메뉴 건너뛰기




Volumn , Issue , 2010, Pages 129-146

Glycosylation of Bacterial and Archaeal Flagellins

Author keywords

[No Author keywords available]

Indexed keywords


EID: 79951988954     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374546-0.00008-0     Document Type: Chapter
Times cited : (2)

References (83)
  • 1
    • 2642619385 scopus 로고    scopus 로고
    • Biochemical and immunological analyses of the flagellin of Clostridium tyrobutyricum ATCC 25755
    • Arnold F., Bedouet L., Batina P., et al. Biochemical and immunological analyses of the flagellin of Clostridium tyrobutyricum ATCC 25755. Microbiol. Immunol. 1998, 42:23-31.
    • (1998) Microbiol. Immunol. , vol.42 , pp. 23-31
    • Arnold, F.1    Bedouet, L.2    Batina, P.3
  • 2
    • 0035979193 scopus 로고    scopus 로고
    • A genomic island in Pseudomonas aeruginosa carries the determinants of flagellin glycosylation
    • Arora S.K., Bangera M., Lory S., Ramphal R. A genomic island in Pseudomonas aeruginosa carries the determinants of flagellin glycosylation. Proc. Natl. Acad. Sci. USA 2001, 98:9342-9347.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9342-9347
    • Arora, S.K.1    Bangera, M.2    Lory, S.3    Ramphal, R.4
  • 3
    • 1642300392 scopus 로고    scopus 로고
    • Sequence polymorphism in the glycosylation island and flagellins of Pseudomonas aeruginosa
    • Arora S.K., Wolfgang M.C., Lory S., Ramphal R. Sequence polymorphism in the glycosylation island and flagellins of Pseudomonas aeruginosa. J. Bacteriol. 2004, 186:2115-2122.
    • (2004) J. Bacteriol. , vol.186 , pp. 2115-2122
    • Arora, S.K.1    Wolfgang, M.C.2    Lory, S.3    Ramphal, R.4
  • 4
    • 21544481151 scopus 로고    scopus 로고
    • Role of motility and flagellin glycosylation in the pathogenesis of Pseudomonas aeruginosa burn wound infections
    • Arora S.K., Neely A.N., Blair B., Lory S., Ramphal R. Role of motility and flagellin glycosylation in the pathogenesis of Pseudomonas aeruginosa burn wound infections. Infect. Immun. 2005, 73:4395-4398.
    • (2005) Infect. Immun. , vol.73 , pp. 4395-4398
    • Arora, S.K.1    Neely, A.N.2    Blair, B.3    Lory, S.4    Ramphal, R.5
  • 5
    • 2642553801 scopus 로고    scopus 로고
    • Recent advances in the structure and assembly of the archaeal flagellum.
    • Bardy S.L., Ng S.Y., Jarrell K.F. Recent advances in the structure and assembly of the archaeal flagellum. J. Mol. Microbiol. Biotechnol. 2004, 7:41-51.
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.7 , pp. 41-51
    • Bardy, S.L.1    Ng, S.Y.2    Jarrell, K.F.3
  • 6
    • 0032246084 scopus 로고    scopus 로고
    • Evidence for an heterogeneous glycosylation of the Clostridium tyrobutyricum ATCC 25755 flagellin
    • Bedouet L., Arnold F., Robreau G., Batina P., Talbot F., Binet A. Evidence for an heterogeneous glycosylation of the Clostridium tyrobutyricum ATCC 25755 flagellin. Microbios 1998, 94:183-192.
    • (1998) Microbios , vol.94 , pp. 183-192
    • Bedouet, L.1    Arnold, F.2    Robreau, G.3    Batina, P.4    Talbot, F.5    Binet, A.6
  • 8
    • 0023731987 scopus 로고
    • Biochemical and cytological analysis of the complex periplasmic flagella from Spirochaeta aurantia
    • Brahamsha B., Greenberg E.P. Biochemical and cytological analysis of the complex periplasmic flagella from Spirochaeta aurantia. J. Bacteriol. 1988, 170:4023-4032.
    • (1988) J. Bacteriol. , vol.170 , pp. 4023-4032
    • Brahamsha, B.1    Greenberg, E.P.2
  • 9
    • 33745207351 scopus 로고    scopus 로고
    • Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in Archaea
    • Chaban B., Voisin S., Kelly J., Logan S.M., Jarrell K.F. Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in Archaea. Mol. Microbiol. 2006, 61:259-268.
    • (2006) Mol. Microbiol. , vol.61 , pp. 259-268
    • Chaban, B.1    Voisin, S.2    Kelly, J.3    Logan, S.M.4    Jarrell, K.F.5
  • 10
    • 27644572105 scopus 로고    scopus 로고
    • Comparative phylogenomics of the food-borne pathogen Campylobacter jejuni reveals genetic markers predictive of infection source
    • Champion O.L., Gaunt M.W., Gundogdu O., et al. Comparative phylogenomics of the food-borne pathogen Campylobacter jejuni reveals genetic markers predictive of infection source. Proc. Natl. Acad. Sci. USA 2005, 102:16043-16048.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16043-16048
    • Champion, O.L.1    Gaunt, M.W.2    Gundogdu, O.3
  • 11
    • 0036948288 scopus 로고    scopus 로고
    • Genetics of motility and chemotaxis of a fascinating group of bacteria: the spirochetes
    • Charon N.W., Goldstein S.F. Genetics of motility and chemotaxis of a fascinating group of bacteria: the spirochetes. Annu. Rev. Genet. 2002, 36:47-73.
    • (2002) Annu. Rev. Genet. , vol.36 , pp. 47-73
    • Charon, N.W.1    Goldstein, S.F.2
  • 12
    • 27744595562 scopus 로고    scopus 로고
    • Identification and characterization of NeuB3 from Campylobacter jejuni as a pseudaminic acid synthase
    • Chou W.K., Dick S., Wakarchuk W.W., Tanner M.E. Identification and characterization of NeuB3 from Campylobacter jejuni as a pseudaminic acid synthase. J. Biol. Chem. 2005, 43:35922-35928.
    • (2005) J. Biol. Chem. , vol.43 , pp. 35922-35928
    • Chou, W.K.1    Dick, S.2    Wakarchuk, W.W.3    Tanner, M.E.4
  • 13
    • 0442292128 scopus 로고    scopus 로고
    • Characterization of CJ1293, a new UDP-GlcNAc C6 dehydratase from Campylobacter jejuni
    • Creuzenet C. Characterization of CJ1293, a new UDP-GlcNAc C6 dehydratase from Campylobacter jejuni. FEBS Lett. 2004, 559:136-140.
    • (2004) FEBS Lett. , vol.559 , pp. 136-140
    • Creuzenet, C.1
  • 14
    • 0034634575 scopus 로고    scopus 로고
    • FlaA1, a new bifunctional UDP-GlcNAc C6 dehydratase/C4 reductase from Helicobacter pylori
    • Creuzenet C., Schur M.J., Li J., Wakarchuk W.W., Lam J.S. FlaA1, a new bifunctional UDP-GlcNAc C6 dehydratase/C4 reductase from Helicobacter pylori. J. Biol. Chem. 2000, 275:34873-34880.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34873-34880
    • Creuzenet, C.1    Schur, M.J.2    Li, J.3    Wakarchuk, W.W.4    Lam, J.S.5
  • 15
    • 0030002653 scopus 로고    scopus 로고
    • Colonization of gnotobiotic piglets by Helicobacter pylori deficient in two flagellin genes
    • Eaton K.A., Suerbaum S., Josenhans C., Krakowka S. Colonization of gnotobiotic piglets by Helicobacter pylori deficient in two flagellin genes. Infect. Immun. 1996, 64:2445-2448.
    • (1996) Infect. Immun. , vol.64 , pp. 2445-2448
    • Eaton, K.A.1    Suerbaum, S.2    Josenhans, C.3    Krakowka, S.4
  • 16
    • 0014939798 scopus 로고
    • Bacterial flagella: polarity of elongation
    • Emerson S.U., Tokuyasu K., Simon M.I. Bacterial flagella: polarity of elongation. Science 1970, 169:190-192.
    • (1970) Science , vol.169 , pp. 190-192
    • Emerson, S.U.1    Tokuyasu, K.2    Simon, M.I.3
  • 17
    • 0034724156 scopus 로고    scopus 로고
    • Heterogeneous glycosylation of immunoglobulin E constructs characterized by top-down high-resolution 2-D mass spectrometry
    • Fridriksson E.K., Beavil A., Holowka D., Gould H.J., Baird B., McLafferty F.W. Heterogeneous glycosylation of immunoglobulin E constructs characterized by top-down high-resolution 2-D mass spectrometry. Biochemistry 2000, 39:3369-3376.
    • (2000) Biochemistry , vol.39 , pp. 3369-3376
    • Fridriksson, E.K.1    Beavil, A.2    Holowka, D.3    Gould, H.J.4    Baird, B.5    McLafferty, F.W.6
  • 18
    • 42349084254 scopus 로고    scopus 로고
    • Divergence of quaternary structures among bacterial flagellar filaments
    • Galkin V.E., Yu X., Bielnicki J., et al. Divergence of quaternary structures among bacterial flagellar filaments. Science 2008, 320:382-385.
    • (2008) Science , vol.320 , pp. 382-385
    • Galkin, V.E.1    Yu, X.2    Bielnicki, J.3
  • 19
    • 0036171803 scopus 로고    scopus 로고
    • Lateral flagella of Aeromonas species are essential for epithelial cell adherence and biofilm formation
    • Gavin R., Rabaan A.A., Merino S., Tomas J.M., Gryllos I., Shaw J.G. Lateral flagella of Aeromonas species are essential for epithelial cell adherence and biofilm formation. Mol. Microbiol. 2002, 43:383-397.
    • (2002) Mol. Microbiol. , vol.43 , pp. 383-397
    • Gavin, R.1    Rabaan, A.A.2    Merino, S.3    Tomas, J.M.4    Gryllos, I.5    Shaw, J.G.6
  • 20
    • 0031965752 scopus 로고    scopus 로고
    • Structure and expression of the FlaA periplasmic flagellar protein of Borrelia burgdorferi
    • Ge Y., Li C., Corum L., Slaughter C.A., Charon N.W. Structure and expression of the FlaA periplasmic flagellar protein of Borrelia burgdorferi. J. Bacteriol. 1998, 180:2418-2425.
    • (1998) J. Bacteriol. , vol.180 , pp. 2418-2425
    • Ge, Y.1    Li, C.2    Corum, L.3    Slaughter, C.A.4    Charon, N.W.5
  • 21
    • 40549146540 scopus 로고    scopus 로고
    • Biosynthesis of CMP-N,N'-diacetyllegionaminic acid from UDP-N,N'-diacetylbacillosamine in Legionella pneumophila
    • Glaze P.A., Watson D.C., Young N.M., Tanner M.E. Biosynthesis of CMP-N,N'-diacetyllegionaminic acid from UDP-N,N'-diacetylbacillosamine in Legionella pneumophila. Biochemistry 2008, 47:3272-3282.
    • (2008) Biochemistry , vol.47 , pp. 3272-3282
    • Glaze, P.A.1    Watson, D.C.2    Young, N.M.3    Tanner, M.E.4
  • 22
    • 0036128480 scopus 로고    scopus 로고
    • Identification of motility and autoagglutination Campylobacter jejuni mutants by random transposon mutagenesis
    • Golden N.J., Acheson D.W. Identification of motility and autoagglutination Campylobacter jejuni mutants by random transposon mutagenesis. Infect. Immun. 2002, 70:1761-1771.
    • (2002) Infect. Immun. , vol.70 , pp. 1761-1771
    • Golden, N.J.1    Acheson, D.W.2
  • 23
    • 0142030034 scopus 로고    scopus 로고
    • Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene
    • Goon S., Kelly J.F., Logan S.M., Ewing C.P., Guerry P. Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene. Mol. Microbiol. 2003, 50:659-671.
    • (2003) Mol. Microbiol. , vol.50 , pp. 659-671
    • Goon, S.1    Kelly, J.F.2    Logan, S.M.3    Ewing, C.P.4    Guerry, P.5
  • 25
    • 0030026519 scopus 로고    scopus 로고
    • Identification and characterization of genes required for post-translational modification of Campylobacter coli VC167 flagellin
    • Guerry P., Doig P., Alm R.A., Burr D.H., Kinsella N., Trust T.J. Identification and characterization of genes required for post-translational modification of Campylobacter coli VC167 flagellin. Mol. Microbiol. 1996, 19:369-378.
    • (1996) Mol. Microbiol. , vol.19 , pp. 369-378
    • Guerry, P.1    Doig, P.2    Alm, R.A.3    Burr, D.H.4    Kinsella, N.5    Trust, T.J.6
  • 26
    • 33645293731 scopus 로고    scopus 로고
    • Changes in flagellin glycosylation affect Campylobacter autoagglutination and virulence
    • Guerry P., Ewing C.P., Schirm M., et al. Changes in flagellin glycosylation affect Campylobacter autoagglutination and virulence. Mol. Microbiol. 2006, 60:299-311.
    • (2006) Mol. Microbiol. , vol.60 , pp. 299-311
    • Guerry, P.1    Ewing, C.P.2    Schirm, M.3
  • 27
    • 0014515268 scopus 로고
    • Polarity of flagellar growth in salmonella
    • Iino T. Polarity of flagellar growth in salmonella. J. Gen. Microbiol. 1969, 56:227-239.
    • (1969) J. Gen. Microbiol. , vol.56 , pp. 227-239
    • Iino, T.1
  • 28
    • 23944508248 scopus 로고    scopus 로고
    • Defense responses of Arabidopsis thaliana inoculated with Pseudomonas syringae pv. tabaci wild type and defective mutants for flagellin (fliC) and flagellin glycosylation (orf1)
    • Ishiga Y., Takeuchi K., Taguchi F., et al. Defense responses of Arabidopsis thaliana inoculated with Pseudomonas syringae pv. tabaci wild type and defective mutants for flagellin (fliC) and flagellin glycosylation (orf1). J. Gen. Plant Pathol. 2005, 71:302-307.
    • (2005) J. Gen. Plant Pathol. , vol.71 , pp. 302-307
    • Ishiga, Y.1    Takeuchi, K.2    Taguchi, F.3
  • 29
    • 0020570237 scopus 로고
    • Synthesis and assembly of flagellar components by Caulo-bacter crescentus motility mutants
    • Johnson R.C., Ferber D.M., Ely B. Synthesis and assembly of flagellar components by Caulo-bacter crescentus motility mutants. J. Bacteriol. 1983, 154:1137-1144.
    • (1983) J. Bacteriol. , vol.154 , pp. 1137-1144
    • Johnson, R.C.1    Ferber, D.M.2    Ely, B.3
  • 30
    • 0032997915 scopus 로고    scopus 로고
    • Cloning and allelic exchange mutagenesis of two flagellin genes of Helicobacter felis
    • Josenhans C., Ferrero R.L., Labigne A., Suerbaum S. Cloning and allelic exchange mutagenesis of two flagellin genes of Helicobacter felis. Mol. Microbiol. 1999, 33:350-362.
    • (1999) Mol. Microbiol. , vol.33 , pp. 350-362
    • Josenhans, C.1    Ferrero, R.L.2    Labigne, A.3    Suerbaum, S.4
  • 31
    • 0037035408 scopus 로고    scopus 로고
    • The neuA/flmD gene cluster of Helicobacter pylori is involved in flagellar biosynthesis and flagellin glycosylation
    • Josenhans C., Vossebein L., Friedrich S., Suerbaum S. The neuA/flmD gene cluster of Helicobacter pylori is involved in flagellar biosynthesis and flagellin glycosylation. FEMS Microbiol. Lett. 2002, 210:165-172.
    • (2002) FEMS Microbiol. Lett. , vol.210 , pp. 165-172
    • Josenhans, C.1    Vossebein, L.2    Friedrich, S.3    Suerbaum, S.4
  • 32
    • 0036181422 scopus 로고    scopus 로고
    • A novel paralogous gene family involved in phase-variable flagella-mediated motility in Campylobacter jejuni
    • Karlyshev A.V., Linton D., Gregson N.A., Wren B.W. A novel paralogous gene family involved in phase-variable flagella-mediated motility in Campylobacter jejuni. Microbiology 2002, 148:473-480.
    • (2002) Microbiology , vol.148 , pp. 473-480
    • Karlyshev, A.V.1    Linton, D.2    Gregson, N.A.3    Wren, B.W.4
  • 34
    • 0002840265 scopus 로고
    • Sialic acids of a new type from the lipopolysaccharides of Pseudomonas aeruginosa and Shigella boydii
    • Knirel Y.A., Vinogradov E.V., L'vov V.L., et al. Sialic acids of a new type from the lipopolysaccharides of Pseudomonas aeruginosa and Shigella boydii. Carbohydr. Res. 1984, 133:C5-C8.
    • (1984) Carbohydr. Res. , vol.133
    • Knirel, Y.A.1    Vinogradov, E.V.2    L'vov, V.L.3
  • 37
    • 33646564396 scopus 로고    scopus 로고
    • Definition of the bacterial N-glycosylation site consensus sequence
    • Kowarik M., Young N.M., Numao S., et al. Definition of the bacterial N-glycosylation site consensus sequence. EMBO J. 2006, 25:1957-1966.
    • (2006) EMBO J. , vol.25 , pp. 1957-1966
    • Kowarik, M.1    Young, N.M.2    Numao, S.3
  • 38
    • 0842303067 scopus 로고    scopus 로고
    • A new class of Caulobacter crescentus flagellar genes
    • Leclerc G., Wang S.P., Ely B. A new class of Caulobacter crescentus flagellar genes. J. Bacteriol. 1998, 180:5010-5019.
    • (1998) J. Bacteriol. , vol.180 , pp. 5010-5019
    • Leclerc, G.1    Wang, S.P.2    Ely, B.3
  • 39
    • 34250348370 scopus 로고    scopus 로고
    • Flagellar motility is critical for Listeria monocytogenes biofilm formation
    • Lemon K.P., Higgins D.E., Kolter R. Flagellar motility is critical for Listeria monocytogenes biofilm formation. J. Bacteriol. 2007, 189:4418-4424.
    • (2007) J. Bacteriol. , vol.189 , pp. 4418-4424
    • Lemon, K.P.1    Higgins, D.E.2    Kolter, R.3
  • 40
    • 0027146367 scopus 로고
    • A species-specific periplasmic flagellar protein of Serpulina (Treponema) hyodysenteriae
    • Li Z., Dumas F., Dubreuil D., Jacques M. A species-specific periplasmic flagellar protein of Serpulina (Treponema) hyodysenteriae. J. Bacteriol. 1993, 175:8000-8007.
    • (1993) J. Bacteriol. , vol.175 , pp. 8000-8007
    • Li, Z.1    Dumas, F.2    Dubreuil, D.3    Jacques, M.4
  • 41
    • 0034057262 scopus 로고    scopus 로고
    • Multiple N-acetyl neuraminic acid synthetase (neuB) genes in Campylobacter jejuni: identification and characterization of the gene involved in sialylation of lipo-oligosaccharide
    • Linton D., Karlyshev A.V., Hitchen P.G., et al. Multiple N-acetyl neuraminic acid synthetase (neuB) genes in Campylobacter jejuni: identification and characterization of the gene involved in sialylation of lipo-oligosaccharide. Mol. Microbiol. 2000, 35:1120-1134.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1120-1134
    • Linton, D.1    Karlyshev, A.V.2    Hitchen, P.G.3
  • 42
    • 33746372147 scopus 로고    scopus 로고
    • PseG of pseudaminic acid biosynthesis: a UDP-sugar hydrolase as a masked glycosyltransferase
    • Liu F., Tanner M.E. PseG of pseudaminic acid biosynthesis: a UDP-sugar hydrolase as a masked glycosyltransferase. J. Biol. Chem. 2006, 281:20902-20909.
    • (2006) J. Biol. Chem. , vol.281 , pp. 20902-20909
    • Liu, F.1    Tanner, M.E.2
  • 43
    • 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
  • 44
    • 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
  • 45
    • 0034176517 scopus 로고    scopus 로고
    • Cloning, sequencing and characterisation of the gene encoding flaC and the post-translational modification of flagellin from Clostridium acetobutylicum ATCC824
    • Lyristis M., Boynton Z.L., Petersen D., Kan Z., Bennett G.N., Rudolph F.B. Cloning, sequencing and characterisation of the gene encoding flaC and the post-translational modification of flagellin from Clostridium acetobutylicum ATCC824. Anaerobe 2000, 6:69-79.
    • (2000) Anaerobe , vol.6 , pp. 69-79
    • Lyristis, M.1    Boynton, Z.L.2    Petersen, D.3    Kan, Z.4    Bennett, G.N.5    Rudolph, F.B.6
  • 46
    • 8844249277 scopus 로고    scopus 로고
    • Type III flagellar protein export and flagellar assembly
    • Macnab R.M. Type III flagellar protein export and flagellar assembly. Biochim. Biophys. Acta 2004, 1694:207-217.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 207-217
    • Macnab, R.M.1
  • 47
    • 33745869039 scopus 로고    scopus 로고
    • Functional characterization of the flagellar glycosylation locus in Campylobacter jejuni 81-176 using a focused metabolomics approach
    • McNally D.J., Hui J.P., Aubry A.J., et al. Functional characterization of the flagellar glycosylation locus in Campylobacter jejuni 81-176 using a focused metabolomics approach. J. Biol. Chem. 2006, 281:18489-18498.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18489-18498
    • McNally, D.J.1    Hui, J.P.2    Aubry, A.J.3
  • 48
    • 34347231618 scopus 로고    scopus 로고
    • Targeted metabolomics analysis of Campylobacter coli VC167 reveals legionaminic acid derivatives as novel flagellar glycans
    • McNally D.J., Aubry A.J., Hui J.P., et al. Targeted metabolomics analysis of Campylobacter coli VC167 reveals legionaminic acid derivatives as novel flagellar glycans. J. Biol. Chem. 2007, 282:14463-14475.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14463-14475
    • McNally, D.J.1    Aubry, A.J.2    Hui, J.P.3
  • 49
    • 48149095691 scopus 로고    scopus 로고
    • CMP-pseudaminic acid is a natural potent inhibitor of PseB, the first enzyme of the pseudaminic acid pathway in Campylobacter jejuni and Helicobacter pylori
    • McNally D.J., Schoenhofen I.C., Houliston R.S., et al. CMP-pseudaminic acid is a natural potent inhibitor of PseB, the first enzyme of the pseudaminic acid pathway in Campylobacter jejuni and Helicobacter pylori. Chem. Med. Chem. 2008, 3:55-59.
    • (2008) Chem. Med. Chem. , vol.3 , pp. 55-59
    • McNally, D.J.1    Schoenhofen, I.C.2    Houliston, R.S.3
  • 50
    • 1842611505 scopus 로고    scopus 로고
    • The Helicobacter pylori flaA1 and wbpB genes control lipopolysaccharide and flagellum synthesis and function
    • Merkx-Jacques A., Obhi R.K., Bethune G., Creuzenet C. The Helicobacter pylori flaA1 and wbpB genes control lipopolysaccharide and flagellum synthesis and function. J. Bacteriol. 2004, 186:2253-2265.
    • (2004) J. Bacteriol. , vol.186 , pp. 2253-2265
    • Merkx-Jacques, A.1    Obhi, R.K.2    Bethune, G.3    Creuzenet, C.4
  • 51
    • 0033784513 scopus 로고    scopus 로고
    • Detection and characterization of autoagglutination activity by Campylobacter jejuni
    • Misawa N., Blaser M.J. Detection and characterization of autoagglutination activity by Campylobacter jejuni. Infect. Immun. 2000, 68:6168-6175.
    • (2000) Infect. Immun. , vol.68 , pp. 6168-6175
    • Misawa, N.1    Blaser, M.J.2
  • 52
    • 20144369141 scopus 로고    scopus 로고
    • Biochemical characterization of the Campylobacter jejuni Cj1294, a novel UDP-4-keto-6-deoxy-GlcNAc aminotransferase that generates UDP-4-amino-4,6-dideoxy-GalNAc
    • Obhi R.K., Creuzenet C. Biochemical characterization of the Campylobacter jejuni Cj1294, a novel UDP-4-keto-6-deoxy-GlcNAc aminotransferase that generates UDP-4-amino-4,6-dideoxy-GalNAc. J. Biol. Chem. 2005, 280:20902-20908.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20902-20908
    • Obhi, R.K.1    Creuzenet, C.2
  • 53
    • 0023779753 scopus 로고
    • Temperature-dependent expression of flagella of Listeria monocytogenes studied by electron microscopy, SDS-PAGE and western blotting
    • Peel M., Donachie W., Shaw A. Temperature-dependent expression of flagella of Listeria monocytogenes studied by electron microscopy, SDS-PAGE and western blotting. J. Gen. Microbiol. 1988, 134:2171-2178.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 2171-2178
    • Peel, M.1    Donachie, W.2    Shaw, A.3
  • 54
    • 0034972996 scopus 로고    scopus 로고
    • Motility and the polar flagellum are required for Aeromonas caviae adherence to HEp-2 cells
    • Rabaan A.A., Gryllos I., Tomas J.M., Shaw J.G. Motility and the polar flagellum are required for Aeromonas caviae adherence to HEp-2 cells. Infect. Immun. 2001, 69:4257-4267.
    • (2001) Infect. Immun. , vol.69 , pp. 4257-4267
    • Rabaan, A.A.1    Gryllos, I.2    Tomas, J.M.3    Shaw, J.G.4
  • 55
    • 0034472722 scopus 로고    scopus 로고
    • Crystallization of the F41 fragment of flagellin and data collection from extremely thin crystals
    • Samatey F.A., Imada K., Vonderviszt F., Shirakihara Y., Namba K. Crystallization of the F41 fragment of flagellin and data collection from extremely thin crystals. J. Struct. Biol. 2000, 132:106-111.
    • (2000) J. Struct. Biol. , vol.132 , pp. 106-111
    • Samatey, F.A.1    Imada, K.2    Vonderviszt, F.3    Shirakihara, Y.4    Namba, K.5
  • 56
    • 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
  • 57
    • 1942540030 scopus 로고    scopus 로고
    • Structural and genetic characterization of glycosylation of type a flagellin in Pseudomonas aeruginosa
    • Schirm M., Arora S.K., Verma A., et al. Structural and genetic characterization of glycosylation of type a flagellin in Pseudomonas aeruginosa. J. Bacteriol. 2004, 186:2523-2531.
    • (2004) J. Bacteriol. , vol.186 , pp. 2523-2531
    • Schirm, M.1    Arora, S.K.2    Verma, A.3
  • 58
    • 4944261230 scopus 로고    scopus 로고
    • Flagellin from Listeria monocytogenes is glycosylated with beta-O-linked N-acetylglucosamine
    • Schirm M., Kalmokoff M., Aubry A., Thibault P., Sandoz M., Logan S.M. Flagellin from Listeria monocytogenes is glycosylated with beta-O-linked N-acetylglucosamine. J. Bacteriol. 2004, 186:6721-6727.
    • (2004) J. Bacteriol. , vol.186 , pp. 6721-6727
    • Schirm, M.1    Kalmokoff, M.2    Aubry, A.3    Thibault, P.4    Sandoz, M.5    Logan, S.M.6
  • 59
    • 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
  • 60
    • 33748687970 scopus 로고    scopus 로고
    • Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction
    • Schoenhofen I.C., McNally D.J., Brisson J.R., Logan S.M. Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction. Glycobiology 2006, 16:8C-14C.
    • (2006) Glycobiology , vol.16
    • Schoenhofen, I.C.1    McNally, D.J.2    Brisson, J.R.3    Logan, S.M.4
  • 61
    • 33644850378 scopus 로고    scopus 로고
    • Functional characterisation of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways
    • Schoenhofen I.C., McNally D.J., Vinogradov E., et al. Functional characterisation 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, I.C.1    McNally, D.J.2    Vinogradov, E.3
  • 62
    • 40449104807 scopus 로고    scopus 로고
    • Identification of the archaeal alg7 gene homolog (encoding N-acetylglucosamine-1-phosphate transferase) of the N-linked glycosylation system by cross-domain complementation in Saccharomyces cerevisiae
    • Shams-Eldin H., Chaban B., Niehus S., Schwarz R.T., Jarrell K.F. Identification of the archaeal alg7 gene homolog (encoding N-acetylglucosamine-1-phosphate transferase) of the N-linked glycosylation system by cross-domain complementation in Saccharomyces cerevisiae. J. Bacteriol. 2008, 190:2217-2220.
    • (2008) J. Bacteriol. , vol.190 , pp. 2217-2220
    • Shams-Eldin, H.1    Chaban, B.2    Niehus, S.3    Schwarz, R.T.4    Jarrell, K.F.5
  • 63
    • 33845388055 scopus 로고    scopus 로고
    • A bifunctional O-GlcNAc transferase governs flagellar motility through anti-repression
    • Shen A., Kamp H.D., Grundling A., Higgins D.E. A bifunctional O-GlcNAc transferase governs flagellar motility through anti-repression. Genes Dev. 2006, 20:3283-3295.
    • (2006) Genes Dev. , vol.20 , pp. 3283-3295
    • Shen, A.1    Kamp, H.D.2    Grundling, A.3    Higgins, D.E.4
  • 64
    • 0842327208 scopus 로고    scopus 로고
    • Selective detection and identification of sugar nucleotides by CE-electrospray-MS and its application to bacterial metabolomics
    • Soo E.C., Aubry A.J., Logan S.M., et al. Selective detection and identification of sugar nucleotides by CE-electrospray-MS and its application to bacterial metabolomics. Anal. Chem. 2004, 76:619-626.
    • (2004) Anal. Chem. , vol.76 , pp. 619-626
    • Soo, E.C.1    Aubry, A.J.2    Logan, S.M.3
  • 65
    • 41549138353 scopus 로고    scopus 로고
    • Flagellin and outer surface proteins from Borrelia burgdorferi are not glycosylated
    • Sterba J., Vancova M., Rudenko N., et al. Flagellin and outer surface proteins from Borrelia burgdorferi are not glycosylated. J. Bacteriol. 2008, 190:2619-2623.
    • (2008) J. Bacteriol. , vol.190 , pp. 2619-2623
    • Sterba, J.1    Vancova, M.2    Rudenko, N.3
  • 66
    • 0037303481 scopus 로고    scopus 로고
    • Differential effects of flagellins from Pseudomonas syringea pvs. tabaci, tomato and glycinea on plant defence response
    • Taguchi F., Shimizu R., Nakajima R., Toyoda K., Shiraishi T., Ichinose Y. Differential effects of flagellins from Pseudomonas syringea pvs. tabaci, tomato and glycinea on plant defence response. Plant Physiol. Biochem. 2003, 41:165-174.
    • (2003) Plant Physiol. Biochem. , vol.41 , pp. 165-174
    • Taguchi, F.1    Shimizu, R.2    Nakajima, R.3    Toyoda, K.4    Shiraishi, T.5    Ichinose, Y.6
  • 67
    • 33845461505 scopus 로고    scopus 로고
    • A homologue of the 3-oxoacyl-(acyl carrier protein) synthase III gene located in the glycosylation island of Pseudomonas syringae pv. tabaci regulates virulence factors via N-acyl homoserine lactone and fatty acid synthesis
    • Taguchi F., Ogawa Y., Takeuchi K., et al. A homologue of the 3-oxoacyl-(acyl carrier protein) synthase III gene located in the glycosylation island of Pseudomonas syringae pv. tabaci regulates virulence factors via N-acyl homoserine lactone and fatty acid synthesis. J. Bacteriol. 2006, 188:8376-8384.
    • (2006) J. Bacteriol. , vol.188 , pp. 8376-8384
    • Taguchi, F.1    Ogawa, Y.2    Takeuchi, K.3
  • 68
    • 33646364311 scopus 로고    scopus 로고
    • Identification of glycosylation genes and glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci
    • Taguchi F., Takeuchi K., Katoh E., et al. Identification of glycosylation genes and glycosylated amino acids of flagellin in Pseudomonas syringae pv. tabaci. Cell Microbiol. 2006, 8:923-938.
    • (2006) Cell Microbiol. , vol.8 , pp. 923-938
    • Taguchi, F.1    Takeuchi, K.2    Katoh, E.3
  • 69
    • 38749097827 scopus 로고    scopus 로고
    • Effects of glycosylation on swimming ability and flagellar polymorphic transformation in Pseudomonas syringae pv. tabaci 6605
    • Taguchi F., Shibata S., Suzuki T., et al. Effects of glycosylation on swimming ability and flagellar polymorphic transformation in Pseudomonas syringae pv. tabaci 6605. J. Bacteriol. 2008, 190:764-768.
    • (2008) J. Bacteriol. , vol.190 , pp. 764-768
    • Taguchi, F.1    Shibata, S.2    Suzuki, T.3
  • 70
    • 0242575011 scopus 로고    scopus 로고
    • Flagellin glycosylation island in Pseudomonas syringea pv. glycinea and its role in host specificity
    • Takeuchi K., Taguchi F., Inagaki Y., Toyoda K., Shiraishi T., Ichinose Y. Flagellin glycosylation island in Pseudomonas syringea pv. glycinea and its role in host specificity. J. Bacteriol. 2003, 185:6658-6665.
    • (2003) J. Bacteriol. , vol.185 , pp. 6658-6665
    • Takeuchi, K.1    Taguchi, F.2    Inagaki, Y.3    Toyoda, K.4    Shiraishi, T.5    Ichinose, Y.6
  • 71
    • 34948833162 scopus 로고    scopus 로고
    • Flagellin glycans from two pathovars of Pseudomonas syringae contain rhamnose in d and l configurations in different ratios and modified 4-amino-4,6-dideoxyglucose
    • Takeuchi K., Ono H., Yoshida M., et al. Flagellin glycans from two pathovars of Pseudomonas syringae contain rhamnose in d and l configurations in different ratios and modified 4-amino-4,6-dideoxyglucose. J. Bacteriol. 2007, 189:6945-6956.
    • (2007) J. Bacteriol. , vol.189 , pp. 6945-6956
    • Takeuchi, K.1    Ono, H.2    Yoshida, M.3
  • 72
    • 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., et al. 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
  • 73
    • 0035105745 scopus 로고    scopus 로고
    • The archaeal flagellum: a different kind of prokaryotic motility structure
    • Thomas N.A., Bardy S.L., Jarrell K.F. The archaeal flagellum: a different kind of prokaryotic motility structure. FEMS Microbiol. Rev. 2001, 25:147-174.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 147-174
    • Thomas, N.A.1    Bardy, S.L.2    Jarrell, K.F.3
  • 74
    • 33748768732 scopus 로고    scopus 로고
    • The archaeabacterial flagellar filament: a bacterial propeller with a pilus-like structure
    • Trachtenberg S., Cohen-Krausz S. The archaeabacterial flagellar filament: a bacterial propeller with a pilus-like structure. J. Mol. Microbiol. Biotechnol. 2006, 11:208-220.
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 208-220
    • Trachtenberg, S.1    Cohen-Krausz, S.2
  • 75
    • 28444479119 scopus 로고    scopus 로고
    • Roles of specific amino acids in the N terminus of Pseudomonas aeruginosa flagellin and of flagellin glycosylation in the innate immune response
    • Verma A., Arora S.K., Kuravi S.K., Ramphal R. Roles of specific amino acids in the N terminus of Pseudomonas aeruginosa flagellin and of flagellin glycosylation in the innate immune response. Infect. Immun. 2005, 73:8237-8246.
    • (2005) Infect. Immun. , vol.73 , pp. 8237-8246
    • Verma, A.1    Arora, S.K.2    Kuravi, S.K.3    Ramphal, R.4
  • 76
    • 33744986533 scopus 로고    scopus 로고
    • Glycosylation of b-Type flagellin of Pseudomonas aeruginosa: structural and genetic basis
    • Verma A., Schirm M., Arora S.K., Thibault P., Logan S.M., Ramphal R. Glycosylation of b-Type flagellin of Pseudomonas aeruginosa: structural and genetic basis. J. Bacteriol. 2006, 188:4395-4403.
    • (2006) J. Bacteriol. , vol.188 , pp. 4395-4403
    • Verma, A.1    Schirm, M.2    Arora, S.K.3    Thibault, P.4    Logan, S.M.5    Ramphal, R.6
  • 77
    • 0022344062 scopus 로고
    • Regulation of sialic acid metabolism in Escherichia coli: role of N-acylneuraminate pyruvate-lyase
    • Vimr E.R., Troy F.A. Regulation of sialic acid metabolism in Escherichia coli: role of N-acylneuraminate pyruvate-lyase. J. Bacteriol. 1985, 164:854-860.
    • (1985) J. Bacteriol. , vol.164 , pp. 854-860
    • Vimr, E.R.1    Troy, F.A.2
  • 79
    • 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., et al. 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
  • 80
    • 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
  • 81
    • 0031741394 scopus 로고    scopus 로고
    • Flagellins, but not endoflagellar sheath proteins of Treponema pallidum and of pathogen-related oral spirochetes are glycosylated
    • Wyss C. Flagellins, but not endoflagellar sheath proteins of Treponema pallidum and of pathogen-related oral spirochetes are glycosylated. Infect. Immun. 1998, 66:5751-5754.
    • (1998) Infect. Immun. , vol.66 , pp. 5751-5754
    • Wyss, C.1
  • 82
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K., Maki-Yonekura S., Namba K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 2003, 424:643-650.
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 83
    • 14844293874 scopus 로고    scopus 로고
    • Building the atomic model for the bacterial flagellar filament by electron cryomicroscopy and image analysis
    • Yonekura K., Maki-Yonekura S., Namba K. Building the atomic model for the bacterial flagellar filament by electron cryomicroscopy and image analysis. Structure 2005, 13:407-412.
    • (2005) Structure , vol.13 , pp. 407-412
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.