severs, N.J.1
  • 112
    • 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. & Sara, M. Crystalline bacterial cell surface layers (S Layers): from supramolecular cell structure to biomimetics and nanotechnology. Angew. Chem. Int. Ed. 38, 1034-1054 (1999).
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1034-1054
    • Sleytr, U.B.1    Messner, P.2    Pum, D.3    Sara, M.4
  • 113
    • 0028262129 scopus 로고
    • Domain structure of the Acetogenium kivui surface-layer revealed by electron crystallography and sequence-analysis
    • Lupas, A. et al. Domain structure of the Acetogenium kivui surface-layer revealed by electron crystallography and sequence-analysis. J. Bacteriol. 176, 1224-1233 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 1224-1233
    • Lupas, A.1
  • 114
    • 84865818668 scopus 로고    scopus 로고
    • Atomic force microscopy: A nanoscopic view of microbial cell surfaces
    • Dorobantu, L. S., Goss, G. G. & Burrell, R. E. Atomic force microscopy: a nanoscopic view of microbial cell surfaces. Micron 43, 1312-1322 (2012).
    • (2012) Micron , vol.43 , pp. 1312-1322
    • Dorobantu, L.S.1    Goss, G.G.2    Burrell, R.E.3
  • 115
    • 78049314887 scopus 로고    scopus 로고
    • Self-catalyzed growth of S layers via an amorphous-to-crystalline transition limited by folding kinetics
    • Chung, S., Shin, S. H., Bertozzi, C. R. & De Yoreo, J. J. Self-catalyzed growth of S layers via an amorphous-to-crystalline transition limited by folding kinetics. Proc. Natl Acad. Sci. USA 107, 16536-16541 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 16536-16541
    • Chung, S.1    Shin, S.H.2    Bertozzi, C.R.3    De Yoreo, J.J.4
  • 116
    • 0033818702 scopus 로고    scopus 로고
    • Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer
    • Stetefeld, J. et al. Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer. Nature Struct. Biol. 7, 772-776 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , pp. 772-776
    • Stetefeld, J.1
  • 117
    • 0036774262 scopus 로고    scopus 로고
    • Archaeal surface layer proteins contain β propeller, PKD, and β helix domains and are related to metazoan cell surface proteins
    • Jing, H. et al. Archaeal surface layer proteins contain β propeller, PKD, and β helix domains and are related to metazoan cell surface proteins. Structure 10, 1453-1464 (2002).
    • (2002) Structure , vol.10 , pp. 1453-1464
    • Jing, H.1
  • 118
    • 84863939189 scopus 로고    scopus 로고
    • Structure of the surface layer of the methanogenic archaean Methanosarcina acetivorans
    • Arbing, M. A. et al. Structure of the surface layer of the methanogenic archaean Methanosarcina acetivorans. Proc. Natl Acad. Sci. USA 109, 11812-11817 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 11812-11817
    • Arbing, M.A.1
  • 119
    • 60649099858 scopus 로고    scopus 로고
    • Structural insights into the molecular organization of the S-layer from Clostridium difficile
    • Fagan, R. P. et al. Structural insights into the molecular organization of the S-layer from Clostridium difficile. Mol. Microbiol. 71, 1308-1322 (2009).
    • (2009) Mol. Microbiol. , vol.71 , pp. 1308-1322
    • Fagan, R.P.1
  • 120
    • 84858077472 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Punta, M. et al. The Pfam protein families database. Nucleic Acids Res. 40, D290-D301 (2012).
    • (2012) Nucleic Acids Res. , vol.40
    • Punta, M.1
  • 121
    • 84859885138 scopus 로고    scopus 로고
    • The type II secretion system: Biogenesis, molecular architecture and mechanism
    • Korotkov, K. V., Sandkvist, M. & Hol, W. G. The type II secretion system: biogenesis, molecular architecture and mechanism. Nature Rev. Microbiol. 10, 336-351 (2012).
    • (2012) Nature Rev. Microbiol. , vol.10 , pp. 336-351
    • Korotkov, K.V.1    Sandkvist, M.2    Hol, W.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.