메뉴 건너뛰기




Volumn 79, Issue 10, 2011, Pages 4068-4080

Functional characterization of epsc, a component of the type II secretion system, in the pathogenicity of vibrio vulnificus

Author keywords

[No Author keywords available]

Indexed keywords

ELASTASE; HEMOLYSIN; OUTER MEMBRANE PROTEIN;

EID: 80855136569     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.05351-11     Document Type: Article
Times cited : (15)

References (63)
  • 1
    • 35348892037 scopus 로고    scopus 로고
    • Type VII secretion-mycobacteria show the way
    • Abdallah, M. A., et al. 2007. Type VII secretion-mycobacteria show the way. Nat. Rev. Microbiol. 5:883-891.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 883-891
    • Abdallah, M.A.1
  • 2
    • 1842686182 scopus 로고    scopus 로고
    • The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold
    • Abendroth, J., A. E. Rice, K. McLuskey, M. Bagdasarian, and W. G. J. Hol. 2004. The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold. J. Mol. Biol. 338:585-596.
    • (2004) J. Mol. Biol. , vol.338 , pp. 585-596
    • Abendroth, J.1    Rice, A.E.2    McLuskey, K.3    Bagdasarian, M.4    Hol, W.G.J.5
  • 3
    • 0021717199 scopus 로고
    • Mutants of Erwinia chrysanthemi defective in secretion of pectinase and cellulase
    • Andro, T., et al. 1984. Mutants of Erwinia chrysanthemi defective in secretion of pectinase and cellulase. J. Bacteriol. 160:1199-1203.
    • (1984) J. Bacteriol. , vol.160 , pp. 1199-1203
    • Andro, T.1
  • 4
    • 0012976388 scopus 로고    scopus 로고
    • Evidence that expression of Vibrio vulnificus hemolysin gene is dependent on cyclic AMP and cyclic AMP receptor protein
    • Bang, Y. B., S. E. Lee, J. H. Rhee, and S. H. Choi. 1999. Evidence that expression of Vibrio vulnificus hemolysin gene is dependent on cyclic AMP and cyclic AMP receptor protein. J. Bacteriol. 181:7639-7642.
    • (1999) J. Bacteriol. , vol.181 , pp. 7639-7642
    • Bang, Y.B.1    Lee, S.E.2    Rhee, J.H.3    Choi, S.H.4
  • 5
  • 6
    • 9244243093 scopus 로고    scopus 로고
    • Vibrio cholerae strains with mutations in an atypical type I secretion system accumulate RTX toxin intracellularly
    • Boardman, B. K., and K. J. Satchell. 2004. Vibrio cholerae strains with mutations in an atypical type I secretion system accumulate RTX toxin intracellularly. J. Bacteriol. 186:8137-8143.
    • (2004) J. Bacteriol. , vol.186 , pp. 8137-8143
    • Boardman, B.K.1    Satchell, K.J.2
  • 7
    • 27844506497 scopus 로고    scopus 로고
    • Type II secretion: a protein secretion system for all seasons
    • Cianciotto, N. P. 2005. Type II secretion: a protein secretion system for all seasons. Trends Microbiol. 13:581-588.
    • (2005) Trends Microbiol. , vol.13 , pp. 581-588
    • Cianciotto, N.P.1
  • 8
    • 34447634995 scopus 로고    scopus 로고
    • Legionella pneumophila type II secretome reveals unique exoproteins and a chitinase that promotes bacterial persistence in the lung
    • DebRoy, S., J. Dao, M. Soderberg, O. Rossier, and N. P. Cianciotto. 2006. Legionella pneumophila type II secretome reveals unique exoproteins and a chitinase that promotes bacterial persistence in the lung. Proc. Natl. Acad. Sci. U. S. A. 103:19146-19151.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 19146-19151
    • DebRoy, S.1    Dao, J.2    Soderberg, M.3    Rossier, O.4    Cianciotto, N.P.5
  • 9
    • 0034865707 scopus 로고    scopus 로고
    • Isolation and characterization of a Vibrio vulnificus mutant deficient in both extracellular metalloprotease and cytolysin
    • Fan, J.-J., C.-P. Shao, Y.-C. Ho, C.-K. Yu, and L.-I. Hor. 2001. Isolation and characterization of a Vibrio vulnificus mutant deficient in both extracellular metalloprotease and cytolysin. Infect. Immun. 69:5943-5948.
    • (2001) Infect. Immun. , vol.69 , pp. 5943-5948
    • Fan, J.-J.1    Shao, C.-P.2    Ho, Y.-C.3    Yu, C.-K.4    Hor, L.-I.5
  • 10
    • 8844269404 scopus 로고    scopus 로고
    • The underlying mechanisms of type II protein secretion
    • Filloux, A. 2004. The underlying mechanisms of type II protein secretion. Biochim. Biophys. Acta 1694:163-179.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 163-179
    • Filloux, A.1
  • 11
    • 0029991619 scopus 로고    scopus 로고
    • Bacterial collagenases and collagen-degrading enzymes and their potential role in human disease
    • Harrington, D. J. 1996. Bacterial collagenases and collagen-degrading enzymes and their potential role in human disease. Infect. Immun. 64:1885-1891.
    • (1996) Infect. Immun. , vol.64 , pp. 1885-1891
    • Harrington, D.J.1
  • 12
    • 79952105809 scopus 로고    scopus 로고
    • A comprehensive review of Vibrio vulnificus: an important cause of severe sepsis and skin and soft-tissue infection
    • Horeseman, M. A., and S. Surani. 2010. A comprehensive review of Vibrio vulnificus: an important cause of severe sepsis and skin and soft-tissue infection. J. Infect. Dis. 15:157-166.
    • (2010) J. Infect. Dis. , vol.15 , pp. 157-166
    • Horeseman, M.A.1    Surani, S.2
  • 13
    • 0033855435 scopus 로고    scopus 로고
    • Construction and phenotypic evaluation of a Vibrio vulnificus vvpE mutant for elastolytic protease
    • Jeong, K. C., et al. 2000. Construction and phenotypic evaluation of a Vibrio vulnificus vvpE mutant for elastolytic protease. Infect. Immun. 68:5096-5106.
    • (2000) Infect. Immun. , vol.68 , pp. 5096-5106
    • Jeong, K.C.1
  • 15
    • 37449017833 scopus 로고    scopus 로고
    • Mapping critical interactive sites within the periplasmic domain of the Vibrio cholerae type II secretion protein Eps M
    • Johnson, T. L., M. E. Scott, and M. Sandkvist. 2007. Mapping critical interactive sites within the periplasmic domain of the Vibrio cholerae type II secretion protein EpsM. J. Bacteriol. 189:9082-9089.
    • (2007) J. Bacteriol. , vol.189 , pp. 9082-9089
    • Johnson, T.L.1    Scott, M.E.2    Sandkvist, M.3
  • 16
    • 65449185894 scopus 로고    scopus 로고
    • Vibrio vulnificus: disease and pathogenesis
    • Jones, M. K., and J. D. Oliver. 2009. Vibrio vulnificus: disease and pathogenesis. Infect. Immun. 77:1723-1733.
    • (2009) Infect. Immun. , vol.77 , pp. 1723-1733
    • Jones, M.K.1    Oliver, J.D.2
  • 18
    • 5644233706 scopus 로고    scopus 로고
    • The secretome of the plant pathogenic bacterium Erwinia chrysanthemi
    • Kazemi-Pour, N., G. Condemine, and N. Hugouvieux-Cotte-Pattat. 2004. The secretome of the plant pathogenic bacterium Erwinia chrysanthemi. Proteomics 4:3177-3186.
    • (2004) Proteomics , vol.4 , pp. 3177-3186
    • Kazemi-Pour, N.1    Condemine, G.2    Hugouvieux-Cotte-Pattat, N.3
  • 19
    • 0023715368 scopus 로고
    • Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria
    • Keen, N. T., S. Tamaki, D. Kobayashi, and D. Trollinger. 1988. Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria. Gene 70:191-197.
    • (1988) Gene , vol.70 , pp. 191-197
    • Keen, N.T.1    Tamaki, S.2    Kobayashi, D.3    Trollinger, D.4
  • 20
    • 60749136290 scopus 로고    scopus 로고
    • Vibrio vulnificusinduced death of human peripheral mononuclear cells requires activation of p38 and ERK1/2 MAPKs inhibited by diphenyleneiodonium chloride
    • Kim, W. H., S. Y. Goo, K.-H. Lee, and S.-J. Park. 2009. Vibrio vulnificusinduced death of human peripheral mononuclear cells requires activation of p38 and ERK1/2 MAPKs inhibited by diphenyleneiodonium chloride. Immunol. Invest. 38:31-48.
    • (2009) Immunol. Invest. , vol.38 , pp. 31-48
    • Kim, W.H.1    Goo, S.Y.2    Lee, K.-H.3    Park, S.-J.4
  • 21
    • 51449111702 scopus 로고    scopus 로고
    • Vibrio vulnificus-induced death of Jurkat T-cells requires activation of p38 mitogen-activated protein kinase by NADPH oxidase-derived reactive oxygen species
    • Kim, W. H., et al. 2008. Vibrio vulnificus-induced death of Jurkat T-cells requires activation of p38 mitogen-activated protein kinase by NADPH oxidase-derived reactive oxygen species. Cell. Immunol. 253:81-91.
    • (2008) Cell. Immunol. , vol.253 , pp. 81-91
    • Kim, W.H.1
  • 22
    • 40749157602 scopus 로고    scopus 로고
    • Vibrio vulnificus RTX toxin kills host cells only after contact of the bacteria with host cells
    • Kim, Y. R., et al. 2008. Vibrio vulnificus RTX toxin kills host cells only after contact of the bacteria with host cells. Cell. Microbiol. 10:848-862.
    • (2008) Cell. Microbiol. , vol.10 , pp. 848-862
    • Kim, Y.R.1
  • 23
    • 0023741616 scopus 로고
    • Syndromes of Vibrio vulnificus infections. Clinical and epidemiologic features in Florida cases, 1981-1987
    • Klontz, K. C., et al. 1988. Syndromes of Vibrio vulnificus infections. Clinical and epidemiologic features in Florida cases, 1981-1987. Ann. Intern. Med. 109:318-323.
    • (1988) Ann. Intern. Med. , vol.109 , pp. 318-323
    • Klontz, K.C.1
  • 24
    • 33748951751 scopus 로고    scopus 로고
    • Structural and functional studies of EpsC, a crucial component of the type 2 secretion system from Vibrio cholerae
    • Korotkov, K. V., B. Krumm, M. Bagdasarian, and W. G. J. Hoi. 2006. Structural and functional studies of EpsC, a crucial component of the type 2 secretion system from Vibrio cholerae. J. Mol. Biol. 363:311-321.
    • (2006) J. Mol. Biol. , vol.363 , pp. 311-321
    • Korotkov, K.V.1    Krumm, B.2    Bagdasarian, M.3    Hoi, W.G.J.4
  • 25
    • 0023241504 scopus 로고
    • Purification and characterization of an elastolytic protease of Vibrio vulnificus
    • Kothary, M. H., and A. S. Kreger. 1987. Purification and characterization of an elastolytic protease of Vibrio vulnificus. J. Gen. Microbiol. 133:1783-1791.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 1783-1791
    • Kothary, M.H.1    Kreger, A.S.2
  • 26
    • 0035861549 scopus 로고    scopus 로고
    • Vibrio vulnificus cytolysin induce superoxide anioninitiated apoptotic signaling pathway in human ECV304 cells
    • Kwon, K. B., et al. 2001. Vibrio vulnificus cytolysin induce superoxide anioninitiated apoptotic signaling pathway in human ECV304 cells. J. Biol. Chem. 276:47518-47523.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47518-47523
    • Kwon, K.B.1
  • 27
    • 56949101322 scopus 로고    scopus 로고
    • Vibrio vulnificus RTX toxin plays an important role in the apoptotic death of human intestinal epithelial cells exposed to Vibrio vulnificus
    • Lee, B. C., S. H. Choi, and T. S. Kim. 2008. Vibrio vulnificus RTX toxin plays an important role in the apoptotic death of human intestinal epithelial cells exposed to Vibrio vulnificus. Microbes Infect. 10:1504-1513.
    • (2008) Microbes Infect. , vol.10 , pp. 1504-1513
    • Lee, B.C.1    Choi, S.H.2    Kim, T.S.3
  • 28
    • 34248208219 scopus 로고    scopus 로고
    • Identification and characterization of the Vibrio vulnificus rtxA essential for cytotoxicity in vitro and virulence in mice
    • Lee, J. H., et al. 2007. Identification and characterization of the Vibrio vulnificus rtxA essential for cytotoxicity in vitro and virulence in mice. J. Microbiol. 45:146-152.
    • (2007) J. Microbiol. , vol.45 , pp. 146-152
    • Lee, J.H.1
  • 29
    • 42149186570 scopus 로고    scopus 로고
    • Vibrio vulnificus rtxE is important for virulence, and its expression is induced by exposure to host cells
    • Lee, B. C., et al. 2008. Vibrio vulnificus rtxE is important for virulence, and its expression is induced by exposure to host cells. Infect. Immun. 76:1509-1517.
    • (2008) Infect. Immun. , vol.76 , pp. 1509-1517
    • Lee, B.C.1
  • 30
    • 4744340688 scopus 로고    scopus 로고
    • Production of Vibrio vulnificus hemolysin in vivo and its pathogenic significance
    • Lee, S. E., et al. 2004. Production of Vibrio vulnificus hemolysin in vivo and its pathogenic significance. Biochem. Biophys. Res. Commun. 324:86-91.
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 86-91
    • Lee, S.E.1
  • 31
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C., and J. Beckwith. 1986. A genetic approach to analyzing membrane protein topology. Science 233:1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 32
    • 0031776687 scopus 로고    scopus 로고
    • Identification of an additional member of the secretin superfamily of proteins in Pseudomonas aeruginosa that is able to function in type II protein secretion
    • Martínez, A., P. Ostrovsky, and D. N. Nunn. 1998. Identification of an additional member of the secretin superfamily of proteins in Pseudomonas aeruginosa that is able to function in type II protein secretion. Mol. Microbiol. 28:1235-1246.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1235-1246
    • Martínez, A.1    Ostrovsky, P.2    Nunn, D.N.3
  • 33
    • 0029913592 scopus 로고    scopus 로고
    • Flagellin A is essential for the virulence of Vibrio anguillarum
    • Milton, D. L., R. O'Toole, P. Hörstedt, and W. H. Wolf. 1996. Flagellin A is essential for the virulence of Vibrio anguillarum. J. Bacteriol. 178:1310-1319.
    • (1996) J. Bacteriol. , vol.178 , pp. 1310-1319
    • Milton, D.L.1    O'Toole, R.2    Hörstedt, P.3    Wolf, W.H.4
  • 34
    • 0023391199 scopus 로고
    • Activation of the plasma kallikrein-kinin system by Vibrio vulnificus protease
    • Miyoshi, N., et al. 1987. Activation of the plasma kallikrein-kinin system by Vibrio vulnificus protease. Infect. Immun. 55:1936-1939.
    • (1987) Infect. Immun. , vol.55 , pp. 1936-1939
    • Miyoshi, N.1
  • 35
    • 0033973889 scopus 로고    scopus 로고
    • Microbial metalloproteases and pathogenesis
    • Miyoshi, S., and S. Shinoda. 2000. Microbial metalloproteases and pathogenesis. Microbes Infect. 2:91-98.
    • (2000) Microbes Infect. , vol.2 , pp. 91-98
    • Miyoshi, S.1    Shinoda, S.2
  • 36
    • 0031741393 scopus 로고    scopus 로고
    • The type IV leader peptidase/N-methyltransferase of Vibrio vulnificus controls factors required for adherence to HEp-2 cells and virulence in ironoverloaded mice
    • Paranjpye, R. N., J. C. Lara, J. C. Pepe, C. M. Pepe, and M. S. Strom. 1998. The type IV leader peptidase/N-methyltransferase of Vibrio vulnificus controls factors required for adherence to HEp-2 cells and virulence in ironoverloaded mice. Infect. Immun. 16:5659-5668.
    • (1998) Infect. Immun. , vol.16 , pp. 5659-5668
    • Paranjpye, R.N.1    Lara, J.C.2    Pepe, J.C.3    Pepe, C.M.4    Strom, M.S.5
  • 37
    • 15544368041 scopus 로고    scopus 로고
    • A Vibrio vulnificus type IV pilin contributes to biofilm formation, adherence to epithelial cells, and virulence
    • Paranjpye, R. N., and M. S. Strom. 2005. A Vibrio vulnificus type IV pilin contributes to biofilm formation, adherence to epithelial cells, and virulence. Infect. Immun. 73:1411-1422.
    • (2005) Infect. Immun. , vol.73 , pp. 1411-1422
    • Paranjpye, R.N.1    Strom, M.S.2
  • 38
    • 46749083508 scopus 로고    scopus 로고
    • Two forms of Vibrio vulnificus metalloprotease VvpE are secreted via the type II general secretion system
    • Park, J., S. Y. Ryu, C. M. Kim, and S. H. Shin. 2008. Two forms of Vibrio vulnificus metalloprotease VvpE are secreted via the type II general secretion system. J. Microbiol. 46:338-343.
    • (2008) J. Microbiol. , vol.46 , pp. 338-343
    • Park, J.1    Ryu, S.Y.2    Kim, C.M.3    Shin, S.H.4
  • 39
    • 70350236752 scopus 로고    scopus 로고
    • Legionella pneumophila secretes an endoglucanase that belongs to the family-5 of glycosyl hydrolases and is dependent upon type II secretion
    • Pearce, M. M., and N. P. Cianciotto. 2009. Legionella pneumophila secretes an endoglucanase that belongs to the family-5 of glycosyl hydrolases and is dependent upon type II secretion. FEMS Microbiol. Lett. 300:256-264.
    • (2009) FEMS Microbiol. Lett. , vol.300 , pp. 256-264
    • Pearce, M.M.1    Cianciotto, N.P.2
  • 40
    • 74349129601 scopus 로고    scopus 로고
    • Two-step and one-step secretion mechanisms in Gram-negative bacteria: contrasting the type IV secretion system and the chaperone-usher pathway of pilus biogenesis
    • Rego, A. T., V. Chandran, and G. Waksman. 2010. Two-step and one-step secretion mechanisms in Gram-negative bacteria: contrasting the type IV secretion system and the chaperone-usher pathway of pilus biogenesis. Biochem. J. 425:475-488.
    • (2010) Biochem. J. , vol.425 , pp. 475-488
    • Rego, A.T.1    Chandran, V.2    Waksman, G.3
  • 41
    • 4744359746 scopus 로고
    • A study on the pathogenetic activity of protease and hemolysin produced by Vibrio vulnificus. I. Biological properties of the hemolysin produced by Vibrio vulnificus
    • Rhee, J. H., et al. 1994. A study on the pathogenetic activity of protease and hemolysin produced by Vibrio vulnificus. I. Biological properties of the hemolysin produced by Vibrio vulnificus. J. Kor. Soc. Microbiol. 29:381-398.
    • (1994) J. Kor. Soc. Microbiol. , vol.29 , pp. 381-398
    • Rhee, J.H.1
  • 42
    • 0141862137 scopus 로고    scopus 로고
    • Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholera
    • Robien, M. A., B. E. Krumm, M. Sandkvist, and W. G. J. Hol. 2003. Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholera. J. Mol. Biol. 333:657-674.
    • (2003) J. Mol. Biol. , vol.333 , pp. 657-674
    • Robien, M.A.1    Krumm, B.E.2    Sandkvist, M.3    Hol, W.G.J.4
  • 43
    • 33845928243 scopus 로고    scopus 로고
    • Transcriptional regulatory cascade for elastase production in Vibrio vulnificus: LuxO activates luxT expression and LuxT represses smcR expression
    • Roh, J. B., et al. 2006. Transcriptional regulatory cascade for elastase production in Vibrio vulnificus: LuxO activates luxT expression and LuxT represses smcR expression. J. Biol. Chem. 281:34775-34784.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34775-34784
    • Roh, J.B.1
  • 44
    • 0033646651 scopus 로고    scopus 로고
    • Bacterial lipases from Pseudomonas: regulation of gene expression and mechanisms of secretion
    • Rosenau, F., and K.-E. Jaeger. 2000. Bacterial lipases from Pseudomonas: regulation of gene expression and mechanisms of secretion. Biochimie 82:1023-1032.
    • (2000) Biochimie , vol.82 , pp. 1023-1032
    • Rosenau, F.1    Jaeger, K.-E.2
  • 45
    • 38949201066 scopus 로고    scopus 로고
    • The type II secretion system of Legionella pneumophila elaborates two aminopeptidases, as well as a metalloprotease that contributes to differential infection among protozoan hosts
    • Rossier, O., J. Dao, and N. P. Cianciotto. 2008. The type II secretion system of Legionella pneumophila elaborates two aminopeptidases, as well as a metalloprotease that contributes to differential infection among protozoan hosts. Appl. Environ. Microbiol. 74:753-761.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 753-761
    • Rossier, O.1    Dao, J.2    Cianciotto, N.P.3
  • 46
    • 0346251028 scopus 로고    scopus 로고
    • Legionella pneumophila type II protein secretion promotes virulence in the A/J. mouse model of Legionnaires' disease pneumonia
    • Rossier, O., S. R. Starkenburg, and N. P. Cianciotto. 2004. Legionella pneumophila type II protein secretion promotes virulence in the A/J. mouse model of Legionnaires' disease pneumonia. Infect. Immun. 72:310-321.
    • (2004) Infect. Immun. , vol.72 , pp. 310-321
    • Rossier, O.1    Starkenburg, S.R.2    Cianciotto, N.P.3
  • 47
    • 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 , pp. 271-283
    • Sandkvist, M.1
  • 48
    • 0030785514 scopus 로고    scopus 로고
    • General secretion pathway (eps) genes required for toxin secretion and outer membrane biogenesis in Vibrio cholerae
    • Sandkvist, M., et al. 1997. General secretion pathway (eps) genes required for toxin secretion and outer membrane biogenesis in Vibrio cholerae . J. Bacteriol. 179:6994-7003.
    • (1997) J. Bacteriol. , vol.179 , pp. 6994-7003
    • Sandkvist, M.1
  • 49
    • 0034118185 scopus 로고    scopus 로고
    • Metalloprotease is not essential for Vibrio vulnificus virulence in mice
    • Shao, C. P., and L. I. Hor. 2000. Metalloprotease is not essential for Vibrio vulnificus virulence in mice. Infect. Immun. 68:3569-3573.
    • (2000) Infect. Immun. , vol.68 , pp. 3569-3573
    • Shao, C.P.1    Hor, L.I.2
  • 50
    • 47549086918 scopus 로고    scopus 로고
    • Direct involvement of type II secretion system in extracellular translocation of Shewanella oneidensis outer membrane cytochrome MtrC and Omc A.
    • Shi, L., et al. 2008. Direct involvement of type II secretion system in extracellular translocation of Shewanella oneidensis outer membrane cytochrome MtrC and OmcA. J. Bacteriol. 190:5512-5516.
    • (2008) J. Bacteriol. , vol.190 , pp. 5512-5516
    • Shi, L.1
  • 52
    • 68949151888 scopus 로고    scopus 로고
    • Cell envelope perturbation induces oxidative stress and changes in iron homeostasis in Vibrio cholerae
    • Sikora, A. E., S. Beyhan, M. Bagdasarian, F. H. Yildiz, and M. Sandkvist. 2009. Cell envelope perturbation induces oxidative stress and changes in iron homeostasis in Vibrio cholerae. J. Bacteriol. 191:5398-5408.
    • (2009) J. Bacteriol. , vol.191 , pp. 5398-5408
    • Sikora, A.E.1    Beyhan, S.2    Bagdasarian, M.3    Yildiz, F.H.4    Sandkvist, M.5
  • 53
    • 36749049160 scopus 로고    scopus 로고
    • Compromised outer membrane integrity in Vibrio cholerae type II secretion mutants
    • Sikora, A. E., S. R. Lybarger, and M. Sandkvist. 2007. Compromised outer membrane integrity in Vibrio cholerae type II secretion mutants. J. Bacteriol. 189:8484-8495.
    • (2007) J. Bacteriol. , vol.189 , pp. 8484-8495
    • Sikora, A.E.1    Lybarger, S.R.2    Sandkvist, M.3
  • 54
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria. Biotechnology 1:784-791.
    • (1983) Biotechnology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 55
    • 50949090202 scopus 로고    scopus 로고
    • Importance of type II secretion system for Legionella pneumophila survival in tap water and amoebae at low temperature
    • Soderberg, M. A., J. Dao, S. Starkenburg, and N. P. Cianciotto. 2008. Importance of type II secretion system for Legionella pneumophila survival in tap water and amoebae at low temperature. Appl. Environ. Microbiol. 74:5583-5588.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 5583-5588
    • Soderberg, M.A.1    Dao, J.2    Starkenburg, S.3    Cianciotto, N.P.4
  • 56
    • 0037076418 scopus 로고    scopus 로고
    • Identification of a protein secretion pathway for the secretion of heat-labile enterotoxin by an enterotoxigenic strain of Escherichia coli
    • Tauschek, M., R. J. Gorrell, R. A. Strugnell, and R. M. Robins-Browne. 2002. Identification of a protein secretion pathway for the secretion of heat-labile enterotoxin by an enterotoxigenic strain of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 99:7066-7071.
    • (2002) Proc. Natl. Acad. Sci. U.S. A. , vol.99 , pp. 7066-7071
    • Tauschek, M.1    Gorrell, R.J.2    Strugnell, R.A.3    Robins-Browne, R.M.4
  • 57
    • 34548479547 scopus 로고    scopus 로고
    • Vibrio vulnificus damages macrophages during the early phase of infection
    • Tsuchiya, T., et al. 2007. Vibrio vulnificus damages macrophages during the early phase of infection. Infect. Immun. 75:4592-4596.
    • (2007) Infect. Immun. , vol.75 , pp. 4592-4596
    • Tsuchiya, T.1
  • 58
    • 0035803406 scopus 로고    scopus 로고
    • Involvement of the twin-arginine translocation system in protein secretion via the type II pathway
    • Voulhoux, R., et al. 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 , pp. 6735-6741
    • Voulhoux, R.1
  • 59
    • 43049165306 scopus 로고    scopus 로고
    • Variation of extracellular proteases produced by Vibrio vulnificus clinical isolates: genetic diversity of the metalloprotease gene (vvp), and serine protease secretion by vvp-negative strains
    • Wang, J., et al. 2008. Variation of extracellular proteases produced by Vibrio vulnificus clinical isolates: genetic diversity of the metalloprotease gene (vvp), and serine protease secretion by vvp-negative strains. Microb. Pathog. 44:494-500.
    • (2008) Microb. Pathog. , vol.44 , pp. 494-500
    • Wang, J.1
  • 60
    • 0026034195 scopus 로고
    • The extracellular cytolysin of Vibrio vulnificus: inactivation and relationship to virulence in mice
    • Wright, A. C., and J. G. Morris, Jr. 1991. The extracellular cytolysin of Vibrio vulnificus: inactivation and relationship to virulence in mice. Infect. Immun. 59:192-197.
    • (1991) Infect. Immun. , vol.59 , pp. 192-197
    • Wright, A.C.1    Morris Jr., J.G.2
  • 62
    • 0026762504 scopus 로고
    • osmY, a new hyperosmotically inducible gene, encodes a periplasmic protein in Escherichia coli
    • Yim, H. H., and M. Villarejo. 1992. osmY, a new hyperosmotically inducible gene, encodes a periplasmic protein in Escherichia coli. J. Bacteriol. 174:3637-3644.
    • (1992) J. Bacteriol. , vol.174 , pp. 3637-3644
    • Yim, H.H.1    Villarejo, M.2
  • 63
    • 34249025819 scopus 로고    scopus 로고
    • Membrane cholesterol is required for activity of Vibrio vulnificus cytolysin
    • Yu, H. N., et al. 2007. Membrane cholesterol is required for activity of Vibrio vulnificus cytolysin. Arch. Microbiol. 187:467-473.
    • (2007) Arch. Microbiol. , vol.187 , pp. 467-473
    • Yu, H.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.