메뉴 건너뛰기




Volumn 50, Issue 2, 2003, Pages 659-671

Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FLAGELLIN; FORMIC ACID DERIVATIVE; PSEUDAMINIC ACID; UNCLASSIFIED DRUG;

EID: 0142030034     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03725.x     Document Type: Article
Times cited : (162)

References (39)
  • 1
    • 0035957518 scopus 로고    scopus 로고
    • Flagellin polymerization control by cytoosolic export chaperone
    • Auvrey, F., Thomas, J., Fraser, G.M., and Hughes, C. (2001) Flagellin polymerization control by cytoosolic export chaperone. J Mol Biol 308: 221-229.
    • (2001) J Mol Biol , vol.308 , pp. 221-229
    • Auvrey, F.1    Thomas, J.2    Fraser, G.M.3    Hughes, C.4
  • 2
    • 0034939563 scopus 로고    scopus 로고
    • Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA-1 adhesin
    • Benz, I., and Schmidt, MA (2001) Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA-1 adhesin. Mol Microbiol 40: 1403-1413.
    • (2001) Mol Microbiol , vol.40 , pp. 1403-1413
    • Benz, I.1    Schmidt, M.A.2
  • 4
    • 0031750753 scopus 로고    scopus 로고
    • Cloning and comparison of fliC genes and identification of glycosylation in the flagellin of Pseudomonas aeruginosa a-type strains
    • Brimer, C.D., and Montie, T.C. (1998) Cloning and comparison of fliC genes and identification of glycosylation in the flagellin of Pseudomonas aeruginosa a-type strains. J Bacteriol 178: 3209-3217.
    • (1998) J Bacteriol , vol.178 , pp. 3209-3217
    • Brimer, C.D.1    Montie, T.C.2
  • 7
    • 0029965091 scopus 로고    scopus 로고
    • Definition of the full extent of glycosylation of the 45-kilodalton glycoprotein of Mycobacterium tuberculosis
    • Dobos, K.M., Khoo, K.H., Swiderek, K.M., Brennan, P.J., and Belisle, J.T. (1996) Definition of the full extent of glycosylation of the 45-kilodalton glycoprotein of Mycobacterium tuberculosis. J Bacteriol 178: 2498-2506.
    • (1996) J Bacteriol , vol.178 , pp. 2498-2506
    • Dobos, K.M.1    Khoo, K.H.2    Swiderek, K.M.3    Brennan, P.J.4    Belisle, J.T.5
  • 8
    • 0030049732 scopus 로고    scopus 로고
    • Characterization of a posttranslational modification of Campylobacter flagellin: Identification of a serospecific glycosyl moiety
    • Doig, P., Kinsella, N., Guerry, P., and Trust, T.J. (1996) Characterization of a posttranslational modification of Campylobacter flagellin: identification of a serospecific glycosyl moiety. Mol Microbiol 19: 379-387.
    • (1996) Mol Microbiol , vol.19 , pp. 379-387
    • Doig, P.1    Kinsella, N.2    Guerry, P.3    Trust, T.J.4
  • 9
    • 0027429745 scopus 로고
    • Evidence for the covalent linkage of carbohydrate polymers to a glycoprotein from Streptococcus sanguis
    • Erickson, P.R., and Herzberg, M.C. (1993) Evidence for the covalent linkage of carbohydrate polymers to a glycoprotein from Streptococcus sanguis. J Biol Chem 268: 23780-23783.
    • (1993) J Biol Chem , vol.268 , pp. 23780-23783
    • Erickson, P.R.1    Herzberg, M.C.2
  • 10
    • 0027514448 scopus 로고
    • Expression of the Mycobacterium tuberculosis 19-kilodalton antigen in Mycobacterium smegmatis: Immunological analysis and evidence of glycosylation
    • Garbe, T., Harris, D., Vordermeier, M., Lathigra, R., Ivanyi, J., and Young, D. (1993) Expression of the Mycobacterium tuberculosis 19-kilodalton antigen in Mycobacterium smegmatis: immunological analysis and evidence of glycosylation. Infect Immun 61: 260-267.
    • (1993) Infect Immun , vol.61 , pp. 260-267
    • Garbe, T.1    Harris, D.2    Vordermeier, M.3    Lathigra, R.4    Ivanyi, J.5    Young, D.6
  • 12
    • 0028198979 scopus 로고
    • Systems of experimental genetics for Campylobacter species
    • Guerry, P., Yao, R., Alm, R.A., Burr, D.H., and Trust, T.J. (1994) Systems of experimental genetics for Campylobacter species. Methods Enzymol 235: 474-481.
    • (1994) Methods Enzymol , vol.235 , pp. 474-481
    • Guerry, P.1    Yao, R.2    Alm, R.A.3    Burr, D.H.4    Trust, T.J.5
  • 13
    • 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., and Trust, T.J. (1996) Identification and characterization of genes required for post-translational modification of Campylobacter coli VC167 flagellin. Mol Microbiol 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
  • 14
    • 0034442692 scopus 로고    scopus 로고
    • Sialylation of lipooligosaccharide cores affects immunogenicity and serum resistance of Campylobacter jejuni
    • Guerry, P., Ewing, C.P., Hickey, T.E., Prendergast, M.M., and Moran, A.P. (2000) Sialylation of lipooligosaccharide cores affects immunogenicity and serum resistance of Campylobacter jejuni. Infect Immun 68: 6656-6662.
    • (2000) Infect Immun , vol.68 , pp. 6656-6662
    • Guerry, P.1    Ewing, C.P.2    Hickey, T.E.3    Prendergast, M.M.4    Moran, A.P.5
  • 15
    • 0036153611 scopus 로고    scopus 로고
    • Phase variation of Campylobacter jejuni 81-176 lipooligosaccharide affects ganglioside mimicry and invasiveness in vitro
    • Guerry, P., Szymanski, C.M., Burr, D.H., Prendergast, M., Ewing, C.P., Hickey, T.E., et al. (2001) Phase variation of Campylobacter jejuni 81-176 lipooligosaccharide affects ganglioside mimicry and invasiveness in vitro. Infect Immun 70: 787-793.
    • (2001) Infect Immun , vol.70 , pp. 787-793
    • Guerry, P.1    Szymanski, C.M.2    Burr, D.H.3    Prendergast, M.4    Ewing, C.P.5    Hickey, T.E.6
  • 16
    • 0023617168 scopus 로고
    • Antigenic variation of Campylobacter flagellin
    • Harris, L.A., Logan, S.M., Guerry, P., and Trust, T.J. (1987) Antigenic variation of Campylobacter flagellin. J Bacteriol 169: 5066-5071.
    • (1987) J Bacteriol , vol.169 , pp. 5066-5071
    • Harris, L.A.1    Logan, S.M.2    Guerry, P.3    Trust, T.J.4
  • 17
    • 0035050923 scopus 로고    scopus 로고
    • Transposon mutagenesis of Campylobacter jejuni identifies a bipartite energy taxis system required for motility
    • Hendrixson, D.R., Akerley, B.J., and DiRita, V.J. (2001) Transposon mutagenesis of Campylobacter jejuni identifies a bipartite energy taxis system required for motility. Mol Microbiol 40: 214-224.
    • (2001) Mol Microbiol , vol.40 , pp. 214-224
    • Hendrixson, D.R.1    Akerley, B.J.2    Dirita, V.J.3
  • 18
    • 0035053888 scopus 로고    scopus 로고
    • Roles of rpoN, fliA, and flgR in expression of flagella in Campylobacter jejuni
    • Jagannathan, A., Constantinidou, C., and Penn, C.W. (2001) Roles of rpoN, fliA, and flgR in expression of flagella in Campylobacter jejuni. J Bacteriol 183: 2937-2942.
    • (2001) J Bacteriol , vol.183 , pp. 2937-2942
    • Jagannathan, A.1    Constantinidou, C.2    Penn, C.W.3
  • 19
    • 0020570237 scopus 로고
    • Synthesis and assembly of flagellar components by Caulobacter crescentus motility mutants
    • Johnson, R.C., Ferber, D.M., and Ely, B. (1983) Synthesis and assembly of flagellar components by Caulobacter crescentus motility mutants. J Bacteriol 154: 1137-1144.
    • (1983) J Bacteriol , vol.154 , pp. 1137-1144
    • Johnson, R.C.1    Ferber, D.M.2    Ely, B.3
  • 20
    • 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., and Suerbaum, S. (2002) The neuA/flmD gene cluster of Helicobacter pylori is involved in flagellar biosynthesis and flagellin glycosylation. FEMS Microbiol Lett 210: 165-172.
    • (2002) FEMS Microbiol Lett , vol.210 , pp. 165-172
    • Josenhans, C.1    Vossebein, L.2    Friedrich, S.3    Suerbaum, S.4
  • 21
    • 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., and Wren, B.W. (2002) A novel paralogous gene family involved in phase variable flagella-mediated motility in Campylobacter jejuni. Microbiol 148: 473-480.
    • (2002) Microbiol , vol.148 , pp. 473-480
    • Karlyshev, A.V.1    Linton, D.2    Gregson, N.A.3    Wren, B.W.4
  • 23
    • 0021824456 scopus 로고
    • A point source outbreak of campylobacteriosis associated with consumption of raw milk
    • Korlath, J.A., Osterholm, M.T., Judy, L.A., Forfang, J.C., and Robinson, R.A. (1985) A point source outbreak of campylobacteriosis associated with consumption of raw milk. J Infect Dis 152: 592-596.
    • (1985) J Infect Dis , vol.152 , pp. 592-596
    • Korlath, J.A.1    Osterholm, M.T.2    Judy, L.A.3    Forfang, J.C.4    Robinson, R.A.5
  • 24
    • 0842303067 scopus 로고    scopus 로고
    • A new class of Caulobacter crescentus flagellar genes
    • LeClerc, G., Wang, S.P., and Ely, B. (1998) A new class of Caulobacter crescentus flagellar genes. J Bacteriol 180: 5010-5019.
    • (1998) J Bacteriol , vol.180 , pp. 5010-5019
    • LeClerc, G.1    Wang, S.P.2    Ely, B.3
  • 25
    • 0032783142 scopus 로고    scopus 로고
    • Identification of a glycoprotein produced by enterotoxigenic Escherichia coli
    • Lindenthal, C., and Elsinghorst, E.A. (1999) Identification of a glycoprotein produced by enterotoxigenic Escherichia coli. Infect Immun 67: 4084-4091.
    • (1999) Infect Immun , vol.67 , pp. 4084-4091
    • Lindenthal, C.1    Elsinghorst, E.A.2
  • 26
    • 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 the lipopolysaccharide
    • Linton, D., Karlyshev, A.V., Hitchen, P.G., Morris, H.R., Dell, A., Gregson, N.A., and Wren, B.W. (2000) Multiple N-acetyl neuraminic acid synthetase (neuB) genes in Campylobacter jejuni: identification and characterization of the gene involved in sialylation of the lipopolysaccharide. Mol Microbiol 35: 1120-1134.
    • (2000) Mol Microbiol , vol.35 , pp. 1120-1134
    • Linton, D.1    Karlyshev, A.V.2    Hitchen, P.G.3    Morris, H.R.4    Dell, A.5    Gregson, N.A.6    Wren, B.W.7
  • 27
    • 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., and Guerry, P. (2002) Structural heterogeneity of carbohydrate modifications affects serospecificity of Campylobacter flagellins. Mol Microbiol 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
  • 28
    • 0036122161 scopus 로고    scopus 로고
    • Functional substitution of the TibC protein of enterotoxigenic Escherichia coli for the authotransporter adhesin heptosyltransferase of the AIDA system
    • Moormann, C., Benz, I., and Schmidt, M.A. (2002) Functional substitution of the TibC protein of enterotoxigenic Escherichia coli for the authotransporter adhesin heptosyltransferase of the AIDA system. Infect Immun 70: 2264-2270.
    • (2002) Infect Immun , vol.70 , pp. 2264-2270
    • Moormann, C.1    Benz, I.2    Schmidt, M.A.3
  • 29
    • 0033003657 scopus 로고    scopus 로고
    • Serotyping of Campylobacter jejuni based on heat-stable antigens: Relevance, molecular basis and implications for pathogenesis
    • Moran, A.P., and Penner, J.L. (1999) Serotyping of Campylobacter jejuni based on heat-stable antigens: relevance, molecular basis and implications for pathogenesis. J Appl Microbiol 66: 361-377.
    • (1999) J Appl Microbiol , vol.66 , pp. 361-377
    • Moran, A.P.1    Penner, J.L.2
  • 30
    • 0034628526 scopus 로고    scopus 로고
    • The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hyper-variable tracts
    • Parkhill, J., Wren, B.W., Mungall, K., Ketley, J.M., Churcher, C., Basham, D., et al. (2000) The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hyper-variable tracts. Nature 403: 665-668.
    • (2000) Nature , vol.403 , pp. 665-668
    • Parkhill, J.1    Wren, B.W.2    Mungall, K.3    Ketley, J.M.4    Churcher, C.5    Basham, D.6
  • 31
    • 0028283047 scopus 로고
    • Structural and antigenic characteristics of Campylobacter coli FlaA flagellin
    • Power, M.E., Guerry, P., McCubbin, W.D., Kay, C.M., and Trust, T.J. (1994) Structural and antigenic characteristics of Campylobacter coli FlaA flagellin. J Bacteriol 176: 3303-3313.
    • (1994) J Bacteriol , vol.176 , pp. 3303-3313
    • Power, M.E.1    Guerry, P.2    McCubbin, W.D.3    Kay, C.M.4    Trust, T.J.5
  • 32
    • 0037560879 scopus 로고    scopus 로고
    • Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori
    • Schirm, M., Soo, E., Aubry, A., Austin, J., Thibault, P., and Logan, S. (2003) Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori. Mol Microbiol 48: 1579-1592.
    • (2003) Mol Microbiol , vol.48 , pp. 1579-1592
    • Schirm, M.1    Soo, E.2    Aubry, A.3    Austin, J.4    Thibault, P.5    Logan, S.6
  • 33
    • 0032589796 scopus 로고    scopus 로고
    • Motility of Helicobacter pylori is coordinately regulated by the transcriptional activator FlgR, an NtrC homolog
    • Spohn, G., and Scarlato, V. (1999) Motility of Helicobacter pylori is coordinately regulated by the transcriptional activator FlgR, an NtrC homolog. J Bacteriol 131: 593-599.
    • (1999) J Bacteriol , vol.131 , pp. 593-599
    • Spohn, G.1    Scarlato, V.2
  • 34
    • 0028840449 scopus 로고
    • Meningococcal pilin: A glycoprotein substituted with digalactosyl 2,4-diacetamido-2,4,6-trideoxyhexose
    • Stimson, E., Virji, M., Makepeace, K., Dell, A., Morris, H.R., Payne, G., et al. (1995) Meningococcal pilin: a glycoprotein substituted with digalactosyl 2,4-diacetamido-2,4,6-trideoxyhexose. Mol Microbiol 17: 1201-1214.
    • (1995) Mol Microbiol , vol.17 , pp. 1201-1214
    • Stimson, E.1    Virji, M.2    Makepeace, K.3    Dell, A.4    Morris, H.R.5    Payne, G.6
  • 35
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • Szymanski, C.M., Yao, R., Ewing, C.P., Trust, T.J., and Guerry, P. (1999) Evidence for a system of general protein glycosylation in Campylobacter jejuni. Mol Microbiol 32: 1022-1030.
    • (1999) Mol Microbiol , vol.32 , pp. 1022-1030
    • Szymanski, C.M.1    Yao, R.2    Ewing, C.P.3    Trust, T.J.4    Guerry, P.5
  • 36
    • 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., and Guerry, P. (2001) Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin. J Biol Chem 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
  • 37
    • 0011928107 scopus 로고    scopus 로고
    • N-linked glycoyslation in Campylobacter jejuni and its functional transfer into E. coli
    • Wacker, M., Linton, D., Hitchen, P.G., Nita-Lazar, M., Haslam, S.M., North, S.J., et al. (2002) N-linked glycoyslation in Campylobacter jejuni and its functional transfer into E. coli. Science 298: 1790-1793.
    • (2002) Science , vol.298 , pp. 1790-1793
    • Wacker, M.1    Linton, D.2    Hitchen, P.G.3    Nita-Lazar, M.4    Haslam, S.M.5    North, S.J.6
  • 38
    • 0027327182 scopus 로고
    • Construction of new Campylobacter jejuni cloning vectors and a new mutational cat cassette
    • Yao, R., Alm, R.A., Trust, T.J., and Guerry, P. (1993) Construction of new Campylobacter jejuni cloning vectors and a new mutational cat cassette. Gene 130: 127-130.
    • (1993) Gene , vol.130 , pp. 127-130
    • Yao, R.1    Alm, R.A.2    Trust, T.J.3    Guerry, P.4
  • 39
    • 0037044765 scopus 로고    scopus 로고
    • Structure of the N-linked glycan present on multiple glycoproteins in the gram-negative bacterium, Campylobacter jejuni
    • Young, N.M., Brisson, J.-R., Kelly, J., Watson, D.C., Tessier, L., Lanthier, P.H., et al. (2002) Structure of the N-linked glycan present on multiple glycoproteins in the gram-negative bacterium, Campylobacter jejuni. J Biol Chem 277: 42530-42539.
    • (2002) J Biol Chem , vol.277 , pp. 42530-42539
    • Young, N.M.1    Brisson, J.-R.2    Kelly, J.3    Watson, D.C.4    Tessier, L.5    Lanthier, P.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.