메뉴 건너뛰기




Volumn 30, Issue 2-3, 1999, Pages 181-202

Secretion of virulence factors by Escherichia coli

Author keywords

E. coli; Secretion; Virulence factors

Indexed keywords

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0033091466     PISSN: 09284249     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (24)

References (122)
  • 1
    • 0030954704 scopus 로고    scopus 로고
    • Characterization of two virulence proteins secreted by rabbit enteropathogenic Escherichia coli, EspA and EspB, whose maximal expression is sensitive to host body temperature
    • Abe A., Kenny B., Stein M., Finlay B.B., Characterization of two virulence proteins secreted by rabbit enteropathogenic Escherichia coli, EspA and EspB, whose maximal expression is sensitive to host body temperature, Infect. Immun. 65 (1997) 3547-3555.
    • (1997) Infect. Immun. , vol.65 , pp. 3547-3555
    • Abe, A.1    Kenny, B.2    Stein, M.3    Finlay, B.B.4
  • 3
    • 0028883418 scopus 로고
    • Mutational analysis of the Yersinia enterocolitica virC operon: Characterization of yscE, F, G, I, J, K required for the Yop secretion and yscH encoding YopR
    • Allaoui A., Schulte R., Cornelis G.R., Mutational analysis of the Yersinia enterocolitica virC operon: characterization of yscE, F, G, I, J, K required for the Yop secretion and yscH encoding YopR, Mol. Microbiol. 18 (1995) 343-355.
    • (1995) Mol. Microbiol. , vol.18 , pp. 343-355
    • Allaoui, A.1    Schulte, R.2    Cornelis, G.R.3
  • 4
    • 0026609257 scopus 로고
    • Escherichia coli HlyT protein, a transcriptional activator of hemolysin synthesis and secretion, is encoded by rfaH (sfrB) locus required for expression of sex factor and lipopolysaccharide genes
    • Bailey M.J., Koronakis V., Schmoll T., Hughes C., Escherichia coli HlyT protein, a transcriptional activator of hemolysin synthesis and secretion, is encoded by rfaH (sfrB) locus required for expression of sex factor and lipopolysaccharide genes, Mol. Microbiol. 6 (1992) 1003-1012.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1003-1012
    • Bailey, M.J.1    Koronakis, V.2    Schmoll, T.3    Hughes, C.4
  • 5
    • 0026748890 scopus 로고
    • Enteroaggregative Escherichia coli secrete a heat-labile toxin antigenically related to E. coli hemolysin
    • Baldwin T.J., Knutton S., Sellers L., Hernandez H.A.M., Aitken A.A., Williams P.H., Enteroaggregative Escherichia coli secrete a heat-labile toxin antigenically related to E. coli hemolysin, Infect. Immun. 60 (1992) 2092-2095.
    • (1992) Infect. Immun. , vol.60 , pp. 2092-2095
    • Baldwin, T.J.1    Knutton, S.2    Sellers, L.3    Hernandez, H.A.M.4    Aitken, A.A.5    Williams, P.H.6
  • 6
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell J.C., McGovern K., Beckwith J., Identification of a protein required for disulfide bond formation in vivo, Cell 65 (1991) 581-589.
    • (1991) Cell , vol.65 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 7
    • 0027503249 scopus 로고
    • Purified E. coli preprotein translocase catalyzes multiple cycles of precursor protein translocation
    • Bassilana M., Wickner W., Purified E. coli preprotein translocase catalyzes multiple cycles of precursor protein translocation, Biochemistry 32 (1993) 2626-2630
    • (1993) Biochemistry , vol.32 , pp. 2626-2630
    • Bassilana, M.1    Wickner, W.2
  • 8
    • 0029671024 scopus 로고    scopus 로고
    • Characterization of an RTX toxin from enterohemorrhagic Escherichia coli O157H7
    • Bauer M.E., Welch R.A., Characterization of an RTX toxin from enterohemorrhagic Escherichia coli O157H7, Infect. Immun. 64 (1996) 167-175.
    • (1996) Infect. Immun. , vol.64 , pp. 167-175
    • Bauer, M.E.1    Welch, R.A.2
  • 9
    • 0031931629 scopus 로고    scopus 로고
    • Diffusely adhering Escherichia coli strains induce attaching and effacing phenotypes and secrete homologs of Esp proteins
    • Beinke C., Laminoacidsrman S., Wachter C., Karch H., Greune L., Schmidt M.A., Diffusely adhering Escherichia coli strains induce attaching and effacing phenotypes and secrete homologs of Esp proteins, Infect. Immun. 66 (1998) 528-539.
    • (1998) Infect. Immun. , vol.66 , pp. 528-539
    • Beinke, C.1    Laminoacidsrman, S.2    Wachter, C.3    Karch, H.4    Greune, L.5    Schmidt, M.A.6
  • 10
    • 0242478028 scopus 로고    scopus 로고
    • Protein secretion by Gram-negative bacterial ABC exporters - A review
    • Binet R., Letoffe S., Ghigo J.M., Delepaire P., Wandersman C., Protein secretion by Gram-negative bacterial ABC exporters - a review, Gene 192 (1997) 7-11.
    • (1997) Gene , vol.192 , pp. 7-11
    • Binet, R.1    Letoffe, S.2    Ghigo, J.M.3    Delepaire, P.4    Wandersman, C.5
  • 11
    • 0031865883 scopus 로고    scopus 로고
    • Evolution of enterohemorrhagic Escherichia coli hemolysin plasmids and the locus for enterocyte effacement in Shiga toxin-producing E. coli
    • Boerlin P., Chen S., Colbourne J.K., Johnson R., De Grandis S., Gyles C., Evolution of enterohemorrhagic Escherichia coli hemolysin plasmids and the locus for enterocyte effacement in Shiga toxin-producing E. coli., Infect. Immun. 66 (1998) 2553-2561.
    • (1998) Infect. Immun. , vol.66 , pp. 2553-2561
    • Boerlin, P.1    Chen, S.2    Colbourne, J.K.3    Johnson, R.4    De Grandis, S.5    Gyles, C.6
  • 12
    • 85087188871 scopus 로고    scopus 로고
    • Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y. enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the Yop B, D, N apparatus
    • Boland A., Sory M.-P., Iriate M., Kerbouch C., Wattiau P., Cornelis G.R., Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y. enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the Yop B, D, N apparatus, EMBO J. 15 (1996) 191-201.
    • (1996) EMBO J. , vol.15 , pp. 191-201
    • Boland, A.1    Sory, M.-P.2    Iriate, M.3    Kerbouch, C.4    Wattiau, P.5    Cornelis, G.R.6
  • 13
    • 0025230537 scopus 로고
    • Secretion and memebrane integration of a filamentous phage-encoded morphogenic protein
    • Brisette J.L., Russel M., Secretion and memebrane integration of a filamentous phage-encoded morphogenic protein, J. Mol. Biol. 211 (1990) 565-580.
    • (1990) J. Mol. Biol. , vol.211 , pp. 565-580
    • Brisette, J.L.1    Russel, M.2
  • 14
    • 0030917724 scopus 로고    scopus 로고
    • EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V
    • Brunder W., Schmidt H., Karch H., EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V, Mol. Microbiol. 24 (1997) 767-778.
    • (1997) Mol. Microbiol. , vol.24 , pp. 767-778
    • Brunder, W.1    Schmidt, H.2    Karch, H.3
  • 15
    • 0026654267 scopus 로고
    • Molecular characterization of an RTX toxin determinant from Actinobacillus suis
    • Burrows L.L., Lo R.Y.C., Molecular characterization of an RTX toxin determinant from Actinobacillus suis, Infect. Immun. 60 (1992) 2166-2173.
    • (1992) Infect. Immun. , vol.60 , pp. 2166-2173
    • Burrows, L.L.1    Lo, R.Y.C.2
  • 16
    • 0026349590 scopus 로고
    • The Actinobacillus pleuropneumoniae hemolysin determinant: Unlinked appCA and appBD loci flanked pseudogenes
    • Chang Y.-F., Young R., Struck D.K., The Actinobacillus pleuropneumoniae hemolysin determinant: unlinked appCA and appBD loci flanked pseudogenes, J. Bacteriol. 173 (1991) 5151-5158.
    • (1991) J. Bacteriol. , vol.173 , pp. 5151-5158
    • Chang, Y.-F.1    Young, R.2    Struck, D.K.3
  • 17
    • 0027285310 scopus 로고
    • Molecular characterization of a leukotoxin gene from Pasteurella haemolytica-like organism, encoding a new member of the RTX toxin family
    • Chang Y., Ma D., Shi J., Chengappa M.M., Molecular characterization of a leukotoxin gene from Pasteurella haemolytica-like organism, encoding a new member of the RTX toxin family, Infect. Immun. 61 (1993) 2089-2095.
    • (1993) Infect. Immun. , vol.61 , pp. 2089-2095
    • Chang, Y.1    Ma, D.2    Shi, J.3    Chengappa, M.M.4
  • 18
    • 0029830550 scopus 로고    scopus 로고
    • Competition between functional signal peptides demonstrates variation in affinity for secretion pathway
    • Chen H., Kim J., Kendall D.A., Competition between functional signal peptides demonstrates variation in affinity for secretion pathway, J. Bacteriol. 178 (1996) 6658-6664.
    • (1996) J. Bacteriol. , vol.178 , pp. 6658-6664
    • Chen, H.1    Kim, J.2    Kendall, D.A.3
  • 19
    • 0026816008 scopus 로고
    • Structural and functional relationships among the RTX toxin determinants of Gram-negative bacteria
    • Coote J.G., Structural and functional relationships among the RTX toxin determinants of Gram-negative bacteria, FEMS Microbiol. Rev. 88 (1992) 137-162.
    • (1992) FEMS Microbiol. Rev. , vol.88 , pp. 137-162
    • Coote, J.G.1
  • 20
    • 0002076570 scopus 로고
    • Yersiniae, finely tuned pathogens
    • Hormaeche C., Penn C.W., Smyth C.J. (Eds.), Society for General Microbiology Symposium, Cambridge University Press Ltd, Cambridge
    • Cornelis G.R, Yersiniae, finely tuned pathogens, in: Hormaeche C., Penn C.W., Smyth C.J. (Eds.), Molecular Biology of Bacterial Infection: Current Status and Future Perspectives, vol. 49, Society for General Microbiology Symposium, Cambridge University Press Ltd, Cambridge, 1992, pp. 231-265.
    • (1992) Molecular Biology of Bacterial Infection: Current Status and Future Perspectives , vol.49 , pp. 231-265
    • Cornelis, G.R.1
  • 21
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia yop virulon: A bacterial system to subvert eukaryotic cell
    • Cornelis G.R., Wolf-Watz H., The Yersinia yop virulon: a bacterial system to subvert eukaryotic cell, Mol. Microbiol. 23 (1997) 861-867.
    • (1997) Mol. Microbiol. , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 22
    • 0026343547 scopus 로고
    • Leader peptidase
    • Dalbey R.E., Leader peptidase, Mol. Microbiol. 5 (1991) 2855-2860.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2855-2860
    • Dalbey, R.E.1
  • 23
    • 0030799018 scopus 로고    scopus 로고
    • Charaterization of an exported protease from Shiga toxin-producing Escherichia coli
    • Djafari S., Ebel F., Deibel C., Krämer S., Hudel S., Chakraborty T., Charaterization of an exported protease from Shiga toxin-producing Escherichia coli, Mol. Microbiol. 25 (1997) 771-784.
    • (1997) Mol. Microbiol. , vol.25 , pp. 771-784
    • Djafari, S.1    Ebel, F.2    Deibel, C.3    Krämer, S.4    Hudel, S.5    Chakraborty, T.6
  • 24
    • 0026674948 scopus 로고
    • Enteropathogenic Escherichia coli
    • Donnenberg M.S., Kaper J.B., Enteropathogenic Escherichia coli, Infect. Immun. 60 (1992) 3953-3961.
    • (1992) Infect. Immun. , vol.60 , pp. 3953-3961
    • Donnenberg, M.S.1    Kaper, J.B.2
  • 25
    • 0026482190 scopus 로고
    • A plasmid-encoded type IV fimbrial gene of enteropathogenic Escherichia coli associated with localized adherence
    • Donnenberg M.S., Giron J.A., Nataro J.P., Kaper J.B., A plasmid-encoded type IV fimbrial gene of enteropathogenic Escherichia coli associated with localized adherence, Mol. Microbiol. 6 (1992) 3427-3437.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3427-3437
    • Donnenberg, M.S.1    Giron, J.A.2    Nataro, J.P.3    Kaper, J.B.4
  • 26
    • 0027250343 scopus 로고
    • A second chromosomal gene necessary for intimate attachment of enteropathogenic Escherichia coli to epithelial cells
    • Donnenberg M.S., Yu J., Kaper J.B., A second chromosomal gene necessary for intimate attachment of enteropathogenic Escherichia coli to epithelial cells, J. Bacteriol. 175 (1993) 4670-4680.
    • (1993) J. Bacteriol. , vol.175 , pp. 4670-4680
    • Donnenberg, M.S.1    Yu, J.2    Kaper, J.B.3
  • 27
    • 0028064967 scopus 로고
    • SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
    • Economou A., Wickner W., SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion, Cell 78 (1994) 835-843.
    • (1994) Cell , vol.78 , pp. 835-843
    • Economou, A.1    Wickner, W.2
  • 28
    • 0025034686 scopus 로고
    • 2+-binding protein that is exported without N-terminal cleavage and is homologous to hemolysin and related proteins
    • 2+-binding protein that is exported without N-terminal cleavage and is homologous to hemolysin and related proteins. EMBO J. 9 (1990) 349-354.
    • (1990) EMBO J. , vol.9 , pp. 349-354
    • Economou, A.1    Hamilton, W.D.O.2    Johnston, A.W.B.3    Downie, J.A.4
  • 30
    • 0000842940 scopus 로고    scopus 로고
    • What is a pathogen?
    • Falkow S., What is a pathogen?, ASM News 63 (1997) 359-365.
    • (1997) ASM News , vol.63 , pp. 359-365
    • Falkow, S.1
  • 31
    • 0022260426 scopus 로고
    • Nucleotide sequence of an Escherichia coli chromosomal hemolysin
    • Felmee T., Pellet S., Welch R.A., Nucleotide sequence of an Escherichia coli chromosomal hemolysin, J. Bacteriol. 163 (1985) 94-105.
    • (1985) J. Bacteriol. , vol.163 , pp. 94-105
    • Felmee, T.1    Pellet, S.2    Welch, R.A.3
  • 32
    • 0030790687 scopus 로고    scopus 로고
    • Common themes in microbial pathogenesis revisited
    • Finlay B.B., Falkow S., Common themes in microbial pathogenesis revisited, Microbiol. Mol. Biol. Rev. 61 (1997) 136-169.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 136-169
    • Finlay, B.B.1    Falkow, S.2
  • 33
    • 0026754089 scopus 로고
    • Cytoskeletal composition of attaching and effacing lesions associated with enteropatogenic Escherichia coli adherence to HeLa cells
    • Finlay B.B., Rosenshine I., Donnenberg M.S., Kaper J.B., Cytoskeletal composition of attaching and effacing lesions associated with enteropatogenic Escherichia coli adherence to HeLa cells, Infect. Immun. 60 (1992) 2541-2543.
    • (1992) Infect. Immun. , vol.60 , pp. 2541-2543
    • Finlay, B.B.1    Rosenshine, I.2    Donnenberg, M.S.3    Kaper, J.B.4
  • 34
    • 0029924909 scopus 로고    scopus 로고
    • The cryptic general secretory pathway (gsp) operon of Escherichia coli K-12 encodes functional proteins
    • Francetic O., Pugsley A.P., The cryptic general secretory pathway (gsp) operon of Escherichia coli K-12 encodes functional proteins, J. Bacteriol. 178 (1996) 3544-3549.
    • (1996) J. Bacteriol. , vol.178 , pp. 3544-3549
    • Francetic, O.1    Pugsley, A.P.2
  • 35
    • 0025895554 scopus 로고
    • Nucleotide sequence of the hemolysin I gene from Actinobacillus pleuropneumoniae
    • Frey J., Meier R., Gygi D., Nicolet J., Nucleotide sequence of the hemolysin I gene from Actinobacillus pleuropneumoniae, Infect. Immun. 59 (1991) 3026-3032.
    • (1991) Infect. Immun. , vol.59 , pp. 3026-3032
    • Frey, J.1    Meier, R.2    Gygi, D.3    Nicolet, J.4
  • 36
    • 0026575486 scopus 로고
    • Topological and functionnal studies on HlyB of Escherichia coli
    • Gentschev I., Goebel W., Topological and functionnal studies on HlyB of Escherichia coli, Mol. Gen. Genet. 232 (1992) 40-48.
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 40-48
    • Gentschev, I.1    Goebel, W.2
  • 37
    • 0026330896 scopus 로고
    • An inducible bundle-forming pilus of enteropathogenic Escherichia coli
    • Giron J.A., Ho A.S.Y., Schoonlik G.K., An inducible bundle-forming pilus of enteropathogenic Escherichia coli, Science 254 (1991) 710-713.
    • (1991) Science , vol.254 , pp. 710-713
    • Giron, J.A.1    Ho, A.S.Y.2    Schoonlik, G.K.3
  • 38
    • 0024195829 scopus 로고
    • Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-hemolysin bifunctional protein of Bordetella pertussis
    • Glaser P., Sakamoto H., Bellalou J., Ullmann A., Danchin A., Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-hemolysin bifunctional protein of Bordetella pertussis, EMBO J. 7 (1988) 3997-4004.
    • (1988) EMBO J. , vol.7 , pp. 3997-4004
    • Glaser, P.1    Sakamoto, H.2    Bellalou, J.3    Ullmann, A.4    Danchin, A.5
  • 39
    • 0030827039 scopus 로고    scopus 로고
    • Bovine attaching and effacing Escherichia coli possess a pathogenesis island related to the LEE of the human enteropathogenic E. coli strain E2348/69
    • Goffaux F., Mainil J., Pirson V., Charlier G., Pohl P., Jacquemin E., China B., Bovine attaching and effacing Escherichia coli possess a pathogenesis island related to the LEE of the human enteropathogenic E. coli strain E2348/69, FEMS Microbiol. Lett. 154 (1997), 415-421.
    • (1997) FEMS Microbiol. Lett. , vol.154 , pp. 415-421
    • Goffaux, F.1    Mainil, J.2    Pirson, V.3    Charlier, G.4    Pohl, P.5    Jacquemin, E.6    China, B.7
  • 40
    • 0028912808 scopus 로고
    • A plasmid-encoded regulatory region activates chromosomal eaeA expression in enteropathogenic Escherichia coli
    • Gomez-Duarte O.G., Kaper J.B., A plasmid-encoded regulatory region activates chromosomal eaeA expression in enteropathogenic Escherichia coli, Infect. Immun. 63 (1995) 1767-1776.
    • (1995) Infect. Immun. , vol.63 , pp. 1767-1776
    • Gomez-Duarte, O.G.1    Kaper, J.B.2
  • 41
    • 0001775904 scopus 로고
    • Escherichia coli enterotoxins
    • Gyles C.L. (Ed.), CAB International, Wallingford
    • Gyles C.L., Escherichia coli enterotoxins, in Gyles C.L. (Ed.), Escherichia coli in Domestic Animals and Humans, CAB International, Wallingford, 1994, pp. 337-364.
    • (1994) Escherichia Coli in Domestic Animals and Humans , pp. 337-364
    • Gyles, C.L.1
  • 42
    • 0020521025 scopus 로고
    • Cloned hemolysin genes from Escherichia coli that cause urinary tract infection determine different levels of toxicity in mice
    • Hacker J., Hughes C., Hof H., Goebel W., Cloned hemolysin genes from Escherichia coli that cause urinary tract infection determine different levels of toxicity in mice, Infect. Immun. 42 (1983) 57-63.
    • (1983) Infect. Immun. , vol.42 , pp. 57-63
    • Hacker, J.1    Hughes, C.2    Hof, H.3    Goebel, W.4
  • 43
    • 0021455107 scopus 로고
    • IgA protease of Neisseria gonorrhoeae: Isolation and characterisation of the gene and its intracellular product
    • Halter R., Pohlner J., Meyer T.F., IgA protease of Neisseria gonorrhoeae: isolation and characterisation of the gene and its intracellular product, EMBO J. 3 (1984) 1595-1601.
    • (1984) EMBO J. , vol.3 , pp. 1595-1601
    • Halter, R.1    Pohlner, J.2    Meyer, T.F.3
  • 44
    • 0025785244 scopus 로고
    • In vitro activation of Escherichia coli prohemolysin to the mature membrane-targeted toxin requires HlyC and a low molecular weight cytosolic polypeptide
    • Hardie K.R., Issartel J.P., Koronakis E., Hugnes C., Koronakis V., In vitro activation of Escherichia coli prohemolysin to the mature membrane-targeted toxin requires HlyC and a low molecular weight cytosolic polypeptide, Mol. Microbiol. 5 (1991) 1669-1679.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1669-1679
    • Hardie, K.R.1    Issartel, J.P.2    Koronakis, E.3    Hugnes, C.4    Koronakis, V.5
  • 45
    • 0025036708 scopus 로고
    • The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
    • Hartl F.U., Lecker S., Schibel E., Hendrik J.P., Wickner W., The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane, Cell 63 (1990) 269-279.
    • (1990) Cell , vol.63 , pp. 269-279
    • Hartl, F.U.1    Lecker, S.2    Schibel, E.3    Hendrik, J.P.4    Wickner, W.5
  • 46
    • 0024580287 scopus 로고
    • DNA sequence of Pasteurella haemolytica leukotoxin gene cluster
    • Highlander S.K., Chidambaram M., Engler M.J., Weinstock G.M., DNA sequence of Pasteurella haemolytica leukotoxin gene cluster, DNA 8 (1989) 15-28.
    • (1989) DNA , vol.8 , pp. 15-28
    • Highlander, S.K.1    Chidambaram, M.2    Engler, M.J.3    Weinstock, G.M.4
  • 47
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plant
    • Hueck C.J., Type III protein secretion systems in bacterial pathogens of animals and plant, Microbiol. Mol. Biol. Rev. 62 (1998) 379-433.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 48
    • 0026739811 scopus 로고
    • Activation of Escherichia coli prohemolysin to the membrane targeted toxin by HlyC-directed ACP-dependent fatty acylation
    • Hughes C., Issartel J.P., Hardie K., Stanley P., Koronakis E., Koronakis V., Activation of Escherichia coli prohemolysin to the membrane targeted toxin by HlyC-directed ACP-dependent fatty acylation, FEMS Microbiol. Immunol. 105 (1992) 37-44.
    • (1992) FEMS Microbiol. Immunol. , vol.105 , pp. 37-44
    • Hughes, C.1    Issartel, J.P.2    Hardie, K.3    Stanley, P.4    Koronakis, E.5    Koronakis, V.6
  • 49
    • 0032055051 scopus 로고    scopus 로고
    • Tye A, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors
    • Iriarte M., Sory M.-P., Boland A., Boyd A.P., Mills S.D., Lambermont I., Cornelis G., Tye A, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors, EMBO J. 17 (1998) 1907-1918.
    • (1998) EMBO J. , vol.17 , pp. 1907-1918
    • Iriarte, M.1    Sory, M.-P.2    Boland, A.3    Boyd, A.P.4    Mills, S.D.5    Lambermont, I.6    Cornelis, G.7
  • 50
    • 0026432638 scopus 로고
    • Activation of Escherichia coli prohemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation
    • Issartell J.P., Koronakis V., Hughes C., Activation of Escherichia coli prohemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation, Nature 351 (1991) 159-161.
    • (1991) Nature , vol.351 , pp. 159-161
    • Issartell, J.P.1    Koronakis, V.2    Hughes, C.3
  • 51
    • 0029859537 scopus 로고    scopus 로고
    • Secretion of extracellular proteins by enterohemorrhagic Escherichia coli via a putative type III secretion system
    • Jarvis K.G., Kaper J.B., Secretion of extracellular proteins by enterohemorrhagic Escherichia coli via a putative type III secretion system, Infect. Immun. 64 (1996) 4826-4829.
    • (1996) Infect. Immun. , vol.64 , pp. 4826-4829
    • Jarvis, K.G.1    Kaper, J.B.2
  • 52
    • 0029099975 scopus 로고
    • Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation
    • Jarvis K.G., Giron J.A., Jerse A.E., McDaniel T.K., Donnenberg M.S., Kaper J.B., Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation, Proc. Natl. Acad. Sci. USA 92 (1995) 7996-8000.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7996-8000
    • Jarvis, K.G.1    Giron, J.A.2    Jerse, A.E.3    McDaniel, T.K.4    Donnenberg, M.S.5    Kaper, J.B.6
  • 53
    • 0027393014 scopus 로고
    • The Seca and SecY subuntis of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids
    • Joly J.C., Wickner W., The SecA and SecY subuntis of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids, EMBO J. 12 (1993) 255-263.
    • (1993) EMBO J. , vol.12 , pp. 255-263
    • Joly, J.C.1    Wickner, W.2
  • 54
    • 0031836721 scopus 로고    scopus 로고
    • EPEC delivers the goods
    • Kaper J.B., EPEC delivers the goods, Trends Microbiol. 6 (1998) 169-172.
    • (1998) Trends Microbiol. , vol.6 , pp. 169-172
    • Kaper, J.B.1
  • 55
    • 0023176586 scopus 로고
    • Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70
    • Katsuragi N., Takizawa N., Murooka Y., Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70, J. Bacteriol. 169 (1987) 2301-2306.
    • (1987) J. Bacteriol. , vol.169 , pp. 2301-2306
    • Katsuragi, N.1    Takizawa, N.2    Murooka, Y.3
  • 56
    • 0025944413 scopus 로고
    • Processing of TCP pilin by TepJ typifies a common step intrinsic to a newly recognized pathway for extracellular protein secretion by gram-negative bacteria
    • Kaufman M.R., Seyer J.M., Taylor R.K., Processing of TCP pilin by TepJ typifies a common step intrinsic to a newly recognized pathway for extracellular protein secretion by gram-negative bacteria, Genes Dev. 5 (1991) 1834-1846.
    • (1991) Genes Dev. , vol.5 , pp. 1834-1846
    • Kaufman, M.R.1    Seyer, J.M.2    Taylor, R.K.3
  • 57
    • 0029155828 scopus 로고
    • Protein secretion by enteropathogenic Escherichia coli is essential for transducing signals to epithelial cells
    • Kenny B., Finlay B.B., Protein secretion by enteropathogenic Escherichia coli is essential for transducing signals to epithelial cells, Proc. Natl. Acad. Sci. USA 92 (1995) 7991-7995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7991-7995
    • Kenny, B.1    Finlay, B.B.2
  • 58
    • 0029972684 scopus 로고    scopus 로고
    • EspA, a protein secreted by enteropathogenic Escherichia coli is required to induces in epithelial epithelial cells
    • Kenny B., Lai L.-C., Finlay B.B., Donnenberg M.S., EspA, a protein secreted by enteropathogenic Escherichia coli is required to induces in epithelial epithelial cells, Mol. Microbiol. 20 (1996) 313-323.
    • (1996) Mol. Microbiol. , vol.20 , pp. 313-323
    • Kenny, B.1    Lai, L.-C.2    Finlay, B.B.3    Donnenberg, M.S.4
  • 59
    • 0030701868 scopus 로고    scopus 로고
    • Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
    • Kenny B., DeVinney R., Stein M., Reinscheid D.J., Frey E.A., Finlay B.B., Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells, Cell 91 (1997) 511-520.
    • (1997) Cell , vol.91 , pp. 511-520
    • Kenny, B.1    DeVinney, R.2    Stein, M.3    Reinscheid, D.J.4    Frey, E.A.5    Finlay, B.B.6
  • 60
    • 0031893538 scopus 로고    scopus 로고
    • Identification of a sequence motif that confers SecB dependence on a SecB-independent secretory protein in vivo
    • Kim J., Kendall D.A., Identification of a sequence motif that confers SecB dependence on a SecB-independent secretory protein in vivo, J. Bacteriol. 180 (1998) 1396-1401.
    • (1998) J. Bacteriol. , vol.180 , pp. 1396-1401
    • Kim, J.1    Kendall, D.A.2
  • 61
    • 0026511122 scopus 로고
    • Selective extracellular release of cholera toxin B subunit by Escherichia coli: Dissection of Neisseria IgAb-mediated outer membrane transport
    • Klauser T., Pohlner J., Meyer T.F., Selective extracellular release of cholera toxin B subunit by Escherichia coli: dissection of Neisseria IgAb-mediated outer membrane transport, EMBO J. 11 (1992) 2327-2335.
    • (1992) EMBO J. , vol.11 , pp. 2327-2335
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 62
    • 0002610259 scopus 로고
    • Attaching and effacing E. coli
    • Gyles C.L. (Ed.), CAB International, Wallingford, UK
    • Knutton S., Attaching and effacing E. coli, in: Gyles C.L. (Ed.), Escherichia coli in Domestic Animals and Humans, CAB International, Wallingford, UK, 1994, pp. 567-591.
    • (1994) Escherichia Coli in Domestic Animals and Humans , pp. 567-591
    • Knutton, S.1
  • 63
    • 0032522344 scopus 로고    scopus 로고
    • A novel EspA-associated surface organelle of enteropathogenic Escherichia coli; involved in protein translocation into epithelial cells
    • Knutton S., Rosenshine I., Pallen M.J., Nisan I., Neves B.C., Bain C., Wolff C., Dougan G., Frankel G., A novel EspA-associated surface organelle of enteropathogenic Escherichia coli; involved in protein translocation into epithelial cells, EMBO J. 17 (1998) 2166-2176.
    • (1998) EMBO J. , vol.17 , pp. 2166-2176
    • Knutton, S.1    Rosenshine, I.2    Pallen, M.J.3    Nisan, I.4    Neves, B.C.5    Bain, C.6    Wolff, C.7    Dougan, G.8    Frankel, G.9
  • 64
    • 0024588797 scopus 로고
    • Cloning and expression of the leukotoxin gene from Actinobacillus actinomycetemcomitans
    • Kolodrubetz D., Dailey T., Ebersole J., Kraig E., Cloning and expression of the leukotoxin gene from Actinobacillus actinomycetemcomitans, Infect. Immun. 57 (1989) 1465-1469.
    • (1989) Infect. Immun. , vol.57 , pp. 1465-1469
    • Kolodrubetz, D.1    Dailey, T.2    Ebersole, J.3    Kraig, E.4
  • 65
    • 0029744875 scopus 로고    scopus 로고
    • Synthesis, maturation and export of Escherichia coli hemolysin
    • Koronakis V., Hughes C., Synthesis, maturation and export of Escherichia coli hemolysin, Med. Microbiol. Immunol. 185 (1996) 65-71.
    • (1996) Med. Microbiol. Immunol. , vol.185 , pp. 65-71
    • Koronakis, V.1    Hughes, C.2
  • 66
    • 0023238044 scopus 로고
    • The secreted hemolysins of Proteus mirabilis, Proleus vulgaris and Morganella morganii are genetically related to each other and to the alpha-hemolysin of Escherichia coli
    • Koronakis V., Cross M., Senior B., Koronakis E., Hughes C., The secreted hemolysins of Proteus mirabilis, Proleus vulgaris and Morganella morganii are genetically related to each other and to the alpha-hemolysin of Escherichia coli, J. Bacteriol. 169 (1987) 1509-1515.
    • (1987) J. Bacteriol. , vol.169 , pp. 1509-1515
    • Koronakis, V.1    Cross, M.2    Senior, B.3    Koronakis, E.4    Hughes, C.5
  • 67
    • 0024386073 scopus 로고
    • Isolation and analysis of the C-terminal signal directing export of Escherichia coli hemolysin protein across both bacterial membranes
    • Koronakis V., Koronakis E., Hughes C., Isolation and analysis of the C-terminal signal directing export of Escherichia coli hemolysin protein across both bacterial membranes, EMBO J. 8 (1989) 595-605.
    • (1989) EMBO J. , vol.8 , pp. 595-605
    • Koronakis, V.1    Koronakis, E.2    Hughes, C.3
  • 68
    • 0025989941 scopus 로고
    • Energetically distinct early and late stages of HlyB/HlyD-dependent secretion across both Escherichia coli membranes
    • Koronakis V., Hughes C., Koronakis E., Energetically distinct early and late stages of HlyB/HlyD-dependent secretion across both Escherichia coli membranes, EMBO J. 10 (1991) 3263-3272.
    • (1991) EMBO J. , vol.10 , pp. 3263-3272
    • Koronakis, V.1    Hughes, C.2    Koronakis, E.3
  • 69
    • 0027190678 scopus 로고
    • ATPase activity and ATP/ADP-induced conformational change in the soluble domain of the bacterial protein translocator HlyB
    • Koronakis V., Hughes C., Koronakis E., ATPase activity and ATP/ADP-induced conformational change in the soluble domain of the bacterial protein translocator HlyB, Mol. Microbiol. 8 (1993) 1163-1175.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1163-1175
    • Koronakis, V.1    Hughes, C.2    Koronakis, E.3
  • 70
    • 0031014882 scopus 로고    scopus 로고
    • Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals
    • Koronakis V., Li J., Koronakis E., Stauffer K., Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals, Mol. Microbiol. 23 (1997) 617-626.
    • (1997) Mol. Microbiol. , vol.23 , pp. 617-626
    • Koronakis, V.1    Li, J.2    Koronakis, E.3    Stauffer, K.4
  • 71
    • 0031009562 scopus 로고    scopus 로고
    • A third secreted protein that is encoded by the enteropathogenic Escherichia coli pathogenicity island is required for transduction of signals and for attaching and effacing activities in host cells
    • Lai L.C., Wainwright L.A., Stone K.D., Donnenberg M.S., A third secreted protein that is encoded by the enteropathogenic Escherichia coli pathogenicity island is required for transduction of signals and for attaching and effacing activities in host cells, Infect. Immun. 65 (1997) 2211-2217.
    • (1997) Infect. Immun. , vol.65 , pp. 2211-2217
    • Lai, L.C.1    Wainwright, L.A.2    Stone, K.D.3    Donnenberg, M.S.4
  • 72
    • 0030998981 scopus 로고    scopus 로고
    • Type III secretion systems: Machines to deliver bacterial protein into eukaryotic cells?
    • Lee C.A., Type III secretion systems: machines to deliver bacterial protein into eukaryotic cells?. Trends Microbiol. 5 (1997) 148-156.
    • (1997) Trends Microbiol. , vol.5 , pp. 148-156
    • Lee, C.A.1
  • 73
    • 0029935766 scopus 로고    scopus 로고
    • RfaH enhances elongation of Escherichia coli hlyCABD mRNA
    • Leeds J.A., Welch R.A., RfaH enhances elongation of Escherichia coli hlyCABD mRNA. J. Bacteriol. 178 (1996) 1850-1857.
    • (1996) J. Bacteriol. , vol.178 , pp. 1850-1857
    • Leeds, J.A.1    Welch, R.A.2
  • 74
    • 0030996159 scopus 로고    scopus 로고
    • Enhancing transcription through the Escherichia coli hemolysin operon, hlyCADB: RfaH and Upstream JUMP-start DNA sequences function together via a postinitiation mechanism
    • Leeds J.A., Welch R.A., Enhancing transcription through the Escherichia coli hemolysin operon, hlyCADB: RfaH and Upstream JUMP-start DNA sequences function together via a postinitiation mechanism, J. Bacteriol. 179 (1997) 3519-3527.
    • (1997) J. Bacteriol. , vol.179 , pp. 3519-3527
    • Leeds, J.A.1    Welch, R.A.2
  • 75
    • 0031931363 scopus 로고    scopus 로고
    • EspB and EspD require a specific chaperone for proper secretion from enteropathogenic Escherichia coli
    • Leslie A., Wainwright L.A., Kaper J.B., EspB and EspD require a specific chaperone for proper secretion from enteropathogenic Escherichia coli, Mol. Microbiol. 27 (1998) 1247-1260.
    • (1998) Mol. Microbiol. , vol.27 , pp. 1247-1260
    • Leslie, A.1    Wainwright, L.A.2    Kaper, J.B.3
  • 76
    • 0025257358 scopus 로고
    • Protease secretion by Erwinia chrysanthemi: The specific secretion functions are analogous to those of Escherichia coli alpha-hemolysin
    • Letoffe S., Delepaire P., Wandersman C., Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli alpha-hemolysin, EMBO J. 9 (1990) 1375-1382.
    • (1990) EMBO J. , vol.9 , pp. 1375-1382
    • Letoffe, S.1    Delepaire, P.2    Wandersman, C.3
  • 77
    • 0025825577 scopus 로고
    • Cloning and expression in Escherichia coli of the Serratia marcescens metalloprotease gene: Secretion of the proteaminoacidsse from E. coli in the presence of the Erwinia chrysantemi protease B
    • Letoffe S., Delepaire P., Wandersman C., Cloning and expression in Escherichia coli of the Serratia marcescens metalloprotease gene: secretion of the proteaminoacidsse from E. coli in the presence of the Erwinia chrysantemi protease B, J. Bacteriol. 174 (1991) 2160-2166.
    • (1991) J. Bacteriol. , vol.174 , pp. 2160-2166
    • Letoffe, S.1    Delepaire, P.2    Wandersman, C.3
  • 78
    • 0023158054 scopus 로고
    • Mutations affecting activity and transport of hemolysin in Escherichia coli
    • Ludwig A., Vogel M., Goebel W., Mutations affecting activity and transport of hemolysin in Escherichia coli, Mol. Gen. Genet. 206 (1987) 238-245.
    • (1987) Mol. Gen. Genet. , vol.206 , pp. 238-245
    • Ludwig, A.1    Vogel, M.2    Goebel, W.3
  • 79
    • 0028945803 scopus 로고
    • A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens
    • McDaniel T.K., Jarvis G., Donnenberg M.S., Kaper J.B., A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens, Proc. Natl. Acad. Sci. USA 92 (1995) 1664-1668.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1664-1668
    • McDaniel, T.K.1    Jarvis, G.2    Donnenberg, M.S.3    Kaper, J.B.4
  • 80
    • 0026735914 scopus 로고
    • Molecular cloning and expression of ptxA, the gene encoding the 120-kilodalton cytotoxin of Actinobacillus pleuropneumoniae serotype 2
    • Mcdonald J, Rycroft A.N., Molecular cloning and expression of ptxA, the gene encoding the 120-kilodalton cytotoxin of Actinobacillus pleuropneumoniae serotype 2, Infect. Immun. 60 (1987) 2726-2732.
    • (1987) Infect. Immun. , vol.60 , pp. 2726-2732
    • Mcdonald, J.1    Rycroft, A.N.2
  • 81
    • 0031711022 scopus 로고    scopus 로고
    • A novel proline-rich protein, EspF, is secreted from enteropathogenic Escherichia coli via the type III export pathway
    • McNamara B.P., Donnenberg M.S., A novel proline-rich protein, EspF, is secreted from enteropathogenic Escherichia coli via the type III export pathway, FEMS Microbiol. Lett. 166 (1998) 71-78.
    • (1998) FEMS Microbiol. Lett. , vol.166 , pp. 71-78
    • McNamara, B.P.1    Donnenberg, M.S.2
  • 82
    • 0026065361 scopus 로고
    • Secretion of hybrid proteins by the Yersinia Yop export system
    • Michiels T., Cornelis G.R., Secretion of hybrid proteins by the Yersinia Yop export system, J. Bacteriol. 173 (1991) 1677-1685.
    • (1991) J. Bacteriol. , vol.173 , pp. 1677-1685
    • Michiels, T.1    Cornelis, G.R.2
  • 84
    • 0020508377 scopus 로고
    • Attaching and effacing activities of rabbit and human enteropathogenic Escherichia coli in pig and rabbit intestines
    • Moon H.W., Whipp S.C., Argenzio R.A., Levine M.M., Giannela R.A., Attaching and effacing activities of rabbit and human enteropathogenic Escherichia coli in pig and rabbit intestines, Infect. Immun. 41 (1983) 1340-1351.
    • (1983) Infect. Immun. , vol.41 , pp. 1340-1351
    • Moon, H.W.1    Whipp, S.C.2    Argenzio, R.A.3    Levine, M.M.4    Giannela, R.A.5
  • 85
    • 0026063242 scopus 로고
    • Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II)
    • Munoa F.J., Miller K.W., Beers R., Graham M., Wu H.C., Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II), J. Biol. Chem. 266 (1991) 17667-17672.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17667-17672
    • Munoa, F.J.1    Miller, K.W.2    Beers, R.3    Graham, M.4    Wu, H.C.5
  • 87
  • 88
    • 0030063067 scopus 로고    scopus 로고
    • Supression of transcription polarity in the Escherichia coli hemolysin operon by short upstream element shared by polysaccharide and DNA transfer determinants
    • Nielo J.M., Bailey M.J.A., Hughes C., Koronakis V., Supression of transcription polarity in the Escherichia coli hemolysin operon by short upstream element shared by polysaccharide and DNA transfer determinants, Mol. Microbiol. 19 (1996) 705-713.
    • (1996) Mol. Microbiol. , vol.19 , pp. 705-713
    • Nielo, J.M.1    Bailey, M.J.A.2    Hughes, C.3    Koronakis, V.4
  • 90
    • 0026345424 scopus 로고
    • Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader peptidase
    • Nunn D., Lory S., Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader peptidase, Proc Natl. Acad. Sci. USA 88 (1991) 3281-3285.
    • (1991) Proc Natl. Acad. Sci. USA , vol.88 , pp. 3281-3285
    • Nunn, D.1    Lory, S.2
  • 92
    • 0027455603 scopus 로고
    • SecA protein: Autoregulated ATPase catalyzing preprotein insertion and translocation across the Escherichia coli inner membrane
    • Oliver D.B., SecA protein: autoregulated ATPase catalyzing preprotein insertion and translocation across the Escherichia coli inner membrane, Mol. Microbiol. 7 (1993) 159-165
    • (1993) Mol. Microbiol. , vol.7 , pp. 159-165
    • Oliver, D.B.1
  • 93
    • 0027422306 scopus 로고
    • Genes required for extracellular secretion of enterotoxin are clustered in Vibrio cholerae
    • Overbye L.J., Sandkvist M., Bagdasarian M., Genes required for extracellular secretion of enterotoxin are clustered in Vibrio cholerae, Gene 132 (1993) 101-106
    • (1993) Gene , vol.132 , pp. 101-106
    • Overbye, L.J.1    Sandkvist, M.2    Bagdasarian, M.3
  • 97
    • 0023128808 scopus 로고
    • Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease
    • Pohlner J., Halter R., Beyreuther K., Meyer T.F., Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease, Nature (London) 325 (1987) 458-462.
    • (1987) Nature (London) , vol.325 , pp. 458-462
    • Pohlner, J.1    Halter, R.2    Beyreuther, K.3    Meyer, T.F.4
  • 98
    • 0345414802 scopus 로고
    • Protein secretion across the outer membrane of Gram-negative bacteria
    • Das R.C., Robbins P.W. (Eds.), Academic Press Inc., San Diego, CA
    • Pugsley A.P., Protein secretion across the outer membrane of Gram-negative bacteria, in: Das R.C., Robbins P.W. (Eds.), Protein transfer and organelle biogenesis, Academic Press Inc., San Diego, CA, 1988, pp. 607-652.
    • (1988) Protein Transfer and Organelle Biogenesis , pp. 607-652
    • Pugsley, A.P.1
  • 99
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley A.P., The complete general secretory pathway in gram-negative bacteria, Microbiol. Rev. 57 (1993) 50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 100
    • 0027982566 scopus 로고
    • Phage assembly: A paradigm for bacterial virulence factor export?
    • Russel M., Phage assembly: a paradigm for bacterial virulence factor export?, Science 265 (1994) 612-614.
    • (1994) Science , vol.265 , pp. 612-614
    • Russel, M.1
  • 101
    • 0027506049 scopus 로고
    • A protein required for secretion of cholera toxin through the outer membrane of Vibrio cholerae
    • Sandkvist M., Morales V., Bagdasarian M., A protein required for secretion of cholera toxin through the outer membrane of Vibrio cholerae, Gene 123 (1993) 81-86.
    • (1993) Gene , vol.123 , pp. 81-86
    • Sandkvist, M.1    Morales, V.2    Bagdasarian, M.3
  • 103
    • 0025694884 scopus 로고
    • Genetic analysis of protein export in Escherichia coli
    • Schatz P.J., Beckwith J., Genetic analysis of protein export in Escherichia coli, Annu. Rev. Genet. 24 (1990) 215-248.
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 215-248
    • Schatz, P.J.1    Beckwith, J.2
  • 104
    • 0028258720 scopus 로고
    • The large-sized plasmids of enterohemorrhagic Escherichia coli 0157 strains encode hemolysins which are presumably members of the E. coli alpha-hemolysin family
    • Schmidt H., Karch H., Beutin L., The large-sized plasmids of enterohemorrhagic Escherichia coli 0157 strains encode hemolysins which are presumably members of the E. coli alpha-hemolysin family, FEMS Microbiol. Lett. 117 (1994) 189-196.
    • (1994) FEMS Microbiol. Lett. , vol.117 , pp. 189-196
    • Schmidt, H.1    Karch, H.2    Beutin, L.3
  • 105
    • 0030993971 scopus 로고    scopus 로고
    • A gene cluster closely realted to type II secretion pathway operons of Gram-negative bacteria is located on the large plasmid of enterohemorrhagic Escherichia coli 0157 strains
    • Schmidt H., Henkel B., Karch H., A gene cluster closely realted to type II secretion pathway operons of Gram-negative bacteria is located on the large plasmid of enterohemorrhagic Escherichia coli 0157 strains, FEMS Microbiol. Lett. 148 (1997) 265-272.
    • (1997) FEMS Microbiol. Lett. , vol.148 , pp. 265-272
    • Schmidt, H.1    Henkel, B.2    Karch, H.3
  • 107
    • 0028105015 scopus 로고
    • Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells
    • Sory M.-P., Cornelis G.R., Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells, Mol. Microbiol. 14 (1994) 583-594.
    • (1994) Mol. Microbiol. , vol.14 , pp. 583-594
    • Sory, M.-P.1    Cornelis, G.R.2
  • 108
    • 0029608720 scopus 로고
    • Identifiaction of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using cyaA gene fusion approach
    • Sory M.-P., Boland A., Lambermont I., Cornelis G.R., Identifiaction of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using cyaA gene fusion approach, Proc. Natl. Acad. Sci. USA 92 (1995) 11998-12002.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11998-12002
    • Sory, M.-P.1    Boland, A.2    Lambermont, I.3    Cornelis, G.R.4
  • 109
    • 0026458260 scopus 로고
    • Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin
    • Spangler B.D., Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin, Microbiol. Rev. 56 (1992) 622-647.
    • (1992) Microbiol. Rev. , vol.56 , pp. 622-647
    • Spangler, B.D.1
  • 110
    • 0028567924 scopus 로고
    • Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin
    • Stanley P., Packman L.C., Koronakis V., Hardie K., Hughes C., Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin, Science 266 (1994) 1992-1996.
    • (1994) Science , vol.266 , pp. 1992-1996
    • Stanley, P.1    Packman, L.C.2    Koronakis, V.3    Hardie, K.4    Hughes, C.5
  • 111
    • 0029989067 scopus 로고    scopus 로고
    • Independent interaction of the acyltransferase HlyC with two maturation domains of the Escherichia coli toxin HlyA
    • Stanley P., Koronakis V., Hughes C., Independent interaction of the acyltransferase HlyC with two maturation domains of the Escherichia coli toxin HlyA, Mol. Microbiol. 20 (1996) 813-822.
    • (1996) Mol. Microbiol. , vol.20 , pp. 813-822
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 112
    • 0031596205 scopus 로고    scopus 로고
    • Acylation of Escherichia coli hemolysin: A unique protein lipidation mechanism underlying toxin function
    • Stanley P., Koronakis V., Hughes C., Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function, Microbiol. Rev. 62 (1998) 309-333.
    • (1998) Microbiol. Rev. , vol.62 , pp. 309-333
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 113
    • 0029961503 scopus 로고    scopus 로고
    • Characteristaion of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin a protease-like family of secreted proteins
    • Stein M., Kenny B., Stein M.A., Finlay B.B., Characteristaion of EspC, a 110-kilodalton protein secreted by enteropathogenic Escherichia coli which is homologous to members of the immunoglobulin A protease-like family of secreted proteins, J. Bacteriol. 178 (1996) 6546-6554.
    • (1996) J. Bacteriol. , vol.178 , pp. 6546-6554
    • Stein, M.1    Kenny, B.2    Stein, M.A.3    Finlay, B.B.4
  • 114
    • 0026562254 scopus 로고
    • Cloning, expression and nucleotide sequence of a lipase gene from Pseudomonas fluorescens B52
    • Tan Y., Miller K.J., Cloning, expression and nucleotide sequence of a lipase gene from Pseudomonas fluorescens B52, Appl. Environ. Microbiol. 58 (1992) 1402-1407.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1402-1407
    • Tan, Y.1    Miller, K.J.2
  • 115
    • 0027235473 scopus 로고
    • The RTX cytotoxin-related FrpA protein of Neisseria meningitidis is secreted extracellularly by meningococci and by the HlyBD abd Escherichia coli
    • Thompson S., Sparling P.P., The RTX cytotoxin-related FrpA protein of Neisseria meningitidis is secreted extracellularly by meningococci and by the HlyBD abd Escherichia coli, Infect. Immun. 61 (1993) 2906-2911.
    • (1993) Infect. Immun. , vol.61 , pp. 2906-2911
    • Thompson, S.1    Sparling, P.P.2
  • 116
    • 0027274752 scopus 로고
    • Cloning and nucleotide sequence of frpC, a second gene from Neisseria meningitidis encoding a protein similar to RTX cytotoxins
    • Thompson S., Wang L., Sparling P.F., Cloning and nucleotide sequence of frpC, a second gene from Neisseria meningitidis encoding a protein similar to RTX cytotoxins, Mol. Microbiol. 9 (1993) 85-96.
    • (1993) Mol. Microbiol. , vol.9 , pp. 85-96
    • Thompson, S.1    Wang, L.2    Sparling, P.F.3
  • 117
    • 0026669327 scopus 로고
    • Secretion across the bacterial outer membrane
    • Wandersman C., Secretion across the bacterial outer membrane, Trends Genet. 8 (1992) 317-321.
    • (1992) Trends Genet. , vol.8 , pp. 317-321
    • Wandersman, C.1
  • 118
    • 0025372570 scopus 로고
    • An Escherichia coli outer membrane protein required for hemolysin secretion
    • Wandersman C., Delepaire P., TolC, An Escherichia coli outer membrane protein required for hemolysin secretion, Proc. Natl, Acad. Sci. USA 87 (1990) 4776-4780.
    • (1990) Proc. Natl, Acad. Sci. USA , vol.87 , pp. 4776-4780
    • Wandersman, C.1    Delepaire, P.2    Tol, C.3
  • 119
    • 0026012975 scopus 로고
    • Analysis of the membrane organization of an Escherichia coli protein translocator, HlyB, a member of the large family of prokaryote and eukaryote surface transport proteins
    • Wang R.C., Seror S.J., Blight M., Pratt J.M., Broomesmith J.K., Holland I.B., Analysis of the membrane organization of an Escherichia coli protein translocator, HlyB, a member of the large family of prokaryote and eukaryote surface transport proteins, J. Mol. Biol. 217 (1991) 441-454.
    • (1991) J. Mol. Biol. , vol.217 , pp. 441-454
    • Wang, R.C.1    Seror, S.J.2    Blight, M.3    Pratt, J.M.4    Broomesmith, J.K.5    Holland, I.B.6
  • 120
    • 0029886432 scopus 로고    scopus 로고
    • Customized secretion chaperones in pathogenic-bacteria
    • Wattiau P., Woestyn S., Cornelis G.R., Customized secretion chaperones in pathogenic-bacteria, Mol. Microbiol. 20 (1996) 255-262.
    • (1996) Mol. Microbiol. , vol.20 , pp. 255-262
    • Wattiau, P.1    Woestyn, S.2    Cornelis, G.R.3
  • 121
    • 0002497505 scopus 로고
    • Phylogenetic analyses of the RTX toxin family
    • Roth J.A., Bolin C.A., Brogden K.A., Minion F.C., Wannemuehler M.J. (Eds.), ASM, Washington
    • Welch R.A., Phylogenetic analyses of the RTX toxin family, in: Roth J.A., Bolin C.A., Brogden K.A., Minion F.C., Wannemuehler M.J. (Eds.), Virulence Mechanisms of Bacterial Pathogens, ASM, Washington, 1995, pp. 195-206.
    • (1995) Virulence Mechanisms of Bacterial Pathogens , pp. 195-206
    • Welch, R.A.1
  • 122
    • 0031922691 scopus 로고    scopus 로고
    • Protein translocation into host epithelial cells by infecting enteropathogenic Escherichia coli
    • Wolff C., Nisan I., Hanski E., Frankel G., Rasenshine I., Protein translocation into host epithelial cells by infecting enteropathogenic Escherichia coli, Mol. Microbiol. 28 (1998) 143-155.
    • (1998) Mol. Microbiol. , vol.28 , pp. 143-155
    • Wolff, C.1    Nisan, I.2    Hanski, E.3    Frankel, G.4    Rasenshine, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.