메뉴 건너뛰기




Volumn 195, Issue 12, 2013, Pages 2718-2727

Secretion of TcpF by the Vibrio cholerae toxin-coregulated pilus biogenesis apparatus requires an N-terminal determinant

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHOLERA TOXIN; PILIN; TCPF PROTEIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 84880011506     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01122-12     Document Type: Article
Times cited : (10)

References (56)
  • 1
    • 33947620478 scopus 로고    scopus 로고
    • Targeting bacterial secretion systems: benefits of disarmament in the microcosm
    • Baron C, Coombes B. 2007. Targeting bacterial secretion systems: benefits of disarmament in the microcosm. Infect. Disord. Drug Targets 7:19 -27.
    • (2007) Infect. Disord. Drug Targets , vol.7
    • Baron, C.1    Coombes, B.2
  • 2
    • 50049122412 scopus 로고    scopus 로고
    • Towards a systems biology approach to study type II/IV secretion systems
    • Hazes B, Frost L. 2008. Towards a systems biology approach to study type II/IV secretion systems. Biochim. Biophys. Acta 1778:1839 -1850.
    • (2008) Biochim. Biophys. Acta , vol.1778
    • Hazes, B.1    Frost, L.2
  • 4
    • 70350734524 scopus 로고    scopus 로고
    • Imaging the assembly, structure and activity of type III secretion systems
    • Enninga J, Rosenshine I. 2009. Imaging the assembly, structure and activity of type III secretion systems. Cell. Microbiol. 11:1462-1470.
    • (2009) Cell. Microbiol. , vol.11 , pp. 1462-1470
    • Enninga, J.1    Rosenshine, I.2
  • 6
    • 0027489247 scopus 로고
    • Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and proteinsecretion apparatus: a general system for the formation of surfaceassociated protein complexes
    • Hobbs M, Mattick JS. 1993. Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and proteinsecretion apparatus: a general system for the formation of surfaceassociated protein complexes. Mol. Microbiol. 10:233-243.
    • (1993) Mol. Microbiol. , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, J.S.2
  • 9
    • 0035029580 scopus 로고    scopus 로고
    • Biology of type II secretion
    • Sandkvist M. 2001. Biology of type II secretion. Mol. Microbiol. 40:271- 283.
    • (2001) Mol. Microbiol. , vol.40
    • Sandkvist, M.1
  • 11
    • 33747872707 scopus 로고    scopus 로고
    • Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions
    • Craig L, Volkmann N, Arvai AS, Pique ME, Yeager M, Egelman EH, Tainer JA. 2006. Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions. Mol. Cell 23:651- 662.
    • (2006) Mol. Cell , vol.23
    • Craig, L.1    Volkmann, N.2    Arvai, A.S.3    Pique, M.E.4    Yeager, M.5    Egelman, E.H.6    Tainer, J.A.7
  • 13
    • 63049092517 scopus 로고    scopus 로고
    • Organization and PprB-dependent control of the Pseudomonas aeruginosa tad locus, involved in Flp pilus biology
    • Bernard CS, Bordi C, Termine E, Filloux A, de Bentzmann S. 2009. Organization and PprB-dependent control of the Pseudomonas aeruginosa tad locus, involved in Flp pilus biology. J. Bacteriol. 191:1961-1973.
    • (2009) J. Bacteriol. , vol.191 , pp. 1961-1973
    • Bernard, C.S.1    Bordi, C.2    Termine, E.3    Filloux, A.4    de Bentzmann, S.5
  • 14
    • 0034999675 scopus 로고    scopus 로고
    • flp-1, the first representative of a new pilin gene subfamily, is required for nonspecific adherence of Actinobacillus actinomycetemcomitans
    • Kachlany SC, Planet PJ, Desalle R, Fine DH, Figurski DH, Kaplan JB. 2001. flp-1, the first representative of a new pilin gene subfamily, is required for nonspecific adherence of Actinobacillus actinomycetemcomitans. Mol. Microbiol. 40:542-554.
    • (2001) Mol. Microbiol. , vol.40 , pp. 542-554
    • Kachlany, S.C.1    Planet, P.J.2    Desalle, R.3    Fine, D.H.4    Figurski, D.H.5    Kaplan, J.B.6
  • 17
    • 77951630652 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa minor pilins are incorporated into type IV pili
    • Giltner CL, Habash M, Burrows LL. 2010. Pseudomonas aeruginosa minor pilins are incorporated into type IV pili. J. Mol. Biol. 398:444-461.
    • (2010) J. Mol. Biol. , vol.398 , pp. 444-461
    • Giltner, C.L.1    Habash, M.2    Burrows, L.L.3
  • 18
    • 0037406829 scopus 로고    scopus 로고
    • Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a multifibrillar and adhesive structure
    • Durand E, Bernadac A, Ball G, Lazdunski A, Sturgis JN, Filloux A. 2003. Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a multifibrillar and adhesive structure. J. Bacteriol. 185:2749 -2758.
    • (2003) J. Bacteriol. , vol.185
    • Durand, E.1    Bernadac, A.2    Ball, G.3    Lazdunski, A.4    Sturgis, J.N.5    Filloux, A.6
  • 19
    • 0034657719 scopus 로고    scopus 로고
    • Pilus formation and protein secretion by the same machinery in Escherichia coli
    • Sauvonnet N, Vignon G, Pugsley AP, Gounon P. 2000. Pilus formation and protein secretion by the same machinery in Escherichia coli. EMBO J. 19:2221-2228.
    • (2000) EMBO J. , vol.19 , pp. 2221-2228
    • Sauvonnet, N.1    Vignon, G.2    Pugsley, A.P.3    Gounon, P.4
  • 20
    • 33748773323 scopus 로고    scopus 로고
    • Type IV pilin structures: insights on shared architecture, fiber assembly, receptor binding and type II secretion
    • Hansen JK, Forest KT. 2006. Type IV pilin structures: insights on shared architecture, fiber assembly, receptor binding and type II secretion. J. Mol. Microbiol. Biotechnol. 11:192-207.
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 192-207
    • Hansen, J.K.1    Forest, K.T.2
  • 21
    • 15244343311 scopus 로고    scopus 로고
    • Identification of a TcpC-TcpQ outer membrane complex involved in the biogenesis of the toxin-coregulated pilus of Vibrio cholerae
    • Bose N, Taylor RK. 2005. Identification of a TcpC-TcpQ outer membrane complex involved in the biogenesis of the toxin-coregulated pilus of Vibrio cholerae. J. Bacteriol. 187:2225-2232.
    • (2005) J. Bacteriol. , vol.187 , pp. 2225-2232
    • Bose, N.1    Taylor, R.K.2
  • 23
    • 0027467127 scopus 로고
    • Biogenesis and regulation of the Vibrio cholerae toxin-coregulated pilus: analogies to other virulence factor secretory systems
    • Kaufman MR, Shaw CE, Jones ID, Taylor RK. 1993. Biogenesis and regulation of the Vibrio cholerae toxin-coregulated pilus: analogies to other virulence factor secretory systems. Gene 126:43- 49.
    • (1993) Gene , vol.126
    • Kaufman, M.R.1    Shaw, C.E.2    Jones, I.D.3    Taylor, R.K.4
  • 24
    • 38849174766 scopus 로고    scopus 로고
    • Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU
    • Chiang P, Sampaleanu LM, Ayers M, Pahuta M, Howell PL, Burrows LL. 2008. Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU. Microbiology 154:114 -126.
    • (2008) Microbiology , vol.154
    • Chiang, P.1    Sampaleanu, L.M.2    Ayers, M.3    Pahuta, M.4    Howell, P.L.5    Burrows, L.L.6
  • 25
    • 77955936558 scopus 로고    scopus 로고
    • Architecture of the type II secretion and type IV pilus machineries
    • Ayers M, Howell PL, Burrows LL. 2010. Architecture of the type II secretion and type IV pilus machineries. Future Microbiol. 5:1203-1218.
    • (2010) Future Microbiol. , vol.5 , pp. 1203-1218
    • Ayers, M.1    Howell, P.L.2    Burrows, L.L.3
  • 26
    • 84860303391 scopus 로고    scopus 로고
    • Structure of an essential type IV pilus biogenesis protein provides insights into pilus and type II secretion systems
    • Yamagata A, Milgotina E, Scanlon K, Craig L, Tainer JA, Donnenberg MS. 2012. Structure of an essential type IV pilus biogenesis protein provides insights into pilus and type II secretion systems. J. Mol. Biol. 419: 110-124.
    • (2012) J. Mol. Biol. , vol.419 , pp. 110-124
    • Yamagata, A.1    Milgotina, E.2    Scanlon, K.3    Craig, L.4    Tainer, J.A.5    Donnenberg, M.S.6
  • 29
    • 0034933204 scopus 로고    scopus 로고
    • The type IV fimbrial subunit gene (fimA) of Dichelobacter nodosus is essential for virulence, protease secretion, and natural competence
    • Kennan RM, Dhungyel OP, Whittington RJ, Egerton JR, Rood JI. 2001. The type IV fimbrial subunit gene (fimA) of Dichelobacter nodosus is essential for virulence, protease secretion, and natural competence. J. Bacteriol. 183:4451- 4458.
    • (2001) J. Bacteriol. , vol.183
    • Kennan, R.M.1    Dhungyel, O.P.2    Whittington, R.J.3    Egerton, J.R.4    Rood, J.I.5
  • 30
    • 34447520502 scopus 로고    scopus 로고
    • Type IV fimbrial biogenesis is required for protease secretion and natural transformation in Dichelobacter nodosus
    • Han X, Kennan RM, Parker D, Davies JK, Rood JI. 2007. Type IV fimbrial biogenesis is required for protease secretion and natural transformation in Dichelobacter nodosus. J. Bacteriol. 189:5022-5033.
    • (2007) J. Bacteriol. , vol.189 , pp. 5022-5033
    • Han, X.1    Kennan, R.M.2    Parker, D.3    Davies, J.K.4    Rood, J.I.5
  • 31
    • 0038385185 scopus 로고    scopus 로고
    • Secretion of a soluble colonization factor by the TCP type 4 pilus biogenesis pathway in Vibrio cholerae
    • Kirn TJ, Bose N, Taylor RK. 2003. Secretion of a soluble colonization factor by the TCP type 4 pilus biogenesis pathway in Vibrio cholerae. Mol. Microbiol. 49:81-92.
    • (2003) Mol. Microbiol. , vol.49 , pp. 81-92
    • Kirn, T.J.1    Bose, N.2    Taylor, R.K.3
  • 32
    • 23344445349 scopus 로고    scopus 로고
    • TcpF is a soluble colonization factor and protective antigen secreted by El Tor and classical O1 and O139 Vibrio cholerae serogroups
    • Kirn TJ, Taylor RK. 2005. TcpF is a soluble colonization factor and protective antigen secreted by El Tor and classical O1 and O139 Vibrio cholerae serogroups. Infect. Immun. 73:4461- 4470.
    • (2005) Infect. Immun. , vol.73
    • Kirn, T.J.1    Taylor, R.K.2
  • 33
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenicity
    • Craig L, Pique ME, Tainer JA. 2004. Type IV pilus structure and bacterial pathogenicity. Nat. Rev. Microbiol. 2:363-378.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 363-378
    • Craig, L.1    Pique, M.E.2    Tainer, J.A.3
  • 34
    • 0035803406 scopus 로고    scopus 로고
    • Involvement of the twin-arginine translocation system in protein secretion via the type II pathway
    • Voulhoux R, Ball G, Ize B, Vasil ML, Lazdunski A, Wu LF, Filloux A. 2001. Involvement of the twin-arginine translocation system in protein secretion via the type II pathway. EMBO J. 20:6735- 6741.
    • (2001) EMBO J. , vol.20
    • Voulhoux, R.1    Ball, G.2    Ize, B.3    Vasil, M.L.4    Lazdunski, A.5    Wu, L.F.6    Filloux, A.7
  • 36
    • 0023736046 scopus 로고
    • Toxin, toxin-coregulated pili, and the toxR regulon are essential for Vibrio cholerae pathogenesis in humans
    • Herrington DA, Hall RH, Losonsky G, Mekalanos JJ, Taylor RK, Levine MM. 1988. Toxin, toxin-coregulated pili, and the toxR regulon are essential for Vibrio cholerae pathogenesis in humans. J. Exp. Med. 168:1487- 1492.
    • (1988) J. Exp. Med. , vol.168
    • Herrington, D.A.1    Hall, R.H.2    Losonsky, G.3    Mekalanos, J.J.4    Taylor, R.K.5    Levine, M.M.6
  • 38
    • 0014544827 scopus 로고
    • Pathogenesis of experimental cholera.Preparation and isolation of choleragen and choleragenoid.
    • Finkelstein RA, LoSpalluto JJ. 1969. Pathogenesis of experimental cholera. Preparation and isolation of choleragen and choleragenoid. J. Exp. Med. 130:185-202.
    • (1969) J. Exp. Med. , vol.130 , pp. 185-202
    • Finkelstein, R.A.1    LoSpalluto, J.J.2
  • 39
    • 0039391898 scopus 로고
    • Use of phoA gene fusions to identify a pilus colonization factor coordinately regulated with cholera toxin
    • Taylor RK, Miller VL, Furlong DB, Mekalanos JJ. 1987. Use of phoA gene fusions to identify a pilus colonization factor coordinately regulated with cholera toxin. Proc. Natl. Acad. Sci. U. S. A. 84:2833-2837.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 2833-2837
    • Taylor, R.K.1    Miller, V.L.2    Furlong, D.B.3    Mekalanos, J.J.4
  • 40
    • 0033609358 scopus 로고    scopus 로고
    • A bacteriophage encoding a pathogenicity island, a type-IV pilus and a phage receptor in cholera bacteria
    • Karaolis DK, Somara S, Maneval DR, Jr, Johnson JA, Kaper JB. 1999. A bacteriophage encoding a pathogenicity island, a type-IV pilus and a phage receptor in cholera bacteria. Nature 399:375-379.
    • (1999) Nature , vol.399 , pp. 375-379
    • Karaolis, D.K.1    Somara, S.2    Maneval, D.R.3    Johnson, J.A.4    Kaper, J.B.5
  • 41
    • 0030957263 scopus 로고    scopus 로고
    • The tcp gene cluster of Vibrio cholerae
    • Manning PA. 1997. The tcp gene cluster of Vibrio cholerae. Gene 192: 63-70.
    • (1997) Gene , vol.192 , pp. 63-70
    • Manning, P.A.1
  • 42
    • 77956538256 scopus 로고    scopus 로고
    • Genetics of Vibrio cholerae colonization and motility
    • In Nair GB, Faruque SM (ed), Vibrio cholerae genomics and molecular biology. Horizon Scientific Press, Norfolk, United Kingdom.
    • Jude BA, Taylor RK. 2008. Genetics of Vibrio cholerae colonization and motility, p 67-99. In Nair GB, Faruque SM (ed), Vibrio cholerae genomics and molecular biology. Horizon Scientific Press, Norfolk, United Kingdom.
    • (2008) , pp. 67-99
    • Jude, B.A.1    Taylor, R.K.2
  • 43
    • 66149141437 scopus 로고    scopus 로고
    • Genetic mapping of secretion and functional determinants of the Vibrio cholerae TcpF colonization factor
    • Krebs SJ, Kirn TJ, Taylor RK. 2009. Genetic mapping of secretion and functional determinants of the Vibrio cholerae TcpF colonization factor. J. Bacteriol. 191:3665-3676.
    • (2009) J. Bacteriol. , vol.191 , pp. 3665-3676
    • Krebs, S.J.1    Kirn, T.J.2    Taylor, R.K.3
  • 45
    • 0033951396 scopus 로고    scopus 로고
    • Delineation of pilin domains required for bacterial association into microcolonies and intestinal colonization by Vibrio cholerae
    • Kirn TJ, Lafferty MJ, Sandoe CM, Taylor RK. 2000. Delineation of pilin domains required for bacterial association into microcolonies and intestinal colonization by Vibrio cholerae. Mol. Microbiol. 35:896 -910.
    • (2000) Mol. Microbiol. , vol.35
    • Kirn, T.J.1    Lafferty, M.J.2    Sandoe, C.M.3    Taylor, R.K.4
  • 46
    • 0029926274 scopus 로고    scopus 로고
    • Positive selection vectors for allelic exchange
    • Skorupski K, Taylor RK. 1996. Positive selection vectors for allelic exchange. Gene 169:47-52.
    • (1996) Gene , vol.169 , pp. 47-52
    • Skorupski, K.1    Taylor, R.K.2
  • 47
    • 34250329174 scopus 로고    scopus 로고
    • Membrane association and multimerization of TcpT, the cognate ATPase ortholog of the Vibrio cholerae toxincoregulated- pilus biogenesis apparatus
    • Tripathi SA, Taylor RK. 2007. Membrane association and multimerization of TcpT, the cognate ATPase ortholog of the Vibrio cholerae toxincoregulated- pilus biogenesis apparatus. J. Bacteriol. 189:4401- 4409.
    • (2007) J. Bacteriol. , vol.189
    • Tripathi, S.A.1    Taylor, R.K.2
  • 48
    • 0030043489 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp
    • Dougherty DA. 1996. Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science 271:163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 50
    • 0035019730 scopus 로고    scopus 로고
    • Type II secretion and pathogenesis
    • Sandkvist M. 2001. Type II secretion and pathogenesis. Infect. Immun. 69:3523-3535.
    • (2001) Infect. Immun. , vol.69 , pp. 3523-3535
    • Sandkvist, M.1
  • 51
    • 43249124991 scopus 로고    scopus 로고
    • The type II secretion arrowhead: the structure of GspIGspJ- GspK
    • Forest KT. 2008. The type II secretion arrowhead: the structure of GspIGspJ- GspK. Nat. Struct. Mol. Biol. 15:428-430.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 428-430
    • Forest, K.T.1
  • 52
    • 78751679366 scopus 로고    scopus 로고
    • In vivo crosslinking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the type II secretion system of Vibrio cholerae
    • Gray MD, Bagdasarian M, Hol WG, Sandkvist M. 2011. In vivo crosslinking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the type II secretion system of Vibrio cholerae. Mol. Microbiol. 79:786 -798.
    • (2011) Mol. Microbiol. , vol.79
    • Gray, M.D.1    Bagdasarian, M.2    Hol, W.G.3    Sandkvist, M.4
  • 54
    • 37549005981 scopus 로고    scopus 로고
    • Vibrio cholerae toxin-coregulated pilus structure analyzed by hydrogen/ deuterium exchange mass spectrometry
    • Li J, Lim MS, Li S, Brock M, Pique ME, Woods VL, Jr, Craig L. 2008. Vibrio cholerae toxin-coregulated pilus structure analyzed by hydrogen/ deuterium exchange mass spectrometry. Structure 16:137-148.
    • (2008) Structure , vol.16 , pp. 137-148
    • Li, J.1    Lim, M.S.2    Li, S.3    Brock, M.4    Pique, M.E.5    Woods, V.L.6    Craig, L.7
  • 55
    • 0034973703 scopus 로고    scopus 로고
    • Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure
    • Collins RF, Davidsen L, Derrick JP, Ford RC, Tonjum T. 2001. Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure. J. Bacteriol. 183: 3825-3832.
    • (2001) J. Bacteriol. , vol.183 , pp. 3825-3832
    • Collins, R.F.1    Davidsen, L.2    Derrick, J.P.3    Ford, R.C.4    Tonjum, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.