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Volumn 93, Issue 5, 2014, Pages 957-974

Flagellar biosynthesis exerts temporal regulation of secretion of specific Campylobacter jejuni colonization and virulence determinants

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FLAGELLIN; PROTEIN CIAL; PROTEIN FEDB; PROTEIN FSPA1; RNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 84906938225     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12711     Document Type: Article
Times cited : (40)

References (84)
  • 1
    • 0035957518 scopus 로고    scopus 로고
    • Flagellin polymerisation control by a cytosolic export chaperone
    • Auvray, F., Thomas, J., Fraser, G.M., and Hughes, C. (2001) Flagellin polymerisation control by a cytosolic export chaperone. J Mol Biol 308: 221-229.
    • (2001) J Mol Biol , vol.308 , pp. 221-229
    • Auvray, F.1    Thomas, J.2    Fraser, G.M.3    Hughes, C.4
  • 2
    • 84855295481 scopus 로고    scopus 로고
    • Polar flagellar biosynthesis and a regulator of flagellar number influence spatial parameters of cell division in Campylobacter jejuni
    • Balaban, M., and Hendrixson, D.R. (2011) Polar flagellar biosynthesis and a regulator of flagellar number influence spatial parameters of cell division in Campylobacter jejuni. PLoS Pathog 7: e1002420.
    • (2011) PLoS Pathog , vol.7
    • Balaban, M.1    Hendrixson, D.R.2
  • 3
    • 77954920256 scopus 로고    scopus 로고
    • FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system
    • Bange, G., Kummerer, N., Engel, C., Bozkurt, G., Wild, K., and Sinning, I. (2010) FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system. Proc Natl Acad Sci USA 107: 11295-11300.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 11295-11300
    • Bange, G.1    Kummerer, N.2    Engel, C.3    Bozkurt, G.4    Wild, K.5    Sinning, I.6
  • 4
    • 84859440834 scopus 로고    scopus 로고
    • Identification and analysis of flagellar coexpressed determinants (Feds) of Campylobacter jejuni involved in colonization
    • Barrero-Tobon, A.M., and Hendrixson, D.R. (2012) Identification and analysis of flagellar coexpressed determinants (Feds) of Campylobacter jejuni involved in colonization. Mol Microbiol 84: 352-369.
    • (2012) Mol Microbiol , vol.84 , pp. 352-369
    • Barrero-Tobon, A.M.1    Hendrixson, D.R.2
  • 5
    • 0035133472 scopus 로고    scopus 로고
    • Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT
    • Bennett, J.C., Thomas, J., Fraser, G.M., and Hughes, C. (2001) Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT. Mol Microbiol 39: 781-791.
    • (2001) Mol Microbiol , vol.39 , pp. 781-791
    • Bennett, J.C.1    Thomas, J.2    Fraser, G.M.3    Hughes, C.4
  • 6
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • Birtalan, S.C., Phillips, R.M., and Ghosh, P. (2002) Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Mol Cell 9: 971-980.
    • (2002) Mol Cell , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 8
    • 84055200536 scopus 로고    scopus 로고
    • A specificity determinant for phosphorylation in a response regulator prevents in vivo cross-talk and modification by acetyl phosphate
    • Boll, J.M., and Hendrixson, D.R. (2011) A specificity determinant for phosphorylation in a response regulator prevents in vivo cross-talk and modification by acetyl phosphate. Proc Natl Acad Sci USA 108: 20160-20165.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 20160-20165
    • Boll, J.M.1    Hendrixson, D.R.2
  • 9
    • 79957464852 scopus 로고    scopus 로고
    • Campylobacter jejuni survival within human epithelial cells is enhanced by the secreted protein CiaI
    • Buelow, D.R., Christensen, J.E., Neal-McKinney, J.M., and Konkel, M.E. (2011) Campylobacter jejuni survival within human epithelial cells is enhanced by the secreted protein CiaI. Mol Microbiol 80: 1296-1312.
    • (2011) Mol Microbiol , vol.80 , pp. 1296-1312
    • Buelow, D.R.1    Christensen, J.E.2    Neal-McKinney, J.M.3    Konkel, M.E.4
  • 10
    • 84862556686 scopus 로고    scopus 로고
    • Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria
    • Buttner, D. (2012) Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria. Microbiol Mol Biol Rev 76: 262-310.
    • (2012) Microbiol Mol Biol Rev , vol.76 , pp. 262-310
    • Buttner, D.1
  • 11
    • 2442584516 scopus 로고    scopus 로고
    • Genome-wide expression analyses of Campylobacter jejuni NCTC11168 reveals coordinate regulation of motility and virulence by flhA
    • Carrillo, C.D., Taboada, E., Nash, J.H., Lanthier, P., Kelly, J., Lau, P.C., etal. (2004) Genome-wide expression analyses of Campylobacter jejuni NCTC11168 reveals coordinate regulation of motility and virulence by flhA. J Biol Chem 279: 20327-20338.
    • (2004) J Biol Chem , vol.279 , pp. 20327-20338
    • Carrillo, C.D.1    Taboada, E.2    Nash, J.H.3    Lanthier, P.4    Kelly, J.5    Lau, P.C.6
  • 13
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • Chevance, F.F., and Hughes, K.T. (2008) Coordinating assembly of a bacterial macromolecular machine. Nat Rev Microbiol 6: 455-465.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 455-465
    • Chevance, F.F.1    Hughes, K.T.2
  • 14
    • 70350181746 scopus 로고    scopus 로고
    • Identification of a Campylobacter jejuni-secreted protein required for maximal invasion of host cells
    • Christensen, J.E., Pacheco, S.A., and Konkel, M.E. (2009) Identification of a Campylobacter jejuni-secreted protein required for maximal invasion of host cells. Mol Microbiol 73: 650-662.
    • (2009) Mol Microbiol , vol.73 , pp. 650-662
    • Christensen, J.E.1    Pacheco, S.A.2    Konkel, M.E.3
  • 15
    • 0038460046 scopus 로고    scopus 로고
    • Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly
    • Claret, L., Calder, S.R., Higgins, M., and Hughes, C. (2003) Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly. Mol Microbiol 48: 1349-1355.
    • (2003) Mol Microbiol , vol.48 , pp. 1349-1355
    • Claret, L.1    Calder, S.R.2    Higgins, M.3    Hughes, C.4
  • 16
    • 84857874120 scopus 로고    scopus 로고
    • A new means to identify type 3 secreted effectors: functionally interchangeable class IB chaperones recognize a conserved sequence
    • e00243-e00211
    • Costa, S.C., Schmitz, A.M., Jahufar, F.F., Boyd, J.D., Cho, M.Y., Glicksman, M.A., and Lesser, C.F. (2012) A new means to identify type 3 secreted effectors: functionally interchangeable class IB chaperones recognize a conserved sequence. mBio 3: e00243-11.
    • (2012) mBio , vol.3
    • Costa, S.C.1    Schmitz, A.M.2    Jahufar, F.F.3    Boyd, J.D.4    Cho, M.Y.5    Glicksman, M.A.6    Lesser, C.F.7
  • 17
    • 75749149345 scopus 로고    scopus 로고
    • Application of a short, disordered N-terminal flagellin segment, a fully functional flagellar type III export signal, to expression of secreted proteins
    • Dobo, J., Varga, J., Sajo, R., Vegh, B.M., Gal, P., Zavodszky, P., and Vonderviszt, F. (2010) Application of a short, disordered N-terminal flagellin segment, a fully functional flagellar type III export signal, to expression of secreted proteins. Appl Environ Microbiol 76: 891-899.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 891-899
    • Dobo, J.1    Varga, J.2    Sajo, R.3    Vegh, B.M.4    Gal, P.5    Zavodszky, P.6    Vonderviszt, F.7
  • 18
    • 77349103262 scopus 로고    scopus 로고
    • The role of the FliK molecular ruler in hook-length control in Salmonella enterica
    • Erhardt, M., Hirano, T., Su, Y., Paul, K., Wee, D.H., Mizuno, S., etal. (2010) The role of the FliK molecular ruler in hook-length control in Salmonella enterica. Mol Microbiol 75: 1272-1284.
    • (2010) Mol Microbiol , vol.75 , pp. 1272-1284
    • Erhardt, M.1    Hirano, T.2    Su, Y.3    Paul, K.4    Wee, D.H.5    Mizuno, S.6
  • 19
    • 79960647596 scopus 로고    scopus 로고
    • An infrequent molecular ruler controls flagellar hook length in Salmonella enterica
    • Erhardt, M., Singer, H.M., Wee, D.H., Keener, J.P., and Hughes, K.T. (2011) An infrequent molecular ruler controls flagellar hook length in Salmonella enterica. EMBO J 30: 2948-2961.
    • (2011) EMBO J , vol.30 , pp. 2948-2961
    • Erhardt, M.1    Singer, H.M.2    Wee, D.H.3    Keener, J.P.4    Hughes, K.T.5
  • 20
    • 33751208041 scopus 로고    scopus 로고
    • An escort mechanism for cycling of export chaperones during flagellum assembly
    • Evans, L.D., Stafford, G.P., Ahmed, S., Fraser, G.M., and Hughes, C. (2006) An escort mechanism for cycling of export chaperones during flagellum assembly. Proc Natl Acad Sci USA 103: 17474-17479.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17474-17479
    • Evans, L.D.1    Stafford, G.P.2    Ahmed, S.3    Fraser, G.M.4    Hughes, C.5
  • 22
    • 0141618445 scopus 로고    scopus 로고
    • Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion
    • Evdokimov, A.G., Phan, J., Tropea, J.E., Routzahn, K.M., Peters, H.K., Pokross, M., and Waugh, D.S. (2003) Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion. Nat Struct Biol 10: 789-793.
    • (2003) Nat Struct Biol , vol.10 , pp. 789-793
    • Evdokimov, A.G.1    Phan, J.2    Tropea, J.E.3    Routzahn, K.M.4    Peters, H.K.5    Pokross, M.6    Waugh, D.S.7
  • 24
    • 0032906245 scopus 로고    scopus 로고
    • Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly
    • Fraser, G.M., Bennett, J.C., and Hughes, C. (1999) Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly. Mol Microbiol 32: 569-580.
    • (1999) Mol Microbiol , vol.32 , pp. 569-580
    • Fraser, G.M.1    Bennett, J.C.2    Hughes, C.3
  • 25
    • 0038016732 scopus 로고    scopus 로고
    • Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhB
    • Fraser, G.M., Hirano, T., Ferris, H.U., Devgan, L.L., Kihara, M., and Macnab, R.M. (2003) Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhB. Mol Microbiol 48: 1043-1057.
    • (2003) Mol Microbiol , vol.48 , pp. 1043-1057
    • Fraser, G.M.1    Hirano, T.2    Ferris, H.U.3    Devgan, L.L.4    Kihara, M.5    Macnab, R.M.6
  • 26
    • 0036128480 scopus 로고    scopus 로고
    • Identification of motility and autoagglutination Campylobacter jejuni mutants by random transposon mutagenesis
    • Golden, N.J., and Acheson, D.W. (2002) Identification of motility and autoagglutination Campylobacter jejuni mutants by random transposon mutagenesis. Infect Immun 70: 1761-1771.
    • (2002) Infect Immun , vol.70 , pp. 1761-1771
    • Golden, N.J.1    Acheson, D.W.2
  • 27
    • 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., and Guerry, P. (2003) Pseudaminic acid, the major modification on Campylobacter flagellin, is synthesized via the Cj1293 gene. Mol Microbiol 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
  • 29
    • 0027190409 scopus 로고
    • Role of flagella in adherence, internalization, and translocation of Campylobacter jejuni in nonpolarized and polarized epithelial cell cultures
    • Grant, C.C.R., Konkel, M.E., Cieplak, W., Jr, and Tompkins, L.S. (1993) Role of flagella in adherence, internalization, and translocation of Campylobacter jejuni in nonpolarized and polarized epithelial cell cultures. Infect Immun 61: 1764-1771.
    • (1993) Infect Immun , vol.61 , pp. 1764-1771
    • Grant, C.C.R.1    Konkel, M.E.2    Cieplak Jr., W.3    Tompkins, L.S.4
  • 30
    • 33748503644 scopus 로고    scopus 로고
    • A phase-variable mechanism controlling the Campylobacter jejuni FlgR response regulator influences commensalism
    • Hendrixson, D.R. (2006) A phase-variable mechanism controlling the Campylobacter jejuni FlgR response regulator influences commensalism. Mol Microbiol 61: 1646-1659.
    • (2006) Mol Microbiol , vol.61 , pp. 1646-1659
    • Hendrixson, D.R.1
  • 31
    • 52649180089 scopus 로고    scopus 로고
    • Restoration of flagellar biosynthesis by varied mutational events in Campylobacter jejuni
    • Hendrixson, D.R. (2008) Restoration of flagellar biosynthesis by varied mutational events in Campylobacter jejuni. Mol Microbiol 70: 519-536.
    • (2008) Mol Microbiol , vol.70 , pp. 519-536
    • Hendrixson, D.R.1
  • 32
    • 0142125272 scopus 로고    scopus 로고
    • 28-dependent flagellar genes in Campylobacter jejuni is associated with formation of the flagellar secretory apparatus
    • 28-dependent flagellar genes in Campylobacter jejuni is associated with formation of the flagellar secretory apparatus. Mol Microbiol 50: 687-702.
    • (2003) Mol Microbiol , vol.50 , pp. 687-702
    • Hendrixson, D.R.1    DiRita, V.J.2
  • 33
    • 1942532926 scopus 로고    scopus 로고
    • Identification of Campylobacter jejuni genes involved in commensal colonization of the chick gastrointestinal tract
    • Hendrixson, D.R., and DiRita, V.J. (2004) Identification of Campylobacter jejuni genes involved in commensal colonization of the chick gastrointestinal tract. Mol Microbiol 52: 471-484.
    • (2004) Mol Microbiol , vol.52 , pp. 471-484
    • Hendrixson, D.R.1    DiRita, V.J.2
  • 34
    • 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
  • 35
    • 0001823786 scopus 로고
    • Recombinant PCR
    • Innis, M.A., Gelfand, D.H., Sninsky, J.J., and White, T.J. (eds). London: Academic Press
    • Higuchi, R. (1990) Recombinant PCR. In PCR Protocols: A Guide to Methods and Applications. Innis, M.A., Gelfand, D.H., Sninsky, J.J., and White, T.J. (eds). London: Academic Press, pp. 77-183.
    • (1990) PCR Protocols: A Guide to Methods and Applications , pp. 77-183
    • Higuchi, R.1
  • 36
    • 0021159373 scopus 로고
    • Excretion of unassembled flagellin by Salmonella typhimurium mutants deficient in hook-associated proteins
    • Homma, M., Fujita, H., Yamaguchi, S., and Iino, T. (1984) Excretion of unassembled flagellin by Salmonella typhimurium mutants deficient in hook-associated proteins. J Bacteriol 159: 1056-1059.
    • (1984) J Bacteriol , vol.159 , pp. 1056-1059
    • Homma, M.1    Fujita, H.2    Yamaguchi, S.3    Iino, T.4
  • 37
    • 0035110827 scopus 로고    scopus 로고
    • Intergenic suppression between the flagellar MS ring protein FliF of Salmonella and FlhA, a membrane component of its export apparatus
    • Kihara, M., Minamino, T., Yamaguchi, S., and Macnab, R.M. (2001) Intergenic suppression between the flagellar MS ring protein FliF of Salmonella and FlhA, a membrane component of its export apparatus. J Bacteriol 183: 1655-1662.
    • (2001) J Bacteriol , vol.183 , pp. 1655-1662
    • Kihara, M.1    Minamino, T.2    Yamaguchi, S.3    Macnab, R.M.4
  • 38
    • 0033016809 scopus 로고    scopus 로고
    • Bacterial secreted proteins are required for the internaliztion of Campylobacter jejuni into cultured mammalian cells
    • Konkel, M.E., Kim, B.J., Rivera-Amill, V., and Garvis, S.G. (1999) Bacterial secreted proteins are required for the internaliztion of Campylobacter jejuni into cultured mammalian cells. Mol Microbiol 32: 691-701.
    • (1999) Mol Microbiol , vol.32 , pp. 691-701
    • Konkel, M.E.1    Kim, B.J.2    Rivera-Amill, V.3    Garvis, S.G.4
  • 39
    • 2442705402 scopus 로고    scopus 로고
    • Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus
    • Konkel, M.E., Klena, J.D., Rivera-Amill, V., Monteville, M.R., Biswas, D., Raphael, B., and Mickelson, J. (2004) Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus. J Bacteriol 186: 3296-3303.
    • (2004) J Bacteriol , vol.186 , pp. 3296-3303
    • Konkel, M.E.1    Klena, J.D.2    Rivera-Amill, V.3    Monteville, M.R.4    Biswas, D.5    Raphael, B.6    Mickelson, J.7
  • 40
    • 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
  • 41
    • 2142787652 scopus 로고
    • Export of an N-terminal fragment of Escherichia coli flagellin by a flagellum-specific pathway
    • Kuwajima, G., Kawagishi, I., Homma, M., Asaka, J., Kondo, E., and Macnab, R.M. (1989) Export of an N-terminal fragment of Escherichia coli flagellin by a flagellum-specific pathway. Proc Natl Acad Sci USA 86: 4953-4957.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4953-4957
    • Kuwajima, G.1    Kawagishi, I.2    Homma, M.3    Asaka, J.4    Kondo, E.5    Macnab, R.M.6
  • 42
    • 0032755489 scopus 로고    scopus 로고
    • Evaluation of a truncated recombinant flagellin subunit vaccine against Campylobacter jejuni
    • Lee, L.H., Burg, E., 3rd, Baqar, S., Bourgeois, A.L., Burr, D.H., Ewing, C.P., etal. (1999) Evaluation of a truncated recombinant flagellin subunit vaccine against Campylobacter jejuni. Infect Immun 67: 5799-5805.
    • (1999) Infect Immun , vol.67 , pp. 5799-5805
    • Lee, L.H.1    Burg III, E.2    Baqar, S.3    Bourgeois, A.L.4    Burr, D.H.5    Ewing, C.P.6
  • 43
    • 79955733488 scopus 로고    scopus 로고
    • Assembly and stability of flagellar motor in Escherichia coli
    • Li, H., and Sourjik, V. (2011) Assembly and stability of flagellar motor in Escherichia coli. Mol Microbiol 80: 886-899.
    • (2011) Mol Microbiol , vol.80 , pp. 886-899
    • Li, H.1    Sourjik, V.2
  • 44
    • 33344459126 scopus 로고    scopus 로고
    • A common structural motif in the binding of virulence factors to bacterial secretion chaperones
    • Lilic, M., Vujanac, M., and Stebbins, C.E. (2006) A common structural motif in the binding of virulence factors to bacterial secretion chaperones. Mol Cell 21: 653-664.
    • (2006) Mol Cell , vol.21 , pp. 653-664
    • Lilic, M.1    Vujanac, M.2    Stebbins, C.E.3
  • 45
    • 84861216612 scopus 로고    scopus 로고
    • Quantitative proteomics of intracellular Campylobacter jejuni reveals metabolic reprogramming
    • Liu, X., Gao, B., Novik, V., and Galan, J.E. (2012) Quantitative proteomics of intracellular Campylobacter jejuni reveals metabolic reprogramming. PLoS Pathog 8: e1002562.
    • (2012) PLoS Pathog , vol.8
    • Liu, X.1    Gao, B.2    Novik, V.3    Galan, J.E.4
  • 46
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab, R.M. (2003) How bacteria assemble flagella. Annu Rev Microbiol 57: 77-100.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 47
    • 0033729426 scopus 로고    scopus 로고
    • Generation of deletion and point mutations with one primer in a single cloning step
    • Makarova, O., Kamberov, E., and Margolis, B. (2000) Generation of deletion and point mutations with one primer in a single cloning step. Biotechniques 29: 970-972.
    • (2000) Biotechniques , vol.29 , pp. 970-972
    • Makarova, O.1    Kamberov, E.2    Margolis, B.3
  • 48
    • 41549097842 scopus 로고    scopus 로고
    • Culture of Campylobacter jejuni with sodium deoxycholate induces virulence gene expression
    • Malik-Kale, P., Parker, C.T., and Konkel, M.E. (2008) Culture of Campylobacter jejuni with sodium deoxycholate induces virulence gene expression. J Bacteriol 190: 2286-2297.
    • (2008) J Bacteriol , vol.190 , pp. 2286-2297
    • Malik-Kale, P.1    Parker, C.T.2    Konkel, M.E.3
  • 49
    • 2642559479 scopus 로고    scopus 로고
    • Self-assembly and type III protein export of the bacterial flagellum
    • Minamino, T., and Namba, K. (2004) Self-assembly and type III protein export of the bacterial flagellum. J Mol Microbiol Biotechnol 7: 5-17.
    • (2004) J Mol Microbiol Biotechnol , vol.7 , pp. 5-17
    • Minamino, T.1    Namba, K.2
  • 50
    • 0033924918 scopus 로고    scopus 로고
    • Role of FliJ in flagellar protein export in Salmonella
    • Minamino, T., Chu, R., Yamaguchi, S., and Macnab, R.M. (2000) Role of FliJ in flagellar protein export in Salmonella. J Bacteriol 182: 4207-4215.
    • (2000) J Bacteriol , vol.182 , pp. 4207-4215
    • Minamino, T.1    Chu, R.2    Yamaguchi, S.3    Macnab, R.M.4
  • 51
    • 58149347646 scopus 로고    scopus 로고
    • Mechanisms of type III protein export for bacterial flagellar assembly
    • Minamino, T., Imada, K., and Namba, K. (2008) Mechanisms of type III protein export for bacterial flagellar assembly. Mol Biosyst 4: 1105-1115.
    • (2008) Mol Biosyst , vol.4 , pp. 1105-1115
    • Minamino, T.1    Imada, K.2    Namba, K.3
  • 52
    • 70350180743 scopus 로고    scopus 로고
    • Interaction of FliK with the bacterial flagellar hook is required for efficient export specificity switching
    • Minamino, T., Moriya, N., Hirano, T., Hughes, K.T., and Namba, K. (2009) Interaction of FliK with the bacterial flagellar hook is required for efficient export specificity switching. Mol Microbiol 74: 239-251.
    • (2009) Mol Microbiol , vol.74 , pp. 239-251
    • Minamino, T.1    Moriya, N.2    Hirano, T.3    Hughes, K.T.4    Namba, K.5
  • 53
    • 84896702974 scopus 로고    scopus 로고
    • Assembly and stoichiometry of FliF and FlhA in Salmonella flagellar basal body
    • Morimoto, Y.V., Ito, M., Hiraoka, K.D., Che, Y.S., Bai, F., Kami-Ike, N., etal. (2014) Assembly and stoichiometry of FliF and FlhA in Salmonella flagellar basal body. Mol Microbiol 91: 1214-1226.
    • (2014) Mol Microbiol , vol.91 , pp. 1214-1226
    • Morimoto, Y.V.1    Ito, M.2    Hiraoka, K.D.3    Che, Y.S.4    Bai, F.5    Kami-Ike, N.6
  • 54
    • 80053998875 scopus 로고    scopus 로고
    • CsrA-FliW interaction governs flagellin homeostasis and a checkpoint on flagellar morphogenesis in Bacillus subtilis
    • Mukherjee, S., Yakhnin, H., Kysela, D., Sokoloski, J., Babitzke, P., and Kearns, D.B. (2011) CsrA-FliW interaction governs flagellin homeostasis and a checkpoint on flagellar morphogenesis in Bacillus subtilis. Mol Microbiol 82: 447-461.
    • (2011) Mol Microbiol , vol.82 , pp. 447-461
    • Mukherjee, S.1    Yakhnin, H.2    Kysela, D.3    Sokoloski, J.4    Babitzke, P.5    Kearns, D.B.6
  • 55
    • 84872168146 scopus 로고    scopus 로고
    • FliW and FliS function independently to control cytoplasmic flagellin levels in Bacillus subtilis
    • Mukherjee, S., Babitzke, P., and Kearns, D.B. (2013) FliW and FliS function independently to control cytoplasmic flagellin levels in Bacillus subtilis. J Bacteriol 195: 297-306.
    • (2013) J Bacteriol , vol.195 , pp. 297-306
    • Mukherjee, S.1    Babitzke, P.2    Kearns, D.B.3
  • 57
    • 0027287847 scopus 로고
    • Role of Campylobacter jejuni flagella as colonization factors for three-day-old chicks: analysis with flagellar mutants
    • Nachamkin, I., Yang, X.-H., and Stern, N.J. (1993) Role of Campylobacter jejuni flagella as colonization factors for three-day-old chicks: analysis with flagellar mutants. Appl Environ Microbiol 59: 1269-1273.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 1269-1273
    • Nachamkin, I.1    Yang, X.-H.2    Stern, N.J.3
  • 58
    • 84884137964 scopus 로고    scopus 로고
    • The Campylobacter jejuni CiaC virulence protein is secreted from the flagellum and delivered to the cytosol of host cells
    • Neal-McKinney, J.M., and Konkel, M.E. (2012) The Campylobacter jejuni CiaC virulence protein is secreted from the flagellum and delivered to the cytosol of host cells. Front Cell Infect Microbiol 2: 31.
    • (2012) Front Cell Infect Microbiol , vol.2 , pp. 31
    • Neal-McKinney, J.M.1    Konkel, M.E.2
  • 59
    • 77952184560 scopus 로고    scopus 로고
    • Amino-terminal residues dictate the export efficiency of the Campylobacter jejuni filament proteins via the flagellum
    • Neal-McKinney, J.M., Christensen, J.E., and Konkel, M.E. (2010) Amino-terminal residues dictate the export efficiency of the Campylobacter jejuni filament proteins via the flagellum. Mol Microbiol 76: 918-931.
    • (2010) Mol Microbiol , vol.76 , pp. 918-931
    • Neal-McKinney, J.M.1    Christensen, J.E.2    Konkel, M.E.3
  • 60
    • 77955294240 scopus 로고    scopus 로고
    • Identification of Campylobacter jejuni genes involved in its interaction with epithelial cells
    • Novik, V., Hofreuter, D., and Galan, J.E. (2010) Identification of Campylobacter jejuni genes involved in its interaction with epithelial cells. Infect Immun 78: 3540-3553.
    • (2010) Infect Immun , vol.78 , pp. 3540-3553
    • Novik, V.1    Hofreuter, D.2    Galan, J.E.3
  • 61
    • 0025083724 scopus 로고
    • Structural and functional analysis of two Campylobacter jejuni flagellin genes
    • Nuijten, P.J., van Asten, F.J., Gaastra, W., and van der Zeijst, B.A. (1990) Structural and functional analysis of two Campylobacter jejuni flagellin genes. J Biol Chem 265: 17798-17804.
    • (1990) J Biol Chem , vol.265 , pp. 17798-17804
    • Nuijten, P.J.1    van Asten, F.J.2    Gaastra, W.3    van der Zeijst, B.A.4
  • 62
    • 34547617364 scopus 로고    scopus 로고
    • Heterogeneity of a Campylobacter jejuni protein that is secreted through the flagellar filament
    • Poly, F., Ewing, C., Goon, S., Hickey, T.E., Rockabrand, D., Majam, G., etal. (2007) Heterogeneity of a Campylobacter jejuni protein that is secreted through the flagellar filament. Infect Immun 75: 3859-3867.
    • (2007) Infect Immun , vol.75 , pp. 3859-3867
    • Poly, F.1    Ewing, C.2    Goon, S.3    Hickey, T.E.4    Rockabrand, D.5    Majam, G.6
  • 63
    • 77949697432 scopus 로고    scopus 로고
    • Functional analysis of the RdxA and RdxB nitroreductases of Campylobacter jejuni reveals that mutations in rdxA confer metronidazole resistance
    • Ribardo, D.A., Bingham-Ramos, L.K., and Hendrixson, D.R. (2010) Functional analysis of the RdxA and RdxB nitroreductases of Campylobacter jejuni reveals that mutations in rdxA confer metronidazole resistance. J Bacteriol 192: 1890-1901.
    • (2010) J Bacteriol , vol.192 , pp. 1890-1901
    • Ribardo, D.A.1    Bingham-Ramos, L.K.2    Hendrixson, D.R.3
  • 64
    • 0035370231 scopus 로고    scopus 로고
    • Secretion of the virulence-associated Campylobacter invasion antigens from Campylobacter jejuni requires a stimulatory signal
    • Rivera-Amill, V., Kim, B.J., Seshu, J., and Konkel, M.E. (2001) Secretion of the virulence-associated Campylobacter invasion antigens from Campylobacter jejuni requires a stimulatory signal. J Infect Dis 183: 1607-1616.
    • (2001) J Infect Dis , vol.183 , pp. 1607-1616
    • Rivera-Amill, V.1    Kim, B.J.2    Seshu, J.3    Konkel, M.E.4
  • 65
    • 84886743358 scopus 로고    scopus 로고
    • Serine phosphorylation of cortactin is required for maximal host cell invasion by Campylobacter jejuni
    • Samuelson, D.R., and Konkel, M.E. (2013) Serine phosphorylation of cortactin is required for maximal host cell invasion by Campylobacter jejuni. Cell Commun Signal 11: 82.
    • (2013) Cell Commun Signal , vol.11 , pp. 82
    • Samuelson, D.R.1    Konkel, M.E.2
  • 66
    • 84885743984 scopus 로고    scopus 로고
    • The Campylobacter jejuni CiaD effector protein activates MAP kinase signaling pathways and is required for the development of disease
    • Samuelson, D.R., Eucker, T.P., Bell, J.A., Dybas, L., Mansfield, L.S., and Konkel, M.E. (2013) The Campylobacter jejuni CiaD effector protein activates MAP kinase signaling pathways and is required for the development of disease. Cell Commun Signal 11: 79.
    • (2013) Cell Commun Signal , vol.11 , pp. 79
    • Samuelson, D.R.1    Eucker, T.P.2    Bell, J.A.3    Dybas, L.4    Mansfield, L.S.5    Konkel, M.E.6
  • 67
    • 0031872389 scopus 로고    scopus 로고
    • Phospholipase A of Yersinia enterocolitica contributes to pathogenesis in a mouse model
    • Schmiel, D.H., Wagar, E., Karamanou, L., Weeks, D., and Miller, V.L. (1998) Phospholipase A of Yersinia enterocolitica contributes to pathogenesis in a mouse model. Infect Immun 66: 3941-3951.
    • (1998) Infect Immun , vol.66 , pp. 3941-3951
    • Schmiel, D.H.1    Wagar, E.2    Karamanou, L.3    Weeks, D.4    Miller, V.L.5
  • 68
    • 33845956897 scopus 로고    scopus 로고
    • Analysis of the roles of FlgP and FlgQ in flagellar motility of Campylobacter jejuni
    • Sommerlad, S.M., and Hendrixson, D.R. (2007) Analysis of the roles of FlgP and FlgQ in flagellar motility of Campylobacter jejuni. J Bacteriol 189: 179-186.
    • (2007) J Bacteriol , vol.189 , pp. 179-186
    • Sommerlad, S.M.1    Hendrixson, D.R.2
  • 69
    • 0021998499 scopus 로고
    • Campylobacter colitis: histological immunohistochemical and ultrastructural findings
    • van Spreeuwel, J.P., Duursma, G.C., Meijer, C.J., Bax, R., Rosekrans, P.C., and Lindeman, J. (1985) Campylobacter colitis: histological immunohistochemical and ultrastructural findings. Gut 26: 945-951.
    • (1985) Gut , vol.26 , pp. 945-951
    • van Spreeuwel, J.P.1    Duursma, G.C.2    Meijer, C.J.3    Bax, R.4    Rosekrans, P.C.5    Lindeman, J.6
  • 70
    • 35748929649 scopus 로고    scopus 로고
    • Sorting of early and late flagellar subunits after docking at the membrane ATPase of the type III export pathway
    • Stafford, G.P., Evans, L.D., Krumscheid, R., Dhillon, P., Fraser, G.M., and Hughes, C. (2007) Sorting of early and late flagellar subunits after docking at the membrane ATPase of the type III export pathway. J Mol Biol 374: 877-882.
    • (2007) J Mol Biol , vol.374 , pp. 877-882
    • Stafford, G.P.1    Evans, L.D.2    Krumscheid, R.3    Dhillon, P.4    Fraser, G.M.5    Hughes, C.6
  • 71
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins, C.E., and Galan, J.E. (2001) Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 414: 77-81.
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 72
    • 1642305413 scopus 로고    scopus 로고
    • Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export
    • Thomas, J., Stafford, G.P., and Hughes, C. (2004) Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export. Proc Natl Acad Sci USA 101: 3945-3950.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3945-3950
    • Thomas, J.1    Stafford, G.P.2    Hughes, C.3
  • 73
    • 33750461658 scopus 로고    scopus 로고
    • Novel conserved assembly factor of the bacterial flagellum
    • Titz, B., Rajagopala, S.V., Ester, C., Hauser, R., and Uetz, P. (2006) Novel conserved assembly factor of the bacterial flagellum. J Bacteriol 188: 7700-7706.
    • (2006) J Bacteriol , vol.188 , pp. 7700-7706
    • Titz, B.1    Rajagopala, S.V.2    Ester, C.3    Hauser, R.4    Uetz, P.5
  • 74
    • 33745804572 scopus 로고    scopus 로고
    • Localization of the flagellum-specific secretion signal in Salmonella flagellin
    • Vegh, B.M., Gal, P., Dobo, J., Zavodszky, P., and Vonderviszt, F. (2006) Localization of the flagellum-specific secretion signal in Salmonella flagellin. Biochem Biophys Res Commun 345: 93-98.
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 93-98
    • Vegh, B.M.1    Gal, P.2    Dobo, J.3    Zavodszky, P.4    Vonderviszt, F.5
  • 75
    • 24344494379 scopus 로고    scopus 로고
    • An amino-terminal secretion signal is required for YplA export by the Ysa, Ysc, and flagellar type III secretion systems of Yersinia enterocolitica biovar 1B
    • Warren, S.M., and Young, G.M. (2005) An amino-terminal secretion signal is required for YplA export by the Ysa, Ysc, and flagellar type III secretion systems of Yersinia enterocolitica biovar 1B. J Bacteriol 187: 6075-6083.
    • (2005) J Bacteriol , vol.187 , pp. 6075-6083
    • Warren, S.M.1    Young, G.M.2
  • 76
    • 0025911942 scopus 로고
    • Inactivation of Campylobacter jejuni flagellin genes by homologous recombination demonstrates that flaA but not flaB is required for invasion
    • Wassenaar, T.M., Bleumink-Pluym, N.M.C., and van der Zeijst, B.A.M. (1991) Inactivation of Campylobacter jejuni flagellin genes by homologous recombination demonstrates that flaA but not flaB is required for invasion. EMBO J 10: 2055-2061.
    • (1991) EMBO J , vol.10 , pp. 2055-2061
    • Wassenaar, T.M.1    Bleumink-Pluym, N.M.C.2    van der Zeijst, B.A.M.3
  • 77
    • 0027234632 scopus 로고
    • Colonization of chicks by motility mutants of Campylobacter jejuni demonstrates the importance of flagellin A expression
    • Wassenaar, T.M., van der Zeijst, B.A.M., Ayling, R., and Newell, D.G. (1993) Colonization of chicks by motility mutants of Campylobacter jejuni demonstrates the importance of flagellin A expression. J Gen Microbiol 139: 1171-1175.
    • (1993) J Gen Microbiol , vol.139 , pp. 1171-1175
    • Wassenaar, T.M.1    van der Zeijst, B.A.M.2    Ayling, R.3    Newell, D.G.4
  • 79
    • 38949103470 scopus 로고    scopus 로고
    • Campylobacter jejuni survives within epithelial cells by avoiding delivery to lysosomes
    • Watson, R.O., and Galan, J.E. (2008) Campylobacter jejuni survives within epithelial cells by avoiding delivery to lysosomes. PLoS Pathog 4: e14.
    • (2008) PLoS Pathog , vol.4
    • Watson, R.O.1    Galan, J.E.2
  • 80
    • 1942533529 scopus 로고    scopus 로고
    • The FlgS/FlgR two-component signal transduction system regulates the fla regulon in Campylobacter jejuni
    • Wosten, M.M.S.M., Wagenaar, J.A., and van Putten, J.P.M. (2004) The FlgS/FlgR two-component signal transduction system regulates the fla regulon in Campylobacter jejuni. J Biol Chem 279: 16214-16222.
    • (2004) J Biol Chem , vol.279 , pp. 16214-16222
    • Wosten, M.M.S.M.1    Wagenaar, J.A.2    van Putten, J.P.M.3
  • 81
    • 0028073696 scopus 로고
    • Isolation of motile and non-motile insertional mutants of Campylobacter jejuni: the role of motility in adherence and invasion of eukaryotic cells
    • Yao, R., Burr, D.H., Doig, P., Trust, T.J., Niu, H., and Guerry, P. (1994) Isolation of motile and non-motile insertional mutants of Campylobacter jejuni: the role of motility in adherence and invasion of eukaryotic cells. Mol Microbiol 14: 883-893.
    • (1994) Mol Microbiol , vol.14 , pp. 883-893
    • Yao, R.1    Burr, D.H.2    Doig, P.3    Trust, T.J.4    Niu, H.5    Guerry, P.6
  • 82
    • 0029118564 scopus 로고
    • Functional analysis of the flagellar genes in the fliD operon of Salmonella typhimurium
    • Yokoseki, T., Kutsukake, K., Ohnishi, K., and Iino, T. (1995) Functional analysis of the flagellar genes in the fliD operon of Salmonella typhimurium. Microbiology 141 (Part 7): 1715-1722.
    • (1995) Microbiology , vol.141 , Issue.PART 7 , pp. 1715-1722
    • Yokoseki, T.1    Kutsukake, K.2    Ohnishi, K.3    Iino, T.4
  • 83
    • 0036008317 scopus 로고    scopus 로고
    • YplA is exported by the Ysc, Ysa, and flagellar type III secretion systems of Yersinia enterocolitica
    • Young, B.M., and Young, G.M. (2002) YplA is exported by the Ysc, Ysa, and flagellar type III secretion systems of Yersinia enterocolitica. J Bacteriol 184: 1324-1334.
    • (2002) J Bacteriol , vol.184 , pp. 1324-1334
    • Young, B.M.1    Young, G.M.2
  • 84
    • 0033033304 scopus 로고    scopus 로고
    • A new pathway for the secretion of virulence factors by bacteria: the flagellar export apparatus functions as a protein-secretion system
    • Young, G.M., Schmiel, D.H., and Miller, V.L. (1999) A new pathway for the secretion of virulence factors by bacteria: the flagellar export apparatus functions as a protein-secretion system. Proc Natl Acad Sci USA 96: 6456-6461.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6456-6461
    • Young, G.M.1    Schmiel, D.H.2    Miller, V.L.3


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