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Volumn 9, Issue 9, 2014, Pages

Outer membrane vesicles mediate transport of biologically active Vibrio cholerae cytolysin (VCC) from V. cholerae strains

Author keywords

[No Author keywords available]

Indexed keywords

CYTOLYSIN; BACTERIAL PROTEIN; CYTOTOXIN; PORE FORMING CYTOTOXIC PROTEIN; RECOMBINANT PROTEIN; VIRULENCE FACTOR;

EID: 84907099587     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0106731     Document Type: Article
Times cited : (58)

References (70)
  • 1
    • 84907101495 scopus 로고    scopus 로고
    • June
    • o107 (Cholera). (http://www.who.int/mediacentre/factsheets/fs107/en/).
    • (2010) o107 (Cholera)
    • WHO1
  • 3
    • 0031792685 scopus 로고    scopus 로고
    • Epidemiology, genetics, and ecology of toxigenic Vibrio cholerae
    • Faruque SM, Albert MJ, Mekalanos JJ (1998) Epidemiology, genetics, and ecology of toxigenic Vibrio cholerae. Microbiol Mol Biol Rev 62: 1301-1314.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1301-1314
    • Faruque, S.M.1    Albert, M.J.2    Mekalanos, J.J.3
  • 4
    • 0033821209 scopus 로고    scopus 로고
    • Characterization of Vibrio cholerae O1 antigen as the bacteriophage K139 receptor and identification of IS1004 insertions aborting O1 antigen biosynthesis
    • Nesper J, Kapfhammer D, Klose KE, Merkert H, Reidl J (2000) Characterization of Vibrio cholerae O1 antigen as the bacteriophage K139 receptor and identification of IS1004 insertions aborting O1 antigen biosynthesis. J Bacteriol 182: 5097-5104.
    • (2000) J Bacteriol , vol.182 , pp. 5097-5104
    • Nesper, J.1    Kapfhammer, D.2    Klose, K.E.3    Merkert, H.4    Reidl, J.5
  • 5
    • 0036117898 scopus 로고    scopus 로고
    • Comparative and genetic analyses of the putative Vibrio cholerae lipopolysaccharide core oligosaccharide biosynthesis (wav) gene cluster
    • Nesper J, Kraiss A, Schild S, Blass J, Klose KE, et al. (2002) Comparative and genetic analyses of the putative Vibrio cholerae lipopolysaccharide core oligosaccharide biosynthesis (wav) gene cluster. Infect Immun 70: 2419-2433.
    • (2002) Infect Immun , vol.70 , pp. 2419-2433
    • Nesper, J.1    Kraiss, A.2    Schild, S.3    Blass, J.4    Klose, K.E.5
  • 6
    • 0036721177 scopus 로고    scopus 로고
    • Occurrence of antibiotic resistance gene cassettes aac(69)-Ib, dfrA5, dfrA12, and ereA2 in class I integrons in non-O1, non-O139 Vibrio cholerae strains in India
    • Thungapathra M, Amita, Sinha KK, Chaudhuri SR, Garg P, et al. (2002) Occurrence of antibiotic resistance gene cassettes aac(69)-Ib, dfrA5, dfrA12, and ereA2 in class I integrons in non-O1, non-O139 Vibrio cholerae strains in India. Antimicrob Agents Chemother 46: 2948-2955.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 2948-2955
    • Thungapathra, M.1    Amita2    Sinha, K.K.3    Chaudhuri, S.R.4    Garg, P.5
  • 7
    • 0028911379 scopus 로고
    • New variant of Vibrio cholerae O1 from clinical isolates in Amazonia
    • Coelho A, Andrade JR, Vicente AC, Salles CA (1995) New variant of Vibrio cholerae O1 from clinical isolates in Amazonia. J Clin Microbiol 33: 114-118.
    • (1995) J Clin Microbiol , vol.33 , pp. 114-118
    • Coelho, A.1    Andrade, J.R.2    Vicente, A.C.3    Salles, C.A.4
  • 8
    • 0029866356 scopus 로고    scopus 로고
    • Nontoxigenic Vibrio cholerae 01 serotype Inaba biotype El Tor associated with a cluster of cases of cholera in southern India
    • Saha PK, Koley H, Mukhopadhyay AK, Bhattacharya SK, Nair GB, et al. (1996) Nontoxigenic Vibrio cholerae 01 serotype Inaba biotype El Tor associated with a cluster of cases of cholera in southern India. J Clin Microbiol 34: 1114-1117.
    • (1996) J Clin Microbiol , vol.34 , pp. 1114-1117
    • Saha, P.K.1    Koley, H.2    Mukhopadhyay, A.K.3    Bhattacharya, S.K.4    Nair, G.B.5
  • 9
    • 84873049877 scopus 로고    scopus 로고
    • Novel cholix toxin variants, ADP-ribosylating toxins in Vibrio cholerae non-O1/non-O139 strains, and their pathogenicity
    • Awasthi SP, Asakura M, Chowdhury N, Neogi SB, Hinenoya A, et al. (2013) Novel cholix toxin variants, ADP-ribosylating toxins in Vibrio cholerae non-O1/non-O139 strains, and their pathogenicity. Infection and immunity 81: 531-541.
    • (2013) Infection and Immunity , vol.81 , pp. 531-541
    • Awasthi, S.P.1    Asakura, M.2    Chowdhury, N.3    Neogi, S.B.4    Hinenoya, A.5
  • 11
    • 84874434890 scopus 로고    scopus 로고
    • Molecular analysis of non-O1/non-O139 Vibrio cholerae isolated from hospitalised patients in China
    • Luo Y, Ye J, Jin D, Ding G, Zhang Z, et al. (2013) Molecular analysis of non-O1/non-O139 Vibrio cholerae isolated from hospitalised patients in China. BMC microbiology 13: 52.
    • (2013) BMC Microbiology , vol.13 , pp. 52
    • Luo, Y.1    Ye, J.2    Jin, D.3    Ding, G.4    Zhang, Z.5
  • 12
    • 34848912537 scopus 로고    scopus 로고
    • Hemolysin and the multifunctional autoprocessing RTX toxin are virulence factors during intestinal infection of mice with Vibrio cholerae El Tor O1 strains
    • Olivier V, Haines GK, 3rd, Tan Y, Satchell KJ (2007) Hemolysin and the multifunctional autoprocessing RTX toxin are virulence factors during intestinal infection of mice with Vibrio cholerae El Tor O1 strains. Infect Immun 75: 5035-5042.
    • (2007) Infect Immun , vol.75 , pp. 5035-5042
    • Olivier, V.1    Haines, G.K.2    Tan, Y.3    Satchell, K.J.4
  • 13
  • 14
    • 37349018983 scopus 로고    scopus 로고
    • Vibrio cholerae cytolysin is essential for high enterotoxicity and apoptosis induction produced by a cholera toxin gene-negative V. cholerae non-O1, non-O139 strain
    • Saka HA, Bidinost C, Sola C, Carranza P, Collino C, et al. (2008) Vibrio cholerae cytolysin is essential for high enterotoxicity and apoptosis induction produced by a cholera toxin gene-negative V. cholerae non-O1, non-O139 strain. Microb Pathog 44: 118-128.
    • (2008) Microb Pathog , vol.44 , pp. 118-128
    • Saka, H.A.1    Bidinost, C.2    Sola, C.3    Carranza, P.4    Collino, C.5
  • 15
    • 0024044243 scopus 로고
    • Extracellular proteins of Vibrio cholerae: Nucleotide sequence of the structural gene (hlyA) for the haemolysin of the haemolytic El Tor strain 017 and characterization of the hlyA mutation in the non-haemolytic classical strain 569B
    • Alm RA, Stroeher UH, Manning PA (1988) Extracellular proteins of Vibrio cholerae: nucleotide sequence of the structural gene (hlyA) for the haemolysin of the haemolytic El Tor strain 017 and characterization of the hlyA mutation in the non-haemolytic classical strain 569B. Mol Microbiol 2: 481-488.
    • (1988) Mol Microbiol , vol.2 , pp. 481-488
    • Alm, R.A.1    Stroeher, U.H.2    Manning, P.A.3
  • 16
    • 0025609753 scopus 로고
    • Two-step processing for activation of the cytolysin/hemolysin of Vibrio cholerae O1 biotype El Tor: Nucleotide sequence of the structural gene (hlyA) and characterization of the processed products
    • Yamamoto K, Ichinose Y, Shinagawa H, Makino K, Nakata A, et al. (1990) Two-step processing for activation of the cytolysin/hemolysin of Vibrio cholerae O1 biotype El Tor: nucleotide sequence of the structural gene (hlyA) and characterization of the processed products. Infect Immun 58: 4106-4116.
    • (1990) Infect Immun , vol.58 , pp. 4106-4116
    • Yamamoto, K.1    Ichinose, Y.2    Shinagawa, H.3    Makino, K.4    Nakata, A.5
  • 17
    • 0031024004 scopus 로고    scopus 로고
    • Intramolecular chaperone activity of the pro-region of Vibrio cholerae El Tor cytolysin
    • Nagamune K, Yamamoto K, Honda T (1997) Intramolecular chaperone activity of the pro-region of Vibrio cholerae El Tor cytolysin. J Biol Chem 272: 1338-1343.
    • (1997) J Biol Chem , vol.272 , pp. 1338-1343
    • Nagamune, K.1    Yamamoto, K.2    Honda, T.3
  • 18
    • 0033556418 scopus 로고    scopus 로고
    • Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane
    • Zitzer A, Zitzer O, Bhakdi S, Palmer M (1999) Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane. J Biol Chem 274: 1375-1380.
    • (1999) J Biol Chem , vol.274 , pp. 1375-1380
    • Zitzer, A.1    Zitzer, O.2    Bhakdi, S.3    Palmer, M.4
  • 19
    • 33947223487 scopus 로고    scopus 로고
    • Pore formation by Vibrio cholerae cytolysin requires cholesterol in both monolayers of the target membrane
    • Krasilnikov OV, Merzlyak PG, Lima VL, Zitzer AO, Valeva A, et al. (2007) Pore formation by Vibrio cholerae cytolysin requires cholesterol in both monolayers of the target membrane. Biochimie 89: 271-277.
    • (2007) Biochimie , vol.89 , pp. 271-277
    • Krasilnikov, O.V.1    Merzlyak, P.G.2    Lima, V.L.3    Zitzer, A.O.4    Valeva, A.5
  • 20
    • 0036313062 scopus 로고    scopus 로고
    • The Vibrio cholerae haemolysin anion channel is required for cell vacuolation and death
    • Moschioni M, Tombola F, de Bernard M, Coelho A, Zitzer A, et al. (2002) The Vibrio cholerae haemolysin anion channel is required for cell vacuolation and death. Cell Microbiol 4: 397-409.
    • (2002) Cell Microbiol , vol.4 , pp. 397-409
    • Moschioni, M.1    Tombola, F.2    De Bernard, M.3    Coelho, A.4    Zitzer, A.5
  • 21
    • 29944444756 scopus 로고    scopus 로고
    • A molecular model of the Vibrio cholerae cytolysin transmembrane pore
    • Pantano S, Montecucco C (2006) A molecular model of the Vibrio cholerae cytolysin transmembrane pore. Toxicon 47: 35-40.
    • (2006) Toxicon , vol.47 , pp. 35-40
    • Pantano, S.1    Montecucco, C.2
  • 22
    • 33846936157 scopus 로고    scopus 로고
    • Protective role of autophagy against Vibrio cholerae cytolysin, a pore-forming toxin from V. cholerae
    • Gutierrez MG, Saka HA, Chinen I, Zoppino FC, Yoshimori T, et al. (2007) Protective role of autophagy against Vibrio cholerae cytolysin, a pore-forming toxin from V. cholerae. Proc Natl Acad Sci U S A 104: 1829-1834.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1829-1834
    • Gutierrez, M.G.1    Saka, H.A.2    Chinen, I.3    Zoppino, F.C.4    Yoshimori, T.5
  • 23
    • 27644493346 scopus 로고    scopus 로고
    • The pleiotropic role of autophagy: From protein metabolism to bactericide
    • Mizushima N (2005) The pleiotropic role of autophagy: from protein metabolism to bactericide. Cell death and differentiation 12 Suppl 2: 1535-1541.
    • (2005) Cell Death and Differentiation , vol.12 , pp. 1535-1541
    • Mizushima, N.1
  • 24
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, et al. (2000) LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. The EMBO journal 19: 5720-5728.
    • (2000) The EMBO Journal , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5
  • 25
    • 0029085873 scopus 로고
    • The release of outer membrane vesicles from the strains of enterotoxigenic Escherichia coli
    • Wai SN, Takade A, Amako K (1995) The release of outer membrane vesicles from the strains of enterotoxigenic Escherichia coli. Microbiol Immunol 39: 451-456.
    • (1995) Microbiol Immunol , vol.39 , pp. 451-456
    • Wai, S.N.1    Takade, A.2    Amako, K.3
  • 26
    • 10744220460 scopus 로고    scopus 로고
    • Vesicle-mediated export and assembly of pore-forming oligomers of the enterobacterial ClyA cytotoxin
    • Wai SN, Lindmark B, Soderblom T, Takade A, Westermark M, et al. (2003) Vesicle-mediated export and assembly of pore-forming oligomers of the enterobacterial ClyA cytotoxin. Cell 115: 25-35.
    • (2003) Cell , vol.115 , pp. 25-35
    • Wai, S.N.1    Lindmark, B.2    Soderblom, T.3    Takade, A.4    Westermark, M.5
  • 27
    • 10644226878 scopus 로고    scopus 로고
    • Enterotoxigenic Escherichia coli vesicles target toxin delivery into mammalian cells
    • Kesty NC, Mason KM, Reedy M, Miller SE, Kuehn MJ (2004) Enterotoxigenic Escherichia coli vesicles target toxin delivery into mammalian cells. EMBO J 23: 4538-4549.
    • (2004) EMBO J , vol.23 , pp. 4538-4549
    • Kesty, N.C.1    Mason, K.M.2    Reedy, M.3    Miller, S.E.4    Kuehn, M.J.5
  • 28
    • 70449381000 scopus 로고    scopus 로고
    • Outer membrane vesicle-mediated release of cytolethal distending toxin (CDT) from Campylobacter jejuni
    • Lindmark B, Rompikuntal PK, Vaitkevicius K, Song T, Mizunoe Y, et al. (2009) Outer membrane vesicle-mediated release of cytolethal distending toxin (CDT) from Campylobacter jejuni. BMC Microbiol 9: 220.
    • (2009) BMC Microbiol , vol.9 , pp. 220
    • Lindmark, B.1    Rompikuntal, P.K.2    Vaitkevicius, K.3    Song, T.4    Mizunoe, Y.5
  • 29
    • 84863411717 scopus 로고    scopus 로고
    • Perinuclear localization of internalized outer membrane vesicles carrying active cytolethal distending toxin from Aggregatibacter actinomycetemcomitans
    • Rompikuntal PK, Thay B, Khan MK, Alanko J, Penttinen AM, et al. (2012) Perinuclear localization of internalized outer membrane vesicles carrying active cytolethal distending toxin from Aggregatibacter actinomycetemcomitans. Infection and immunity 80: 31-42.
    • (2012) Infection and Immunity , vol.80 , pp. 31-42
    • Rompikuntal, P.K.1    Thay, B.2    Khan, M.K.3    Alanko, J.4    Penttinen, A.M.5
  • 30
    • 0036157198 scopus 로고    scopus 로고
    • Outer membrane-like vesicles secreted by Actinobacillus actinomycetemcomitans are enriched in leukotoxin
    • Kato S, Kowashi Y, Demuth DR (2002) Outer membrane-like vesicles secreted by Actinobacillus actinomycetemcomitans are enriched in leukotoxin. Microb Pathog 32: 1-13.
    • (2002) Microb Pathog , vol.32 , pp. 1-13
    • Kato, S.1    Kowashi, Y.2    Demuth, D.R.3
  • 31
    • 25844501470 scopus 로고    scopus 로고
    • Free-soluble and outer membrane vesicle-associated VacA from Helicobacter pylori: Two forms of release, a different activity
    • Ricci V, Chiozzi V, Necchi V, Oldani A, Romano M, et al. (2005) Free-soluble and outer membrane vesicle-associated VacA from Helicobacter pylori: Two forms of release, a different activity. Biochem Biophys Res Commun 337: 173-178.
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 173-178
    • Ricci, V.1    Chiozzi, V.2    Necchi, V.3    Oldani, A.4    Romano, M.5
  • 32
    • 70649091281 scopus 로고    scopus 로고
    • Vibrio cholerae cytolysin causes an inflammatory response in human intestinal epithelial cells that is modulated by the PrtV protease
    • Ou G, Rompikuntal PK, Bitar A, Lindmark B, Vaitkevicius K, et al. (2009) Vibrio cholerae cytolysin causes an inflammatory response in human intestinal epithelial cells that is modulated by the PrtV protease. PLoS One 4: e7806.
    • (2009) PLoS One , vol.4 , pp. e7806
    • Ou, G.1    Rompikuntal, P.K.2    Bitar, A.3    Lindmark, B.4    Vaitkevicius, K.5
  • 33
    • 33745154808 scopus 로고    scopus 로고
    • A Vibrio cholerae protease needed for killing of Caenorhabditis elegans has a role in protection from natural predator grazing
    • Vaitkevicius K, Lindmark B, Ou G, Song T, Toma C, et al. (2006) A Vibrio cholerae protease needed for killing of Caenorhabditis elegans has a role in protection from natural predator grazing. Proc Natl Acad Sci U S A 103: 9280-9285.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 9280-9285
    • Vaitkevicius, K.1    Lindmark, B.2    Ou, G.3    Song, T.4    Toma, C.5
  • 35
    • 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
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A 76: 4350-4354.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 38
    • 33645070224 scopus 로고    scopus 로고
    • Release of the type I secreted alpha-haemolysin via outer membrane vesicles from Escherichia coli
    • Balsalobre C, Silvan JM, Berglund S, Mizunoe Y, Uhlin BE, et al. (2006) Release of the type I secreted alpha-haemolysin via outer membrane vesicles from Escherichia coli. Mol Microbiol 59: 99-112.
    • (2006) Mol Microbiol , vol.59 , pp. 99-112
    • Balsalobre, C.1    Silvan, J.M.2    Berglund, S.3    Mizunoe, Y.4    Uhlin, B.E.5
  • 39
    • 0034085052 scopus 로고    scopus 로고
    • Yersinia enterocolitica TyeA, an intracellular regulator of the type III machinery, is required for specific targeting of YopE, YopH, YopM, and YopN into the cytosol of eukaryotic cells
    • Cheng LW, Schneewind O (2000) Yersinia enterocolitica TyeA, an intracellular regulator of the type III machinery, is required for specific targeting of YopE, YopH, YopM, and YopN into the cytosol of eukaryotic cells. J Bacteriol 182: 3183-3190.
    • (2000) J Bacteriol , vol.182 , pp. 3183-3190
    • Cheng, L.W.1    Schneewind, O.2
  • 40
    • 0031707437 scopus 로고    scopus 로고
    • Vibrio cholerae O1 strain TSI-4 produces the exopolysaccharide materials that determine colony morphology, stress resistance, and biofilm formation
    • Wai SN, Mizunoe Y, Takade A, Kawabata SI, Yoshida SI (1998) Vibrio cholerae O1 strain TSI-4 produces the exopolysaccharide materials that determine colony morphology, stress resistance, and biofilm formation. Appl Environ Microbiol 64: 3648-3655.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3648-3655
    • Wai, S.N.1    Mizunoe, Y.2    Takade, A.3    Kawabata, S.I.4    Yoshida, S.I.5
  • 42
    • 0025871608 scopus 로고
    • Amino-terminal domain of the El Tor haemolysin of Vibrio cholerae O1 is expressed in classical strains and is cytotoxic
    • Alm RA, Mayrhofer G, Kotlarski I, Manning PA (1991) Amino-terminal domain of the El Tor haemolysin of Vibrio cholerae O1 is expressed in classical strains and is cytotoxic. Vaccine 9: 588-594.
    • (1991) Vaccine , vol.9 , pp. 588-594
    • Alm, R.A.1    Mayrhofer, G.2    Kotlarski, I.3    Manning, P.A.4
  • 43
    • 0034682744 scopus 로고    scopus 로고
    • Nucleoid proteins stimulate stringently controlled bacterial promoters: A link between the cAMP-CRP and the (p)ppGpp regulons in Escherichia coli
    • Johansson J, Balsalobre C, Wang SY, Urbonaviciene J, Jin DJ, et al. (2000) Nucleoid proteins stimulate stringently controlled bacterial promoters: a link between the cAMP-CRP and the (p)ppGpp regulons in Escherichia coli. Cell 102: 475-485.
    • (2000) Cell , vol.102 , pp. 475-485
    • Johansson, J.1    Balsalobre, C.2    Wang, S.Y.3    Urbonaviciene, J.4    Jin, D.J.5
  • 44
    • 0033031407 scopus 로고    scopus 로고
    • Molecular analysis of the cytolytic protein ClyA (SheA) from Escherichia coli
    • Oscarsson J, Mizunoe Y, Li L, Lai XH, Wieslander A, et al. (1999) Molecular analysis of the cytolytic protein ClyA (SheA) from Escherichia coli. Mol Microbiol 32: 1226-1238.
    • (1999) Mol Microbiol , vol.32 , pp. 1226-1238
    • Oscarsson, J.1    Mizunoe, Y.2    Li, L.3    Lai, X.H.4    Wieslander, A.5
  • 45
    • 0021021637 scopus 로고
    • Cholera toxin genes: Nucleotide sequence, deletion analysis and vaccine development
    • Mekalanos JJ, Swartz DJ, Pearson GD, Harford N, Groyne F, et al. (1983) Cholera toxin genes: nucleotide sequence, deletion analysis and vaccine development. Nature 306: 551-557.
    • (1983) Nature , vol.306 , pp. 551-557
    • Mekalanos, J.J.1    Swartz, D.J.2    Pearson, G.D.3    Harford, N.4    Groyne, F.5
  • 46
    • 0014139523 scopus 로고
    • Electron microscopic observations on the excretion of cell-wall material by Vibrio cholerae
    • Chatterjee SN, Das J (1967) Electron microscopic observations on the excretion of cell-wall material by Vibrio cholerae. J Gen Microbiol 49: 1-11.
    • (1967) J Gen Microbiol , vol.49 , pp. 1-11
    • Chatterjee, S.N.1    Das, J.2
  • 47
    • 0027223653 scopus 로고
    • Release of the outer membrane vesicles from Vibrio cholerae and Vibrio parahaemolyticus
    • Kondo K, Takade A, Amako K (1993) Release of the outer membrane vesicles from Vibrio cholerae and Vibrio parahaemolyticus. Microbiol Immunol 37: 149-152.
    • (1993) Microbiol Immunol , vol.37 , pp. 149-152
    • Kondo, K.1    Takade, A.2    Amako, K.3
  • 48
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B, Kroemer G (2008) Autophagy in the pathogenesis of disease. Cell 132: 27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 49
    • 79551553480 scopus 로고    scopus 로고
    • Dissecting the dynamic turnover of GFP-LC3 in the autolysosome
    • Ni HM, Bockus A, Wozniak AL, Jones K, Weinman S, et al. (2011) Dissecting the dynamic turnover of GFP-LC3 in the autolysosome. Autophagy 7: 188-204.
    • (2011) Autophagy , vol.7 , pp. 188-204
    • Ni, H.M.1    Bockus, A.2    Wozniak, A.L.3    Jones, K.4    Weinman, S.5
  • 50
    • 68849110746 scopus 로고    scopus 로고
    • Pore formation by Vibrio cholerae cytolysin follows the same archetypical mode as beta-barrel toxins from gram-positive organisms
    • Lohner S, Walev I, Boukhallouk F, Palmer M, Bhakdi S, et al. (2009) Pore formation by Vibrio cholerae cytolysin follows the same archetypical mode as beta-barrel toxins from gram-positive organisms. FASEB J 23: 2521-2528.
    • (2009) FASEB J , vol.23 , pp. 2521-2528
    • Lohner, S.1    Walev, I.2    Boukhallouk, F.3    Palmer, M.4    Bhakdi, S.5
  • 52
    • 84894144847 scopus 로고    scopus 로고
    • The beta-prism lectin domain of Vibrio cholerae hemolysin promotes self-assembly of the beta-pore-forming toxin by a carbohydrate-independent mechanism
    • Ganguly S, Mukherjee A, Mazumdar B, Ghosh AN, Banerjee KK (2014) The beta-Prism Lectin Domain of Vibrio cholerae Hemolysin Promotes Self-assembly of the beta-Pore-forming Toxin by a Carbohydrate-independent Mechanism. J Biol Chem 289: 4001-4008.
    • (2014) J Biol Chem , vol.289 , pp. 4001-4008
    • Ganguly, S.1    Mukherjee, A.2    Mazumdar, B.3    Ghosh, A.N.4    Banerjee, K.K.5
  • 53
    • 0028533504 scopus 로고
    • Heterologous protein secretion and the versatile Escherichia coli haemolysin translocator
    • Blight MA, Holland IB (1994) Heterologous protein secretion and the versatile Escherichia coli haemolysin translocator. Trends Biotechnol 12: 450-455.
    • (1994) Trends Biotechnol , vol.12 , pp. 450-455
    • Blight, M.A.1    Holland, I.B.2
  • 54
    • 79955765269 scopus 로고    scopus 로고
    • Proteomic analysis of the Vibrio cholerae type II secretome reveals new proteins, including three related serine proteases
    • Sikora AE, Zielke RA, Lawrence DA, Andrews PC, Sandkvist M (2011) Proteomic analysis of the Vibrio cholerae type II secretome reveals new proteins, including three related serine proteases. The Journal of biological chemistry 286: 16555-16566.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 16555-16566
    • Sikora, A.E.1    Zielke, R.A.2    Lawrence, D.A.3    Andrews, P.C.4    Sandkvist, M.5
  • 55
    • 0032839616 scopus 로고    scopus 로고
    • Structures of gram-negative cell walls and their derived membrane vesicles
    • Beveridge TJ (1999) Structures of gram-negative cell walls and their derived membrane vesicles. Journal of bacteriology 181: 4725-4733.
    • (1999) Journal of Bacteriology , vol.181 , pp. 4725-4733
    • Beveridge, T.J.1
  • 56
    • 0029009438 scopus 로고
    • Virulence factors are released from Pseudomonas aeruginosa in association with membrane vesicles during normal growth and exposure to gentamicin: A novel mechanism of enzyme secretion
    • Kadurugamuwa JL, Beveridge TJ (1995) Virulence factors are released from Pseudomonas aeruginosa in association with membrane vesicles during normal growth and exposure to gentamicin: a novel mechanism of enzyme secretion. Journal of bacteriology 177: 3998-4008.
    • (1995) Journal of Bacteriology , vol.177 , pp. 3998-4008
    • Kadurugamuwa, J.L.1    Beveridge, T.J.2
  • 57
    • 0034724910 scopus 로고    scopus 로고
    • Enterotoxigenic Escherichia coli secretes active heat-labile enterotoxin via outer membrane vesicles
    • Horstman AL, Kuehn MJ (2000) Enterotoxigenic Escherichia coli secretes active heat-labile enterotoxin via outer membrane vesicles. J Biol Chem 275: 12489-12496.
    • (2000) J Biol Chem , vol.275 , pp. 12489-12496
    • Horstman, A.L.1    Kuehn, M.J.2
  • 58
    • 42949174067 scopus 로고    scopus 로고
    • Proteomic characterization of the whole secretome of Legionella pneumophila and functional analysis of outer membrane vesicles
    • Galka F, Wai SN, Kusch H, Engelmann S, Hecker M, et al. (2008) Proteomic characterization of the whole secretome of Legionella pneumophila and functional analysis of outer membrane vesicles. Infect Immun 76: 1825-1836.
    • (2008) Infect Immun , vol.76 , pp. 1825-1836
    • Galka, F.1    Wai, S.N.2    Kusch, H.3    Engelmann, S.4    Hecker, M.5
  • 59
    • 0030976392 scopus 로고    scopus 로고
    • Pleiotropic effects of a mutation in rfaC on Escherichia coli hemolysin
    • Bauer ME, Welch RA (1997) Pleiotropic effects of a mutation in rfaC on Escherichia coli hemolysin. Infection and immunity 65: 2218-2224.
    • (1997) Infection and Immunity , vol.65 , pp. 2218-2224
    • Bauer, M.E.1    Welch, R.A.2
  • 60
    • 0344404206 scopus 로고    scopus 로고
    • Reversible denaturation, self-aggregation, and membrane activity of Escherichia coli alpha-hemolysin, a protein stable in 6 M urea
    • Soloaga A, Ramirez JM, Goni FM (1998) Reversible denaturation, self-aggregation, and membrane activity of Escherichia coli alpha-hemolysin, a protein stable in 6 M urea. Biochemistry 37: 6387-6393.
    • (1998) Biochemistry , vol.37 , pp. 6387-6393
    • Soloaga, A.1    Ramirez, J.M.2    Goni, F.M.3
  • 61
    • 0033972526 scopus 로고    scopus 로고
    • Conformational studies of Actinobacillus actinomycetemcomitans leukotoxin: Partial denaturation enhances toxicity
    • Lear JD, Karakelian D, Furblur U, Lally ET, Tanaka JC (2000) Conformational studies of Actinobacillus actinomycetemcomitans leukotoxin: partial denaturation enhances toxicity. Biochimica et biophysica acta 1476: 350-362.
    • (2000) Biochimica et Biophysica Acta , vol.1476 , pp. 350-362
    • Lear, J.D.1    Karakelian, D.2    Furblur, U.3    Lally, E.T.4    Tanaka, J.C.5
  • 62
    • 84874841702 scopus 로고    scopus 로고
    • Autophagy and toxins: A matter of life or death
    • Mestre MB, Colombo MI (2013) Autophagy and toxins: a matter of life or death. Curr Mol Med 13: 241-251.
    • (2013) Curr Mol Med , vol.13 , pp. 241-251
    • Mestre, M.B.1    Colombo, M.I.2
  • 63
    • 84873741499 scopus 로고    scopus 로고
    • Autophagy and bacterial clearance: A not so clear picture
    • Mostowy S (2013) Autophagy and bacterial clearance: a not so clear picture. Cellular microbiology 15: 395-402.
    • (2013) Cellular Microbiology , vol.15 , pp. 395-402
    • Mostowy, S.1
  • 64
    • 0032799337 scopus 로고    scopus 로고
    • Clonal analysis of non-toxigenic Vibrio cholerae O1 associated with an outbreak of cholera
    • Pal A, Saha PK, Nair GB, Yamasaki S, Takeda T, et al. (1999) Clonal analysis of non-toxigenic Vibrio cholerae O1 associated with an outbreak of cholera. Indian J Med Res 109: 208-211.
    • (1999) Indian J Med Res , vol.109 , pp. 208-211
    • Pal, A.1    Saha, P.K.2    Nair, G.B.3    Yamasaki, S.4    Takeda, T.5
  • 65
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D (1983) Studies on transformation of Escherichia coli with plasmids. Journal of molecular biology 166: 557-580.
    • (1983) Journal of Molecular Biology , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 66
    • 0023892552 scopus 로고
    • A novel suicide vector and its use in construction of insertion mutations: Osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR
    • Miller VL MJ (1988) A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR. J Bacteriol 170: 2575-2583.
    • (1988) J Bacteriol , vol.170 , pp. 2575-2583
    • Miller, V.L.M.J.1
  • 67
    • 0018959055 scopus 로고
    • In vitro gene fusions that join an enzymatically active beta-galactosidase segment to amino-terminal fragments of exogenous proteins: Escherichia coli plasmid vectors for the detection and cloning of translational initiation signals
    • Casadaban MJ, Chou J, Cohen SN (1980) In vitro gene fusions that join an enzymatically active beta-galactosidase segment to amino-terminal fragments of exogenous proteins: Escherichia coli plasmid vectors for the detection and cloning of translational initiation signals. Journal of bacteriology 143: 971-980.
    • (1980) Journal of Bacteriology , vol.143 , pp. 971-980
    • Casadaban, M.J.1    Chou, J.2    Cohen, S.N.3
  • 68
    • 0026411101 scopus 로고
    • Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector
    • Donnenberg MS, Kaper JB (1991) Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector. Infect Immun 59: 4310-4317.
    • (1991) Infect Immun , vol.59 , pp. 4310-4317
    • Donnenberg, M.S.1    Kaper, J.B.2
  • 69
    • 0022870839 scopus 로고
    • Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector
    • Furste JP, Pansegrau W, Frank R, Blocker H, Scholz P, et al. (1986) Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48: 119-131.
    • (1986) Gene , vol.48 , pp. 119-131
    • Furste, J.P.1    Pansegrau, W.2    Frank, R.3    Blocker, H.4    Scholz, P.5
  • 70
    • 0017584161 scopus 로고
    • Construction and characterization of new cloning vehicles. II. A multipurpose cloning system
    • Bolivar F, Rodriguez RL, Greene PJ, Betlach MC, Heyneker HL, et al. (1977) Construction and characterization of new cloning vehicles. II. A multipurpose cloning system. Gene 2: 95-113.
    • (1977) Gene , vol.2 , pp. 95-113
    • Bolivar, F.1    Rodriguez, R.L.2    Greene, P.J.3    Betlach, M.C.4    Heyneker, H.L.5


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