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Volumn 163, Issue 9-10, 2012, Pages 659-673

Neglected but amazingly diverse type IVb pili

Author keywords

BFP; Flp pilus; R64 plasmid; TCP; Type IVb pilus

Indexed keywords

CHOLERA TOXIN; HOST FACTOR; PERIPLASMIC PROTEIN; PILIN;

EID: 84870738200     PISSN: 09232508     EISSN: 17697123     Source Type: Journal    
DOI: 10.1016/j.resmic.2012.10.015     Document Type: Article
Times cited : (29)

References (132)
  • 1
    • 69049095025 scopus 로고    scopus 로고
    • Bicarbonate induces Vibrio cholerae virulence gene expression by enhancing ToxT activity
    • Abuaita B.H., Withey J.H. Bicarbonate induces Vibrio cholerae virulence gene expression by enhancing ToxT activity. Infect. Immun. 2009, 77:4111-4120.
    • (2009) Infect. Immun. , vol.77 , pp. 4111-4120
    • Abuaita, B.H.1    Withey, J.H.2
  • 2
    • 84860417881 scopus 로고    scopus 로고
    • Termination of Vibrio cholerae virulence gene expression is mediated by proteolysis of the major virulence activator, ToxT
    • Abuaita B.H., Withey J.H. Termination of Vibrio cholerae virulence gene expression is mediated by proteolysis of the major virulence activator, ToxT. Mol. Microbiol. 2011, 81:1640-1653.
    • (2011) Mol. Microbiol. , vol.81 , pp. 1640-1653
    • Abuaita, B.H.1    Withey, J.H.2
  • 3
    • 23744489452 scopus 로고    scopus 로고
    • Analysis of the pilU gene for the prepilin peptidase involved in the biogenesis of type IV pili encoded by plasmid R64
    • Akahane K., Sakai D., Furuya N., Komano T. Analysis of the pilU gene for the prepilin peptidase involved in the biogenesis of type IV pili encoded by plasmid R64. Mol. Genet. Genomics 2005, 273:350-359.
    • (2005) Mol. Genet. Genomics , vol.273 , pp. 350-359
    • Akahane, K.1    Sakai, D.2    Furuya, N.3    Komano, T.4
  • 4
    • 0031985046 scopus 로고    scopus 로고
    • Role of BfpF, a member of the PilT family of putative nucleotide-binding proteins, in type IV pilus biogenesis and in interactions between enteropathogenic Escherichia coli and host cells
    • Anantha R.P., Stone K.D., Donnenberg M.S. Role of BfpF, a member of the PilT family of putative nucleotide-binding proteins, in type IV pilus biogenesis and in interactions between enteropathogenic Escherichia coli and host cells. Infect. Immun. 1998, 66:122-131.
    • (1998) Infect. Immun. , vol.66 , pp. 122-131
    • Anantha, R.P.1    Stone, K.D.2    Donnenberg, M.S.3
  • 5
    • 0034005318 scopus 로고    scopus 로고
    • Effects of bfp mutations on biogenesis of functional enteropathogenic Escherichia coli type IV pili
    • Anantha R.P., Stone K.D., Donnenberg M.S. Effects of bfp mutations on biogenesis of functional enteropathogenic Escherichia coli type IV pili. J. Bacteriol. 2000, 182:2498-2506.
    • (2000) J. Bacteriol. , vol.182 , pp. 2498-2506
    • Anantha, R.P.1    Stone, K.D.2    Donnenberg, M.S.3
  • 7
    • 77955936558 scopus 로고    scopus 로고
    • Architecture of the type II secretion and type IV pilus machineries
    • Ayers M., Howell P.L., Burrows L.L. Architecture of the type II secretion and type IV pilus machineries. Future Microbiol. 2010, 5:1203-1218.
    • (2010) Future Microbiol. , vol.5 , pp. 1203-1218
    • Ayers, M.1    Howell, P.L.2    Burrows, L.L.3
  • 8
    • 10044288424 scopus 로고    scopus 로고
    • TcpH influences virulence gene expression in Vibrio cholerae by inhibiting degradation of the transcription activator TcpP
    • Beck N.A., Krukonis E.S., DiRita V.J. TcpH influences virulence gene expression in Vibrio cholerae by inhibiting degradation of the transcription activator TcpP. J. Bacteriol. 2004, 186:8309-8316.
    • (2004) J. Bacteriol. , vol.186 , pp. 8309-8316
    • Beck, N.A.1    Krukonis, E.S.2    DiRita, V.J.3
  • 9
    • 33745467867 scopus 로고    scopus 로고
    • FppA, a novel Pseudomonas aeruginosa prepilin peptidase involved in assembly of type IVb pili
    • de Bentzmann S., Aurouze M., Ball G., Filloux A. FppA, a novel Pseudomonas aeruginosa prepilin peptidase involved in assembly of type IVb pili. J. Bacteriol. 2006, 188:4851-4860.
    • (2006) J. Bacteriol. , vol.188 , pp. 4851-4860
    • de Bentzmann, S.1    Aurouze, M.2    Ball, G.3    Filloux, A.4
  • 10
    • 63049092517 scopus 로고    scopus 로고
    • Organization and PprB-dependent control of the Pseudomonas aeruginosa tad Locus, involved in Flp pilus biology
    • Bernard C.S., Bordi C., Termine E., Filloux A., de Bentzmann S. Organization and PprB-dependent control of the Pseudomonas aeruginosa tad Locus, involved in Flp pilus biology. J. Bacteriol. 2009, 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
  • 11
    • 0034816350 scopus 로고    scopus 로고
    • Nonspecific adherence and fibril biogenesis by Actinobacillus actinomycetemcomitans: TadA protein is an ATPase
    • Bhattacharjee M.K., Kachlany S.C., Fine D.H., Figurski D.H. Nonspecific adherence and fibril biogenesis by Actinobacillus actinomycetemcomitans: TadA protein is an ATPase. J. Bacteriol. 2001, 183:5927-5936.
    • (2001) J. Bacteriol. , vol.183 , pp. 5927-5936
    • Bhattacharjee, M.K.1    Kachlany, S.C.2    Fine, D.H.3    Figurski, D.H.4
  • 12
    • 0032568984 scopus 로고    scopus 로고
    • Type IV pili, transient bacterial aggregates, and virulence of enteropathogenic Escherichia coli
    • Bieber D., Ramer S.W., Wu C.Y., Murray W.J., Tobe T., Fernandez R., Schoolnik G.K. Type IV pili, transient bacterial aggregates, and virulence of enteropathogenic Escherichia coli. Science 1998, 280:2114-2118.
    • (1998) Science , vol.280 , pp. 2114-2118
    • Bieber, D.1    Ramer, S.W.2    Wu, C.Y.3    Murray, W.J.4    Tobe, T.5    Fernandez, R.6    Schoolnik, G.K.7
  • 13
    • 51149114355 scopus 로고    scopus 로고
    • Interaction of Salmonella enterica serovar Typhi with cultured epithelial cells: roles of surface structures in adhesion and invasion
    • Bishop A., House D., Perkins T., Baker S., Kingsley R.A., Dougan G. Interaction of Salmonella enterica serovar Typhi with cultured epithelial cells: roles of surface structures in adhesion and invasion. Microbiology 2008, 154:1914-1926.
    • (2008) Microbiology , vol.154 , pp. 1914-1926
    • Bishop, A.1    House, D.2    Perkins, T.3    Baker, S.4    Kingsley, R.A.5    Dougan, G.6
  • 14
    • 0034937029 scopus 로고    scopus 로고
    • Novel topology of BfpE, a cytoplasmic membrane protein required for type IV fimbrial biogenesis in enteropathogenic Escherichia coli
    • Blank T.E., Donnenberg M.S. Novel topology of BfpE, a cytoplasmic membrane protein required for type IV fimbrial biogenesis in enteropathogenic Escherichia coli. J. Bacteriol. 2001, 183:4435-4450.
    • (2001) J. Bacteriol. , vol.183 , pp. 4435-4450
    • Blank, T.E.1    Donnenberg, M.S.2
  • 15
    • 0034444843 scopus 로고    scopus 로고
    • Molecular variation among type IV pilin (bfpA) genes from diverse enteropathogenic Escherichia coli strains
    • Blank T.E., Zhong H., Bell A.L., Whittam T.S., Donnenberg M.S. Molecular variation among type IV pilin (bfpA) genes from diverse enteropathogenic Escherichia coli strains. Infect. Immun. 2000, 68:7028-7038.
    • (2000) Infect. Immun. , vol.68 , pp. 7028-7038
    • Blank, T.E.1    Zhong, H.2    Bell, A.L.3    Whittam, T.S.4    Donnenberg, M.S.5
  • 17
    • 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 R.K. Identification of a TcpC-TcpQ outer membrane complex involved in the biogenesis of the toxin-coregulated pilus of Vibrio cholerae. J. Bacteriol. 2005, 187:2225-2232.
    • (2005) J. Bacteriol. , vol.187 , pp. 2225-2232
    • Bose, N.1    Taylor, R.K.2
  • 18
    • 79960967875 scopus 로고    scopus 로고
    • A genome-wide approach to discovery of small RNAs involved in regulation of virulence in Vibrio cholerae
    • Bradley E.S., Bodi K., Ismail A.M., Camilli A. A genome-wide approach to discovery of small RNAs involved in regulation of virulence in Vibrio cholerae. PLoS Pathog. 2011, 7:e1002126.
    • (2011) PLoS Pathog. , vol.7
    • Bradley, E.S.1    Bodi, K.2    Ismail, A.M.3    Camilli, A.4
  • 19
    • 84870705958 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa twitching motility: type IV pili in action
    • Burrows L.L. Pseudomonas aeruginosa twitching motility: type IV pili in action. Annu. Rev. Microbiol. 2012, 66:493-520.
    • (2012) Annu. Rev. Microbiol. , vol.66 , pp. 493-520
    • Burrows, L.L.1
  • 20
    • 79851515749 scopus 로고    scopus 로고
    • Modeling pilus structures from sparse data
    • Campos M., Francetic O., Nilges M. Modeling pilus structures from sparse data. J. Struct. Biol. 2011, 173:436-444.
    • (2011) J. Struct. Biol. , vol.173 , pp. 436-444
    • Campos, M.1    Francetic, O.2    Nilges, M.3
  • 21
    • 77954374364 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa pathogenicity island PAPI-1 is transferred via a novel type IV pilus
    • Carter M.Q., Chen J., Lory S. The Pseudomonas aeruginosa pathogenicity island PAPI-1 is transferred via a novel type IV pilus. J. Bacteriol. 2010, 192:3249-3258.
    • (2010) J. Bacteriol. , vol.192 , pp. 3249-3258
    • Carter, M.Q.1    Chen, J.2    Lory, S.3
  • 22
    • 34547531184 scopus 로고    scopus 로고
    • Regulation of virulence in Vibrio cholerae: the ToxR regulon
    • Childers B.M., Klose K.E. Regulation of virulence in Vibrio cholerae: the ToxR regulon. Future Microbiol. 2007, 2:335-344.
    • (2007) Future Microbiol. , vol.2 , pp. 335-344
    • Childers, B.M.1    Klose, K.E.2
  • 23
    • 33947164676 scopus 로고    scopus 로고
    • Identification of residues critical for the function of the Vibrio cholerae virulence regulator ToxT by scanning alanine mutagenesis
    • Childers B.M., Weber G.G., Prouty M.G., Castaneda M.M., Peng F., Klose K.E. Identification of residues critical for the function of the Vibrio cholerae virulence regulator ToxT by scanning alanine mutagenesis. J. Mol. Biol. 2007, 367:1413-1430.
    • (2007) J. Mol. Biol. , vol.367 , pp. 1413-1430
    • Childers, B.M.1    Weber, G.G.2    Prouty, M.G.3    Castaneda, M.M.4    Peng, F.5    Klose, K.E.6
  • 24
    • 38649126553 scopus 로고    scopus 로고
    • Outer membrane components of the Tad (tight adherence) secreton of Aggregatibacter actinomycetemcomitans
    • Clock S.A., Planet P.J., Perez B.A., Figurski D.H. Outer membrane components of the Tad (tight adherence) secreton of Aggregatibacter actinomycetemcomitans. J. Bacteriol. 2008, 190:980-990.
    • (2008) J. Bacteriol. , vol.190 , pp. 980-990
    • Clock, S.A.1    Planet, P.J.2    Perez, B.A.3    Figurski, D.H.4
  • 25
    • 12444272635 scopus 로고    scopus 로고
    • Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin
    • Craig L., Taylor R.K., Pique M.E., Adair B.D., Arvai A.S., Singh M., Lloyd S.J., Shin D.S., et al. Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin. Mol. Cell. 2003, 11:1139-1150.
    • (2003) Mol. Cell. , vol.11 , pp. 1139-1150
    • Craig, L.1    Taylor, R.K.2    Pique, M.E.3    Adair, B.D.4    Arvai, A.S.5    Singh, M.6    Lloyd, S.J.7    Shin, D.S.8
  • 26
    • 0037340113 scopus 로고    scopus 로고
    • Membrane localization of the ToxR winged-helix domain is required for TcpP-mediated virulence gene activation in Vibrio cholerae
    • Crawford J.A., Krukonis E.S., DiRita V.J. Membrane localization of the ToxR winged-helix domain is required for TcpP-mediated virulence gene activation in Vibrio cholerae. Mol. Microbiol. 2003, 47:1459-1473.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1459-1473
    • Crawford, J.A.1    Krukonis, E.S.2    DiRita, V.J.3
  • 27
    • 1942424083 scopus 로고    scopus 로고
    • The inner membrane subassembly of the enteropathogenic Escherichia coli bundle-forming pilus machine
    • Crowther L.J., Anantha R.P., Donnenberg M.S. The inner membrane subassembly of the enteropathogenic Escherichia coli bundle-forming pilus machine. Mol. Microbiol. 2004, 52:67-79.
    • (2004) Mol. Microbiol. , vol.52 , pp. 67-79
    • Crowther, L.J.1    Anantha, R.P.2    Donnenberg, M.S.3
  • 28
    • 33747093681 scopus 로고    scopus 로고
    • Interaction and localization studies of enteropathogenic Escherichia coli type IV bundle-forming pilus outer membrane components
    • Daniel A., Singh A., Crowther L.J., Fernandes P.J., Schreiber W., Donnenberg M.S. Interaction and localization studies of enteropathogenic Escherichia coli type IV bundle-forming pilus outer membrane components. Microbiology 2006, 152:2405-2420.
    • (2006) Microbiology , vol.152 , pp. 2405-2420
    • Daniel, A.1    Singh, A.2    Crowther, L.J.3    Fernandes, P.J.4    Schreiber, W.5    Donnenberg, M.S.6
  • 29
    • 84859754930 scopus 로고    scopus 로고
    • Coordinated regulation of accessory genetic elements produces cyclic di-nucleotides for V. cholerae virulence
    • Davies B.W., Bogard R.W., Young T.S., Mekalanos J.J. Coordinated regulation of accessory genetic elements produces cyclic di-nucleotides for V. cholerae virulence. Cell 2012, 149:358-370.
    • (2012) Cell , vol.149 , pp. 358-370
    • Davies, B.W.1    Bogard, R.W.2    Young, T.S.3    Mekalanos, J.J.4
  • 30
    • 84867137814 scopus 로고    scopus 로고
    • BfpL is essential for type IV bundle-forming pilus biogenesis and interacts with the periplasmic face of BfpC
    • De Masi L., Szmacinski H., Schreiber W., Donnenberg M.S. BfpL is essential for type IV bundle-forming pilus biogenesis and interacts with the periplasmic face of BfpC. Microbiology 2012, 158:2515-2526.
    • (2012) Microbiology , vol.158 , pp. 2515-2526
    • De Masi, L.1    Szmacinski, H.2    Schreiber, W.3    Donnenberg, M.S.4
  • 31
    • 0026098804 scopus 로고
    • Periplasmic interaction between two membrane regulatory proteins, ToxR and ToxS, results in signal transduction and transcriptional activation
    • DiRita V.J., Mekalanos J.J. Periplasmic interaction between two membrane regulatory proteins, ToxR and ToxS, results in signal transduction and transcriptional activation. Cell 1991, 64:29-37.
    • (1991) Cell , vol.64 , pp. 29-37
    • DiRita, V.J.1    Mekalanos, J.J.2
  • 32
    • 80055061248 scopus 로고    scopus 로고
    • Bacterial-epithelial contact is a key determinant of host innate immune responses to enteropathogenic and enteroaggregative Escherichia coli
    • Edwards L.A., Bajaj-Elliott M., Klein N.J., Murch S.H., Phillips A.D. Bacterial-epithelial contact is a key determinant of host innate immune responses to enteropathogenic and enteroaggregative Escherichia coli. PLoS One 2011, 6:e27030.
    • (2011) PLoS One , vol.6
    • Edwards, L.A.1    Bajaj-Elliott, M.2    Klein, N.J.3    Murch, S.H.4    Phillips, A.D.5
  • 33
    • 0033386211 scopus 로고    scopus 로고
    • Tenacious adhesion of Actinobacillus actinomycetemcomitans strain CU1000 to salivary-coated hydroxyapatite
    • Fine D.H., Furgang D., Kaplan J., Charlesworth J., Figurski D.H. Tenacious adhesion of Actinobacillus actinomycetemcomitans strain CU1000 to salivary-coated hydroxyapatite. Arch. Oral Biol. 1999, 44:1063-1076.
    • (1999) Arch. Oral Biol. , vol.44 , pp. 1063-1076
    • Fine, D.H.1    Furgang, D.2    Kaplan, J.3    Charlesworth, J.4    Figurski, D.H.5
  • 34
    • 78649734744 scopus 로고    scopus 로고
    • Biological " glue" and " Velcro" : molecular tools for adhesion and biofilm formation in the hairy and gluey bug Pseudomonas aeruginosa
    • Giraud C., Bernard C.S., Ruer S., de Bentzmann S. Biological " glue" and " Velcro" : molecular tools for adhesion and biofilm formation in the hairy and gluey bug Pseudomonas aeruginosa. Environ. Microbiol. Rep. 2010, 2:343-358.
    • (2010) Environ. Microbiol. Rep. , vol.2 , pp. 343-358
    • Giraud, C.1    Bernard, C.S.2    Ruer, S.3    de Bentzmann, S.4
  • 35
    • 0026330896 scopus 로고
    • An inducible bundle-forming pilus of enteropathogenic Escherichia coli
    • Giron J.A., Ho A.S., Schoolnik G.K. An inducible bundle-forming pilus of enteropathogenic Escherichia coli. Science 1991, 254:710-713.
    • (1991) Science , vol.254 , pp. 710-713
    • Giron, J.A.1    Ho, A.S.2    Schoolnik, G.K.3
  • 36
    • 0343924353 scopus 로고    scopus 로고
    • Longus pilus of enterotoxigenic Escherichia coli and its relatedness to other type-4 pili - a minireview
    • Giron J.A., Gomez-Duarte O.G., Jarvis K.G., Kaper J.B. Longus pilus of enterotoxigenic Escherichia coli and its relatedness to other type-4 pili - a minireview. Gene 1997, 192:39-43.
    • (1997) Gene , vol.192 , pp. 39-43
    • Giron, J.A.1    Gomez-Duarte, O.G.2    Jarvis, K.G.3    Kaper, J.B.4
  • 38
    • 0032984036 scopus 로고    scopus 로고
    • Identification and molecular analysis of rough-colony-specific outer membrane proteins of Actinobacillus actinomycetemcomitans
    • Haase E.M., Zmuda J.L., Scannapieco F.A. Identification and molecular analysis of rough-colony-specific outer membrane proteins of Actinobacillus actinomycetemcomitans. Infect. Immun. 1999, 67:2901-2908.
    • (1999) Infect. Immun. , vol.67 , pp. 2901-2908
    • Haase, E.M.1    Zmuda, J.L.2    Scannapieco, F.A.3
  • 39
    • 0031930690 scopus 로고    scopus 로고
    • TcpP protein is a positive regulator of virulence gene expression in Vibrio cholerae
    • Hase C.C., Mekalanos J.J. TcpP protein is a positive regulator of virulence gene expression in Vibrio cholerae. Proc. Natl. Acad. Sci. U S A 1998, 95:730-734.
    • (1998) Proc. Natl. Acad. Sci. U S A , vol.95 , pp. 730-734
    • Hase, C.C.1    Mekalanos, J.J.2
  • 40
    • 0023736046 scopus 로고
    • Toxin, toxin-coregulated pili, and the toxR regulon are essential for Vibrio cholerae pathogenesis in humans
    • Herrington D.A., Hall R.H., Losonsky G., Mekalanos J.J., Taylor R.K., Levine M.M. Toxin, toxin-coregulated pili, and the toxR regulon are essential for Vibrio cholerae pathogenesis in humans. J. Exp. Med. 1988, 168:1487-1492.
    • (1988) J. Exp. Med. , vol.168 , pp. 1487-1492
    • Herrington, D.A.1    Hall, R.H.2    Losonsky, G.3    Mekalanos, J.J.4    Taylor, R.K.5    Levine, M.M.6
  • 41
    • 0027489247 scopus 로고
    • Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein complexes
    • Hobbs M., Mattick J.S. Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein complexes. Mol. Microbiol. 1993, 10:233-243.
    • (1993) Mol. Microbiol. , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, J.S.2
  • 42
    • 38449087356 scopus 로고    scopus 로고
    • Post-transcriptional cross-talk between pro- and anti-colonization pili biosynthesis systems in Vibrio cholerae
    • Hsiao A., Toscano K., Zhu J. Post-transcriptional cross-talk between pro- and anti-colonization pili biosynthesis systems in Vibrio cholerae. Mol. Microbiol. 2008, 67:849-860.
    • (2008) Mol. Microbiol. , vol.67 , pp. 849-860
    • Hsiao, A.1    Toscano, K.2    Zhu, J.3
  • 43
    • 63149150088 scopus 로고    scopus 로고
    • Direct regulation by the Vibrio cholerae regulator ToxT to modulate colonization and anticolonization pilus expression
    • Hsiao A., Xu X., Kan B., Kulkarni R.V., Zhu J. Direct regulation by the Vibrio cholerae regulator ToxT to modulate colonization and anticolonization pilus expression. Infect. Immun. 2009, 77:1383-1388.
    • (2009) Infect. Immun. , vol.77 , pp. 1383-1388
    • Hsiao, A.1    Xu, X.2    Kan, B.3    Kulkarni, R.V.4    Zhu, J.5
  • 44
    • 77952846943 scopus 로고    scopus 로고
    • N-acetyllactosamine-induced retraction of bundle-forming pili regulates virulence-associated gene expression in enteropathogenic Escherichia coli
    • Humphries R.M., Griener T.P., Vogt S.L., Mulvey G.L., Raivio T., Donnenberg M.S., Kitov P.I., Surette M., et al. N-acetyllactosamine-induced retraction of bundle-forming pili regulates virulence-associated gene expression in enteropathogenic Escherichia coli. Mol. Microbiol. 2010, 76:1111-1126.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1111-1126
    • Humphries, R.M.1    Griener, T.P.2    Vogt, S.L.3    Mulvey, G.L.4    Raivio, T.5    Donnenberg, M.S.6    Kitov, P.I.7    Surette, M.8
  • 46
    • 0037406928 scopus 로고    scopus 로고
    • Identification of the DNA binding sites of PerA, the transcriptional activator of the bfp and per operons in enteropathogenic Escherichia coli
    • Ibarra J.A., Villalba M.I., Puente J.L. Identification of the DNA binding sites of PerA, the transcriptional activator of the bfp and per operons in enteropathogenic Escherichia coli. J. Bacteriol. 2003, 185:2835-2847.
    • (2003) J. Bacteriol. , vol.185 , pp. 2835-2847
    • Ibarra, J.A.1    Villalba, M.I.2    Puente, J.L.3
  • 47
    • 0031968738 scopus 로고    scopus 로고
    • Molecular characterization of low-molecular-weight component protein, Flp, in Actinobacillus actinomycetemcomitans fimbriae
    • Inoue T., Tanimoto I., Ohta H., Kato K., Murayama Y., Fukui K. Molecular characterization of low-molecular-weight component protein, Flp, in Actinobacillus actinomycetemcomitans fimbriae. Microbiol. Immunol. 1998, 42:253-258.
    • (1998) Microbiol. Immunol. , vol.42 , pp. 253-258
    • Inoue, T.1    Tanimoto, I.2    Ohta, H.3    Kato, K.4    Murayama, Y.5    Fukui, K.6
  • 48
    • 0033859189 scopus 로고    scopus 로고
    • Heterogeneous post-translational modification of Actinobacillus actinomycetemcomitans fimbrillin
    • Inoue T., Ohta H., Tanimoto I., Shingaki R., Fukui K. Heterogeneous post-translational modification of Actinobacillus actinomycetemcomitans fimbrillin. Microbiol. Immunol. 2000, 44:715-718.
    • (2000) Microbiol. Immunol. , vol.44 , pp. 715-718
    • Inoue, T.1    Ohta, H.2    Tanimoto, I.3    Shingaki, R.4    Fukui, K.5
  • 49
    • 0033825976 scopus 로고    scopus 로고
    • The lipopolysaccharide of recipient cells is a specific receptor for PilV proteins, selected by shufflon DNA rearrangement, in liquid matings with donors bearing the R64 plasmid
    • Ishiwa A., Komano T. The lipopolysaccharide of recipient cells is a specific receptor for PilV proteins, selected by shufflon DNA rearrangement, in liquid matings with donors bearing the R64 plasmid. Mol. Gen. Genet. 2000, 263:159-164.
    • (2000) Mol. Gen. Genet. , vol.263 , pp. 159-164
    • Ishiwa, A.1    Komano, T.2
  • 50
    • 4744376093 scopus 로고    scopus 로고
    • PilV adhesins of plasmid R64 thin pili specifically bind to the lipopolysaccharides of recipient cells
    • Ishiwa A., Komano T. PilV adhesins of plasmid R64 thin pili specifically bind to the lipopolysaccharides of recipient cells. J. Mol. Biol. 2004, 343:615-625.
    • (2004) J. Mol. Biol. , vol.343 , pp. 615-625
    • Ishiwa, A.1    Komano, T.2
  • 51
    • 2542542070 scopus 로고    scopus 로고
    • The emergence of catalytic and structural diversity within the beta-clip fold
    • Iyer L.M., Aravind L. The emergence of catalytic and structural diversity within the beta-clip fold. Proteins 2004, 55:977-991.
    • (2004) Proteins , vol.55 , pp. 977-991
    • Iyer, L.M.1    Aravind, L.2
  • 52
    • 79955749079 scopus 로고    scopus 로고
    • The Vibrio cholerae VarS/VarA two-component system controls the expression of virulence proteins through ToxT regulation
    • Jang J., Jung K.T., Park J., Yoo C.K., Rhie G.E. The Vibrio cholerae VarS/VarA two-component system controls the expression of virulence proteins through ToxT regulation. Microbiology 2011, 157:1466-1473.
    • (2011) Microbiology , vol.157 , pp. 1466-1473
    • Jang, J.1    Jung, K.T.2    Park, J.3    Yoo, C.K.4    Rhie, G.E.5
  • 54
    • 79956210276 scopus 로고    scopus 로고
    • The physical basis of type 4 pilus-mediated microcolony formation by Vibrio cholerae O1
    • Jude B.A., Taylor R.K. The physical basis of type 4 pilus-mediated microcolony formation by Vibrio cholerae O1. J. Struct. Biol. 2011, 175:1-9.
    • (2011) J. Struct. Biol. , vol.175 , pp. 1-9
    • Jude, B.A.1    Taylor, R.K.2
  • 56
    • 0035449036 scopus 로고    scopus 로고
    • Genes for tight adherence of Actinobacillus actinomycetemcomitans: from plaque to plague to pond scum
    • Kachlany S.C., Planet P.J., DeSalle R., Fine D.H., Figurski D.H. Genes for tight adherence of Actinobacillus actinomycetemcomitans: from plaque to plague to pond scum. Trends Microbiol. 2001, 9:429-437.
    • (2001) Trends Microbiol. , vol.9 , pp. 429-437
    • Kachlany, S.C.1    Planet, P.J.2    DeSalle, R.3    Fine, D.H.4    Figurski, D.H.5
  • 57
    • 0034999675 scopus 로고    scopus 로고
    • Flp-1, the first representative of a new pilin gene subfamily, is required for non-specific adherence of Actinobacillus actinomycetemcomitans
    • Kachlany S.C., Planet P.J., Desalle R., Fine D.H., Figurski D.H., Kaplan J.B. flp-1, the first representative of a new pilin gene subfamily, is required for non-specific adherence of Actinobacillus actinomycetemcomitans. Mol. Microbiol. 2001, 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
  • 58
    • 0030998924 scopus 로고    scopus 로고
    • The plasmid R64 thin pilus identified as a type IV pilus
    • Kim S.R., Komano T. The plasmid R64 thin pilus identified as a type IV pilus. J. Bacteriol. 1997, 179:3594-3603.
    • (1997) J. Bacteriol. , vol.179 , pp. 3594-3603
    • Kim, S.R.1    Komano, T.2
  • 59
    • 0033951396 scopus 로고    scopus 로고
    • Delineation of pilin domains required for bacterial association into microcolonies and intestinal colonization by Vibrio cholerae
    • Kirn T.J., Lafferty M.J., Sandoe C.M., Taylor R.K. Delineation of pilin domains required for bacterial association into microcolonies and intestinal colonization by Vibrio cholerae. Mol. Microbiol. 2000, 35:896-910.
    • (2000) Mol. Microbiol. , vol.35 , pp. 896-910
    • Kirn, T.J.1    Lafferty, M.J.2    Sandoe, C.M.3    Taylor, R.K.4
  • 60
    • 0038385185 scopus 로고    scopus 로고
    • Secretion of a soluble colonization factor by the TCP type 4 pilus biogenesis pathway in Vibrio cholerae
    • Kirn T.J., Bose N., Taylor R.K. Secretion of a soluble colonization factor by the TCP type 4 pilus biogenesis pathway in Vibrio cholerae. Mol. Microbiol. 2003, 49:81-92.
    • (2003) Mol. Microbiol. , vol.49 , pp. 81-92
    • Kirn, T.J.1    Bose, N.2    Taylor, R.K.3
  • 61
    • 0025361370 scopus 로고
    • Transfer region of IncI1 plasmid R64 and role of shufflon in R64 transfer
    • Komano T., Funayama N., Kim S.R., Nisioka T. Transfer region of IncI1 plasmid R64 and role of shufflon in R64 transfer. J. Bacteriol. 1990, 172:2230-2235.
    • (1990) J. Bacteriol. , vol.172 , pp. 2230-2235
    • Komano, T.1    Funayama, N.2    Kim, S.R.3    Nisioka, T.4
  • 62
    • 0027942908 scopus 로고
    • DNA rearrangement of the shufflon determines recipient specificity in liquid mating of IncI1 plasmid R64
    • Komano T., Kim S.R., Yoshida T., Nisioka T. DNA rearrangement of the shufflon determines recipient specificity in liquid mating of IncI1 plasmid R64. J. Mol. Biol. 1994, 243:6-9.
    • (1994) J. Mol. Biol. , vol.243 , pp. 6-9
    • Komano, T.1    Kim, S.R.2    Yoshida, T.3    Nisioka, T.4
  • 63
    • 0028917486 scopus 로고
    • Mating variation by DNA inversions of shufflon in plasmid R64
    • Komano T., Kim S.R., Yoshida T. Mating variation by DNA inversions of shufflon in plasmid R64. Adv. Biophys. 1995, 31:181-193.
    • (1995) Adv. Biophys. , vol.31 , pp. 181-193
    • Komano, T.1    Kim, S.R.2    Yoshida, T.3
  • 64
    • 0344393521 scopus 로고    scopus 로고
    • Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria
    • Koraimann G. Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria. Cell. Mol. Life Sci. 2003, 60:2371-2388.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2371-2388
    • Koraimann, G.1
  • 65
    • 44349162964 scopus 로고    scopus 로고
    • Transcriptional regulation of the tad locus in Aggregatibacter actinomycetemcomitans: a termination cascade
    • Kram K.E., Hovel-Miner G.A., Tomich M., Figurski D.H. Transcriptional regulation of the tad locus in Aggregatibacter actinomycetemcomitans: a termination cascade. J. Bacteriol. 2008, 190:3859-3868.
    • (2008) J. Bacteriol. , vol.190 , pp. 3859-3868
    • Kram, K.E.1    Hovel-Miner, G.A.2    Tomich, M.3    Figurski, D.H.4
  • 66
    • 80053586476 scopus 로고    scopus 로고
    • Protection and attachment of Vibrio cholerae mediated by the toxin-coregulated pilus in the infant mouse model
    • Krebs S.J., Taylor R.K. Protection and attachment of Vibrio cholerae mediated by the toxin-coregulated pilus in the infant mouse model. J. Bacteriol. 2011, 193:5260-5270.
    • (2011) J. Bacteriol. , vol.193 , pp. 5260-5270
    • Krebs, S.J.1    Taylor, R.K.2
  • 67
    • 0042671266 scopus 로고    scopus 로고
    • DNA binding and ToxR responsiveness by the wing domain of TcpP, an activator of virulence gene expression in Vibrio cholerae
    • Krukonis E.S., DiRita V.J. DNA binding and ToxR responsiveness by the wing domain of TcpP, an activator of virulence gene expression in Vibrio cholerae. Mol. Cell. 2003, 12:157-165.
    • (2003) Mol. Cell. , vol.12 , pp. 157-165
    • Krukonis, E.S.1    DiRita, V.J.2
  • 68
    • 0033815224 scopus 로고    scopus 로고
    • The Vibrio cholerae ToxR/TcpP/ToxT virulence cascade: distinct roles for two membrane-localized transcriptional activators on a single promoter
    • Krukonis E.S., Yu R.R., Dirita V.J. The Vibrio cholerae ToxR/TcpP/ToxT virulence cascade: distinct roles for two membrane-localized transcriptional activators on a single promoter. Mol. Microbiol. 2000, 38:67-84.
    • (2000) Mol. Microbiol. , vol.38 , pp. 67-84
    • Krukonis, E.S.1    Yu, R.R.2    Dirita, V.J.3
  • 69
    • 0033978638 scopus 로고    scopus 로고
    • The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases
    • LaPointe C.F., Taylor R.K. The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases. J. Biol. Chem. 2000, 275:1502-1510.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1502-1510
    • LaPointe, C.F.1    Taylor, R.K.2
  • 70
    • 33745712466 scopus 로고    scopus 로고
    • The Salmonella enterica serovar Typhi Vi capsule and self-association pili share controls on expression
    • Lee F.K., Morris C., Hackett J. The Salmonella enterica serovar Typhi Vi capsule and self-association pili share controls on expression. FEMS Microbiol. Lett. 2006, 261:41-46.
    • (2006) FEMS Microbiol. Lett. , vol.261 , pp. 41-46
    • Lee, F.K.1    Morris, C.2    Hackett, J.3
  • 71
    • 84862777302 scopus 로고    scopus 로고
    • Structure of the Vibrio cholerae Type IVb Pilus and stability comparison with the Neisseria gonorrhoeae type IVa pilus
    • Li J., Egelman E.H., Craig L. Structure of the Vibrio cholerae Type IVb Pilus and stability comparison with the Neisseria gonorrhoeae type IVa pilus. J. Mol. Biol. 2012, 418:47-64.
    • (2012) J. Mol. Biol. , vol.418 , pp. 47-64
    • Li, J.1    Egelman, E.H.2    Craig, L.3
  • 72
    • 84860328998 scopus 로고    scopus 로고
    • Outer membrane targeting, ultrastructure, and single molecule localization of the enteropathogenic Escherichia coli type IV pilus secretin BfpB
    • Lieberman J.A., Frost N.A., Hoppert M., Fernandes P.J., Vogt S.L., Raivio T.L., Blanpied T.A., Donnenberg M.S. Outer membrane targeting, ultrastructure, and single molecule localization of the enteropathogenic Escherichia coli type IV pilus secretin BfpB. J. Bacteriol. 2012, 194:1646-1658.
    • (2012) J. Bacteriol. , vol.194 , pp. 1646-1658
    • Lieberman, J.A.1    Frost, N.A.2    Hoppert, M.3    Fernandes, P.J.4    Vogt, S.L.5    Raivio, T.L.6    Blanpied, T.A.7    Donnenberg, M.S.8
  • 73
    • 28044455049 scopus 로고    scopus 로고
    • Degradation of the membrane-localized virulence activator TcpP by the YaeL protease in Vibrio cholerae
    • Matson J.S., DiRita V.J. Degradation of the membrane-localized virulence activator TcpP by the YaeL protease in Vibrio cholerae. Proc. Natl. Acad. Sci. U S A 2005, 102:16403-16408.
    • (2005) Proc. Natl. Acad. Sci. U S A , vol.102 , pp. 16403-16408
    • Matson, J.S.1    DiRita, V.J.2
  • 74
    • 77952563493 scopus 로고    scopus 로고
    • Longus, a type IV pilus of enterotoxigenic Escherichia coli, is involved in adherence to intestinal epithelial cells
    • Mazariego-Espinosa K., Cruz A., Ledesma M.A., Ochoa S.A., Xicohtencatl-Cortes J. Longus, a type IV pilus of enterotoxigenic Escherichia coli, is involved in adherence to intestinal epithelial cells. J. Bacteriol. 2010, 192:2791-2800.
    • (2010) J. Bacteriol. , vol.192 , pp. 2791-2800
    • Mazariego-Espinosa, K.1    Cruz, A.2    Ledesma, M.A.3    Ochoa, S.A.4    Xicohtencatl-Cortes, J.5
  • 76
    • 80051559805 scopus 로고    scopus 로고
    • The inner membrane subassembly of the enteropathogenic Escherichia coli bundle-forming pilus machine
    • Milgotina E.I., Lieberman J.A., Donnenberg M.S. The inner membrane subassembly of the enteropathogenic Escherichia coli bundle-forming pilus machine. Mol. Microbiol. 2011, 81:1125-1127.
    • (2011) Mol. Microbiol. , vol.81 , pp. 1125-1127
    • Milgotina, E.I.1    Lieberman, J.A.2    Donnenberg, M.S.3
  • 77
    • 0022255694 scopus 로고
    • Genetic analysis of the cholera toxin-positive regulatory gene toxR
    • Miller V.L., Mekalanos J.J. Genetic analysis of the cholera toxin-positive regulatory gene toxR. J. Bacteriol. 1985, 163:580-585.
    • (1985) J. Bacteriol. , vol.163 , pp. 580-585
    • Miller, V.L.1    Mekalanos, J.J.2
  • 78
    • 0037369743 scopus 로고    scopus 로고
    • The shufflon of Salmonella enterica serovar Typhi regulates type IVB pilus-mediated bacterial self-association
    • Morris C., Yip C.M., Tsui I.S., Wong D.K., Hackett J. The shufflon of Salmonella enterica serovar Typhi regulates type IVB pilus-mediated bacterial self-association. Infect. Immun. 2003, 71:1141-1146.
    • (2003) Infect. Immun. , vol.71 , pp. 1141-1146
    • Morris, C.1    Yip, C.M.2    Tsui, I.S.3    Wong, D.K.4    Hackett, J.5
  • 79
    • 0032856768 scopus 로고    scopus 로고
    • Differential transcription of the tcpPH operon confers biotype-specific control of the Vibrio cholerae ToxR virulence regulon
    • Murley Y.M., Carroll P.A., Skorupski K., Taylor R.K., Calderwood S.B. Differential transcription of the tcpPH operon confers biotype-specific control of the Vibrio cholerae ToxR virulence regulon. Infect. Immun. 1999, 67:5117-5123.
    • (1999) Infect. Immun. , vol.67 , pp. 5117-5123
    • Murley, Y.M.1    Carroll, P.A.2    Skorupski, K.3    Taylor, R.K.4    Calderwood, S.B.5
  • 81
    • 0026345424 scopus 로고
    • Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader peptidase
    • Nunn D.N., Lory S. Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader peptidase. Proc. Natl. Acad. Sci. U S A 1991, 88:3281-3285.
    • (1991) Proc. Natl. Acad. Sci. U S A , vol.88 , pp. 3281-3285
    • Nunn, D.N.1    Lory, S.2
  • 82
    • 0033941006 scopus 로고    scopus 로고
    • Vibrio cholerae H-NS silences virulence gene expression at multiple steps in the ToxR regulatory cascade
    • Nye M.B., Pfau J.D., Skorupski K., Taylor R.K. Vibrio cholerae H-NS silences virulence gene expression at multiple steps in the ToxR regulatory cascade. J. Bacteriol. 2000, 182:4295-4303.
    • (2000) J. Bacteriol. , vol.182 , pp. 4295-4303
    • Nye, M.B.1    Pfau, J.D.2    Skorupski, K.3    Taylor, R.K.4
  • 83
    • 0026939131 scopus 로고
    • TCP pilus biosynthesis in Vibrio cholerae O1: gene sequence of tcpC encoding an outer membrane lipoprotein
    • Ogierman M.A., Manning P.A. TCP pilus biosynthesis in Vibrio cholerae O1: gene sequence of tcpC encoding an outer membrane lipoprotein. FEMS Microbiol. Lett. 1992, 76:179-184.
    • (1992) FEMS Microbiol. Lett. , vol.76 , pp. 179-184
    • Ogierman, M.A.1    Manning, P.A.2
  • 84
    • 0026082664 scopus 로고
    • ToxR regulates the production of lipoproteins and the expression of serum resistance in Vibrio cholerae
    • Parsot C., Taxman E., Mekalanos J.J. ToxR regulates the production of lipoproteins and the expression of serum resistance in Vibrio cholerae. Proc. Natl. Acad. Sci. U S A 1991, 88:1641-1645.
    • (1991) Proc. Natl. Acad. Sci. U S A , vol.88 , pp. 1641-1645
    • Parsot, C.1    Taxman, E.2    Mekalanos, J.J.3
  • 85
    • 0032563102 scopus 로고    scopus 로고
    • Amino acid substitutions in PilD, a bifunctional enzyme of Pseudomonas aeruginosa. Effect on leader peptidase and N-methyltransferase activities in vitro and in vivo
    • Pepe J.C., Lory S. Amino acid substitutions in PilD, a bifunctional enzyme of Pseudomonas aeruginosa. Effect on leader peptidase and N-methyltransferase activities in vitro and in vivo. J. Biol. Chem. 1998, 273:19120-19129.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19120-19129
    • Pepe, J.C.1    Lory, S.2
  • 86
    • 33748993158 scopus 로고    scopus 로고
    • Genetic analysis of the requirement for flp-2, tadV, and rcpB in Actinobacillus actinomycetemcomitans biofilm formation
    • Perez B.A., Planet P.J., Kachlany S.C., Tomich M., Fine D.H., Figurski D.H. Genetic analysis of the requirement for flp-2, tadV, and rcpB in Actinobacillus actinomycetemcomitans biofilm formation. J. Bacteriol. 2006, 188:6361-6375.
    • (2006) J. Bacteriol. , vol.188 , pp. 6361-6375
    • Perez, B.A.1    Planet, P.J.2    Kachlany, S.C.3    Tomich, M.4    Fine, D.H.5    Figurski, D.H.6
  • 87
    • 84856565557 scopus 로고    scopus 로고
    • The product of tadZ, a new member of the parA/minD superfamily, localizes to a pole in Aggregatibacter actinomycetemcomitans
    • Perez-Cheeks B.A., Planet P.J., Sarkar I.N., Clock S.A., Xu Q., Figurski D.H. The product of tadZ, a new member of the parA/minD superfamily, localizes to a pole in Aggregatibacter actinomycetemcomitans. Mol. Microbiol. 2012, 83:694-711.
    • (2012) Mol. Microbiol. , vol.83 , pp. 694-711
    • Perez-Cheeks, B.A.1    Planet, P.J.2    Sarkar, I.N.3    Clock, S.A.4    Xu, Q.5    Figurski, D.H.6
  • 88
    • 0031753364 scopus 로고    scopus 로고
    • Mutations in toxR and toxS that separate transcriptional activation from DNA binding at the cholera toxin gene promoter
    • Pfau J.D., Taylor R.K. Mutations in toxR and toxS that separate transcriptional activation from DNA binding at the cholera toxin gene promoter. J. Bacteriol. 1998, 180:4724-4733.
    • (1998) J. Bacteriol. , vol.180 , pp. 4724-4733
    • Pfau, J.D.1    Taylor, R.K.2
  • 90
    • 0038617707 scopus 로고    scopus 로고
    • The widespread colonization island of Actinobacillus actinomycetemcomitans
    • Planet P.J., Kachlany S.C., Fine D.H., DeSalle R., Figurski D.H. The widespread colonization island of Actinobacillus actinomycetemcomitans. Nat. Genet. 2003, 34:193-198.
    • (2003) Nat. Genet. , vol.34 , pp. 193-198
    • Planet, P.J.1    Kachlany, S.C.2    Fine, D.H.3    DeSalle, R.4    Figurski, D.H.5
  • 91
    • 8544239349 scopus 로고    scopus 로고
    • Direct and indirect transcriptional activation of virulence genes by an AraC-like protein, PerA from enteropathogenic Escherichia coli
    • Porter M.E., Mitchell P., Roe A.J., Free A., Smith D.G., Gally D.L. Direct and indirect transcriptional activation of virulence genes by an AraC-like protein, PerA from enteropathogenic Escherichia coli. Mol. Microbiol. 2004, 54:1117-1133.
    • (2004) Mol. Microbiol. , vol.54 , pp. 1117-1133
    • Porter, M.E.1    Mitchell, P.2    Roe, A.J.3    Free, A.4    Smith, D.G.5    Gally, D.L.6
  • 92
    • 27944462141 scopus 로고    scopus 로고
    • Characterization of functional domains of the Vibrio cholerae virulence regulator ToxT
    • Prouty M.G., Osorio C.R., Klose K.E. Characterization of functional domains of the Vibrio cholerae virulence regulator ToxT. Mol. Microbiol. 2005, 58:1143-1156.
    • (2005) Mol. Microbiol. , vol.58 , pp. 1143-1156
    • Prouty, M.G.1    Osorio, C.R.2    Klose, K.E.3
  • 93
    • 0029928660 scopus 로고    scopus 로고
    • The bundle-forming pili of enteropathogenic Escherichia coli: transcriptional regulation by environmental signals
    • Puente J.L., Bieber D., Ramer S.W., Murray W., Schoolnik G.K. The bundle-forming pili of enteropathogenic Escherichia coli: transcriptional regulation by environmental signals. Mol. Microbiol. 1996, 20:87-100.
    • (1996) Mol. Microbiol. , vol.20 , pp. 87-100
    • Puente, J.L.1    Bieber, D.2    Ramer, S.W.3    Murray, W.4    Schoolnik, G.K.5
  • 95
    • 0029904580 scopus 로고    scopus 로고
    • BfpB, an outer membrane lipoprotein required for the biogenesis of bundle-forming pili in enteropathogenic Escherichia coli
    • Ramer S.W., Bieber D., Schoolnik G.K. BfpB, an outer membrane lipoprotein required for the biogenesis of bundle-forming pili in enteropathogenic Escherichia coli. J. Bacteriol. 1996, 178:6555-6563.
    • (1996) J. Bacteriol. , vol.178 , pp. 6555-6563
    • Ramer, S.W.1    Bieber, D.2    Schoolnik, G.K.3
  • 96
    • 0036279961 scopus 로고    scopus 로고
    • The type IV pilus assembly complex: biogenic interactions among the bundle-forming pilus proteins of enteropathogenic Escherichia coli
    • Ramer S.W., Schoolnik G.K., Wu C.Y., Hwang J., Schmidt S.A., Bieber D. The type IV pilus assembly complex: biogenic interactions among the bundle-forming pilus proteins of enteropathogenic Escherichia coli. J. Bacteriol. 2002, 184:3457-3465.
    • (2002) J. Bacteriol. , vol.184 , pp. 3457-3465
    • Ramer, S.W.1    Schoolnik, G.K.2    Wu, C.Y.3    Hwang, J.4    Schmidt, S.A.5    Bieber, D.6
  • 97
    • 0034088899 scopus 로고    scopus 로고
    • The pilL and pilN genes of IncI1 plasmids R64 and ColIb-P9 encode outer membrane lipoproteins responsible for thin pilus biogenesis
    • Sakai D., Komano T. The pilL and pilN genes of IncI1 plasmids R64 and ColIb-P9 encode outer membrane lipoproteins responsible for thin pilus biogenesis. Plasmid 2000, 43:149-152.
    • (2000) Plasmid , vol.43 , pp. 149-152
    • Sakai, D.1    Komano, T.2
  • 98
    • 0036135642 scopus 로고    scopus 로고
    • Genes required for plasmid R64 thin-pilus biogenesis: identification and localization of products of the pilK, pilM, pilO, pilP, pilR, and pilT genes
    • Sakai D., Komano T. Genes required for plasmid R64 thin-pilus biogenesis: identification and localization of products of the pilK, pilM, pilO, pilP, pilR, and pilT genes. J. Bacteriol. 2002, 184:444-451.
    • (2002) J. Bacteriol. , vol.184 , pp. 444-451
    • Sakai, D.1    Komano, T.2
  • 99
    • 0035947655 scopus 로고    scopus 로고
    • Atpase activity and multimer formation of Pilq protein are required for thin pilus biogenesis in plasmid R64
    • Sakai D., Horiuchi T., Komano T. Atpase activity and multimer formation of Pilq protein are required for thin pilus biogenesis in plasmid R64. J. Biol. Chem. 2001, 276:17968-17975.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17968-17975
    • Sakai, D.1    Horiuchi, T.2    Komano, T.3
  • 100
    • 0023404513 scopus 로고
    • Effect of anaerobiosis on the surface ultrastructure and surface proteins of Actinobacillus actinomycetemcomitans (Haemophilus actinomycetemcomitans)
    • Scannapieco F.A., Millar S.J., Reynolds H.S., Zambon J.J., Levine M.J. Effect of anaerobiosis on the surface ultrastructure and surface proteins of Actinobacillus actinomycetemcomitans (Haemophilus actinomycetemcomitans). Infect. Immun. 1987, 55:2320-2323.
    • (1987) Infect. Immun. , vol.55 , pp. 2320-2323
    • Scannapieco, F.A.1    Millar, S.J.2    Reynolds, H.S.3    Zambon, J.J.4    Levine, M.J.5
  • 102
    • 0034906825 scopus 로고    scopus 로고
    • Structure-function analysis of BfpB, a secretin-like protein encoded by the bundle-forming-pilus operon of enteropathogenic Escherichia coli
    • Schmidt S.A., Bieber D., Ramer S.W., Hwang J., Wu C.Y., Schoolnik G. Structure-function analysis of BfpB, a secretin-like protein encoded by the bundle-forming-pilus operon of enteropathogenic Escherichia coli. J. Bacteriol. 2001, 183:4848-4859.
    • (2001) J. Bacteriol. , vol.183 , pp. 4848-4859
    • Schmidt, S.A.1    Bieber, D.2    Ramer, S.W.3    Hwang, J.4    Wu, C.Y.5    Schoolnik, G.6
  • 103
    • 0036667437 scopus 로고    scopus 로고
    • BfpU, a soluble protein essential for type IV pilus biogenesis in enteropathogenic Escherichia coli
    • Schreiber W., Stone K.D., Strong M.A., DeTolla L.J., Hoppert M., Donnenberg M.S. BfpU, a soluble protein essential for type IV pilus biogenesis in enteropathogenic Escherichia coli. Microbiology 2002, 148:2507-2518.
    • (2002) Microbiology , vol.148 , pp. 2507-2518
    • Schreiber, W.1    Stone, K.D.2    Strong, M.A.3    DeTolla, L.J.4    Hoppert, M.5    Donnenberg, M.S.6
  • 105
    • 36549014037 scopus 로고    scopus 로고
    • Molecular mechanisms of virstatin resistance by non-O1/non-O139 strains of Vibrio cholerae
    • Shakhnovich E.A., Sturtevant D., Mekalanos J.J. Molecular mechanisms of virstatin resistance by non-O1/non-O139 strains of Vibrio cholerae. Mol. Microbiol. 2007, 66:1331-1341.
    • (2007) Mol. Microbiol. , vol.66 , pp. 1331-1341
    • Shakhnovich, E.A.1    Sturtevant, D.2    Mekalanos, J.J.3
  • 106
    • 38949108710 scopus 로고    scopus 로고
    • Novel class of mutations of pilS mutants, encoding plasmid R64 type IV prepilin: interface of PilS-PilV interactions
    • Shimoda E., Muto T., Horiuchi T., Furuya N., Komano T. Novel class of mutations of pilS mutants, encoding plasmid R64 type IV prepilin: interface of PilS-PilV interactions. J. Bacteriol. 2008, 190:1202-1208.
    • (2008) J. Bacteriol. , vol.190 , pp. 1202-1208
    • Shimoda, E.1    Muto, T.2    Horiuchi, T.3    Furuya, N.4    Komano, T.5
  • 107
    • 0034600835 scopus 로고    scopus 로고
    • Identification and cell cycle control of a novel pilus system in Caulobacter crescentus
    • Skerker J.M., Shapiro L. Identification and cell cycle control of a novel pilus system in Caulobacter crescentus. EMBO J. 2000, 19:3223-3234.
    • (2000) EMBO J. , vol.19 , pp. 3223-3234
    • Skerker, J.M.1    Shapiro, L.2
  • 108
    • 84859922301 scopus 로고    scopus 로고
    • Development of a genetic tool for activating chromosomal expression of cryptic or tightly regulated loci in Pseudomonas aeruginosa
    • Spagnolo J., Bigot S., Denis Y., Bordi C., de Bentzmann S. Development of a genetic tool for activating chromosomal expression of cryptic or tightly regulated loci in Pseudomonas aeruginosa. Plasmid 2012, 67:245-251.
    • (2012) Plasmid , vol.67 , pp. 245-251
    • Spagnolo, J.1    Bigot, S.2    Denis, Y.3    Bordi, C.4    de Bentzmann, S.5
  • 109
    • 0029879021 scopus 로고    scopus 로고
    • A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for the biogenesis of a type IV pilus
    • Stone K.D., Zhang H.Z., Carlson L.K., Donnenberg M.S. A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for the biogenesis of a type IV pilus. Mol. Microbiol. 1996, 20:325-337.
    • (1996) Mol. Microbiol. , vol.20 , pp. 325-337
    • Stone, K.D.1    Zhang, H.Z.2    Carlson, L.K.3    Donnenberg, M.S.4
  • 110
    • 46049119425 scopus 로고    scopus 로고
    • Integration host factor positively regulates virulence gene expression in Vibrio cholerae
    • Stonehouse E., Kovacikova G., Taylor R.K., Skorupski K. Integration host factor positively regulates virulence gene expression in Vibrio cholerae. J. Bacteriol. 2008, 190:4736-4748.
    • (2008) J. Bacteriol. , vol.190 , pp. 4736-4748
    • Stonehouse, E.1    Kovacikova, G.2    Taylor, R.K.3    Skorupski, K.4
  • 111
    • 33748076140 scopus 로고    scopus 로고
    • The Salmonella enterica serovar Typhi type IVB self-association pili are detached from the bacterial cell by the PilV minor pilus proteins
    • Tam C.K., Morris C., Hackett J. The Salmonella enterica serovar Typhi type IVB self-association pili are detached from the bacterial cell by the PilV minor pilus proteins. Infect. Immun. 2006, 74:5414-5418.
    • (2006) Infect. Immun. , vol.74 , pp. 5414-5418
    • Tam, C.K.1    Morris, C.2    Hackett, J.3
  • 112
    • 0039391898 scopus 로고
    • Use of phoA gene fusions to identify a pilus colonization factor coordinately regulated with cholera toxin
    • Taylor R.K., Miller V.L., Furlong D.B., Mekalanos J.J. Use of phoA gene fusions to identify a pilus colonization factor coordinately regulated with cholera toxin. Proc. Natl. Acad. Sci. U S A 1987, 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
  • 113
    • 23944431512 scopus 로고    scopus 로고
    • Cyclic diguanylate regulates Vibrio cholerae virulence gene expression
    • Tischler A.D., Camilli A. Cyclic diguanylate regulates Vibrio cholerae virulence gene expression. Infect. Immun. 2005, 73:5873-5882.
    • (2005) Infect. Immun. , vol.73 , pp. 5873-5882
    • Tischler, A.D.1    Camilli, A.2
  • 114
    • 0029849368 scopus 로고    scopus 로고
    • Cloning and characterization of bfpTVW, genes required for the transcriptional activation of bfpA in enteropathogenic Escherichia coli
    • Tobe T., Schoolnik G.K., Sohel I., Bustamante V.H., Puente J.L. Cloning and characterization of bfpTVW, genes required for the transcriptional activation of bfpA in enteropathogenic Escherichia coli. Mol. Microbiol. 1996, 21:963-975.
    • (1996) Mol. Microbiol. , vol.21 , pp. 963-975
    • Tobe, T.1    Schoolnik, G.K.2    Sohel, I.3    Bustamante, V.H.4    Puente, J.L.5
  • 115
    • 33749345746 scopus 로고    scopus 로고
    • The TadV protein of Actinobacillus actinomycetemcomitans is a novel aspartic acid prepilin peptidase required for maturation of the Flp1 pilin and TadE and TadF pseudopilins
    • Tomich M., Fine D.H., Figurski D.H. The TadV protein of Actinobacillus actinomycetemcomitans is a novel aspartic acid prepilin peptidase required for maturation of the Flp1 pilin and TadE and TadF pseudopilins. J. Bacteriol. 2006, 188:6899-6914.
    • (2006) J. Bacteriol. , vol.188 , pp. 6899-6914
    • Tomich, M.1    Fine, D.H.2    Figurski, D.H.3
  • 116
    • 34247221579 scopus 로고    scopus 로고
    • The tad locus: postcards from the widespread colonization island
    • Tomich M., Planet P.J., Figurski D.H. The tad locus: postcards from the widespread colonization island. Nat. Rev. Microbiol. 2007, 5:363-375.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 363-375
    • Tomich, M.1    Planet, P.J.2    Figurski, D.H.3
  • 117
    • 34250329174 scopus 로고    scopus 로고
    • Membrane association and multimerization of TcpT, the cognate ATPase ortholog of the Vibrio cholerae toxin-coregulated-pilus biogenesis apparatus
    • Tripathi S.A., Taylor R.K. Membrane association and multimerization of TcpT, the cognate ATPase ortholog of the Vibrio cholerae toxin-coregulated-pilus biogenesis apparatus. J. Bacteriol. 2007, 189:4401-4409.
    • (2007) J. Bacteriol. , vol.189 , pp. 4401-4409
    • Tripathi, S.A.1    Taylor, R.K.2
  • 118
    • 0141668952 scopus 로고    scopus 로고
    • The type IVB pili of Salmonella enterica serovar Typhi bind to the cystic fibrosis transmembrane conductance regulator
    • Tsui I.S., Yip C.M., Hackett J., Morris C. The type IVB pili of Salmonella enterica serovar Typhi bind to the cystic fibrosis transmembrane conductance regulator. Infect. Immun. 2003, 71:6049-6050.
    • (2003) Infect. Immun. , vol.71 , pp. 6049-6050
    • Tsui, I.S.1    Yip, C.M.2    Hackett, J.3    Morris, C.4
  • 119
    • 0037487270 scopus 로고    scopus 로고
    • A lytic transglycosylase homologue, PleA, is required for the assembly of pili and the flagellum at the Caulobacter crescentus cell pole
    • Viollier P.H., Shapiro L. A lytic transglycosylase homologue, PleA, is required for the assembly of pili and the flagellum at the Caulobacter crescentus cell pole. Mol. Microbiol. 2003, 49:331-345.
    • (2003) Mol. Microbiol. , vol.49 , pp. 331-345
    • Viollier, P.H.1    Shapiro, L.2
  • 120
    • 77952802182 scopus 로고    scopus 로고
    • The Cpx envelope stress response both facilitates and inhibits elaboration of the enteropathogenic Escherichia coli bundle-forming pilus
    • Vogt S.L., Nevesinjac A.Z., Humphries R.M., Donnenberg M.S., Armstrong G.D., Raivio T.L. The Cpx envelope stress response both facilitates and inhibits elaboration of the enteropathogenic Escherichia coli bundle-forming pilus. Mol. Microbiol. 2010, 76:1095-1110.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1095-1110
    • Vogt, S.L.1    Nevesinjac, A.Z.2    Humphries, R.M.3    Donnenberg, M.S.4    Armstrong, G.D.5    Raivio, T.L.6
  • 121
    • 0030057090 scopus 로고    scopus 로고
    • Lysogenic conversion by a filamentous phage encoding cholera toxin
    • Waldor M.K., Mekalanos J.J. Lysogenic conversion by a filamentous phage encoding cholera toxin. Science 1996, 272:1910-1914.
    • (1996) Science , vol.272 , pp. 1910-1914
    • Waldor, M.K.1    Mekalanos, J.J.2
  • 122
    • 23444435416 scopus 로고    scopus 로고
    • Type IVB piliated Salmonella typhi enhance IL-6 and NF-kappaB production in human monocytic THP-1 cells through activation of protein kinase C
    • Wang F., Zhang X.L., Zhou Y., Ye L., Qi Z., Wu J. Type IVB piliated Salmonella typhi enhance IL-6 and NF-kappaB production in human monocytic THP-1 cells through activation of protein kinase C. Immunobiology 2005, 210:283-293.
    • (2005) Immunobiology , vol.210 , pp. 283-293
    • Wang, F.1    Zhang, X.L.2    Zhou, Y.3    Ye, L.4    Qi, Z.5    Wu, J.6
  • 123
    • 19744373475 scopus 로고    scopus 로고
    • Genetic basis for conversion of rough-to-smooth colony morphology in Actinobacillus actinomycetemcomitans
    • Wang Y., Liu A., Chen C. Genetic basis for conversion of rough-to-smooth colony morphology in Actinobacillus actinomycetemcomitans. Infect. Immun. 2005, 73:3749-3753.
    • (2005) Infect. Immun. , vol.73 , pp. 3749-3753
    • Wang, Y.1    Liu, A.2    Chen, C.3
  • 124
    • 79952947161 scopus 로고    scopus 로고
    • The complexity of ToxT-dependent transcription in Vibrio cholerae
    • Weber G.G., Klose K.E. The complexity of ToxT-dependent transcription in Vibrio cholerae. Indian J. Med. Res. 2011, 133:201-206.
    • (2011) Indian J. Med. Res. , vol.133 , pp. 201-206
    • Weber, G.G.1    Klose, K.E.2
  • 125
    • 70350169211 scopus 로고    scopus 로고
    • The TviA auxiliary protein renders the Salmonella enterica serotype Typhi RcsB regulon responsive to changes in osmolarity
    • Winter S.E., Winter M.G., Thiennimitr P., Gerriets V.A., Nuccio S.P., Russmann H., Baumler A.J. The TviA auxiliary protein renders the Salmonella enterica serotype Typhi RcsB regulon responsive to changes in osmolarity. Mol. Microbiol. 2009, 74:175-193.
    • (2009) Mol. Microbiol. , vol.74 , pp. 175-193
    • Winter, S.E.1    Winter, M.G.2    Thiennimitr, P.3    Gerriets, V.A.4    Nuccio, S.P.5    Russmann, H.6    Baumler, A.J.7
  • 126
    • 33645471024 scopus 로고    scopus 로고
    • The toxbox: specific DNA sequence requirements for activation of Vibrio cholerae virulence genes by ToxT
    • Withey J.H., DiRita V.J. The toxbox: specific DNA sequence requirements for activation of Vibrio cholerae virulence genes by ToxT. Mol. Microbiol. 2006, 59:1779-1789.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1779-1789
    • Withey, J.H.1    DiRita, V.J.2
  • 127
    • 3843129685 scopus 로고    scopus 로고
    • NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus
    • Xu X.F., Tan Y.W., Lam L., Hackett J., Zhang M., Mok Y.K. NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus. J. Biol. Chem. 2004, 279:31599-31605.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31599-31605
    • Xu, X.F.1    Tan, Y.W.2    Lam, L.3    Hackett, J.4    Zhang, M.5    Mok, Y.K.6
  • 129
    • 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 J.A., Donnenberg M.S. Structure of an essential type IV pilus biogenesis protein provides insights into pilus and type II secretion systems. J. Mol. Biol. 2012, 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
  • 130
    • 0032963612 scopus 로고    scopus 로고
    • Twelve pil genes are required for biogenesis of the R64 thin pilus
    • Yoshida T., Kim S.R., Komano T. Twelve pil genes are required for biogenesis of the R64 thin pilus. J. Bacteriol. 1999, 181:2038-2043.
    • (1999) J. Bacteriol. , vol.181 , pp. 2038-2043
    • Yoshida, T.1    Kim, S.R.2    Komano, T.3
  • 132
    • 0034115689 scopus 로고    scopus 로고
    • Salmonella enterica serovar typhi uses type IVB pili to enter human intestinal epithelial cells
    • Zhang X.L., Tsui I.S., Yip C.M., Fung A.W., Wong D.K., Dai X., Yang Y., Hackett J., et al. Salmonella enterica serovar typhi uses type IVB pili to enter human intestinal epithelial cells. Infect. Immun. 2000, 68:3067-3073.
    • (2000) Infect. Immun. , vol.68 , pp. 3067-3073
    • Zhang, X.L.1    Tsui, I.S.2    Yip, C.M.3    Fung, A.W.4    Wong, D.K.5    Dai, X.6    Yang, Y.7    Hackett, J.8


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