메뉴 건너뛰기




Volumn 187, Issue 7, 2005, Pages 2286-2296

Strong decrease in invasive ability and outer membrane vesicle release in Crohn's disease-associated adherent-invasive Escherichia coli strain LF82 with the yfgL gene deleted

Author keywords

[No Author keywords available]

Indexed keywords

LIPOPROTEIN; OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN C; OUTER SURFACE PROTEIN A;

EID: 15244360470     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.7.2286-2296.2005     Document Type: Article
Times cited : (90)

References (44)
  • 2
    • 4143085204 scopus 로고    scopus 로고
    • Identification of a new Salmonella enterica serovar Enteritidis locus involved in cell invasion and in the colonisation of chicks
    • Amy, M., P. Velge, D. Senocq, E. Bottreau, F. Mompart, and I. Virlogeux-Payant. 2004. Identification of a new Salmonella enterica serovar Enteritidis locus involved in cell invasion and in the colonisation of chicks. Res. Microbiol. 155:543-552.
    • (2004) Res. Microbiol. , vol.155 , pp. 543-552
    • Amy, M.1    Velge, P.2    Senocq, D.3    Bottreau, E.4    Mompart, F.5    Virlogeux-Payant, I.6
  • 3
    • 0038349279 scopus 로고    scopus 로고
    • Regulatory and functional co-operation of flagella and type 1 pili in adhesive and invasive abilities of AIEC strain LF82 isolated from a patient with Crohn's disease
    • Barnich, N., J. Boudeau, L. Claret, and A. Darfeuille-Michaud. 2003. Regulatory and functional co-operation of flagella and type 1 pili in adhesive and invasive abilities of AIEC strain LF82 isolated from a patient with Crohn's disease. Mol. Microbiol. 48:781-794.
    • (2003) Mol. Microbiol. , vol.48 , pp. 781-794
    • Barnich, N.1    Boudeau, J.2    Claret, L.3    Darfeuille-Michaud, A.4
  • 4
    • 2142763021 scopus 로고    scopus 로고
    • Involvement of lipoprotein NlpI in the virulence of adherent invasive Escherichia coli strain LF82 isolated from a patient with Crohn's disease
    • Barnich, N., M. A. Bringer, L. Claret, and A. Darfeuille-Michaud. 2004. Involvement of lipoprotein NlpI in the virulence of adherent invasive Escherichia coli strain LF82 isolated from a patient with Crohn's disease. Infect. Immun. 72:2484-2493.
    • (2004) Infect. Immun. , vol.72 , pp. 2484-2493
    • Barnich, N.1    Bringer, M.A.2    Claret, L.3    Darfeuille-Michaud, A.4
  • 6
    • 0032839616 scopus 로고    scopus 로고
    • Structures of gram-negative cell walls and their derived membrane vesicles
    • Beveridge, T. J. 1999. Structures of gram-negative cell walls and their derived membrane vesicles. J. Bacteriol. 181:4725-4733.
    • (1999) J. Bacteriol. , vol.181 , pp. 4725-4733
    • Beveridge, T.J.1
  • 7
    • 0035100599 scopus 로고    scopus 로고
    • Type 1 pili-mediated adherence of Escherichia coli strain LF82 isolated from Crohn's disease is involved in bacterial invasion of intestinal epithelial cells
    • Boudeau, J., N. Barnich, and A. Darfeuille-Michaud. 2001. Type 1 pili-mediated adherence of Escherichia coli strain LF82 isolated from Crohn's disease is involved in bacterial invasion of intestinal epithelial cells. Mol. Microbiol. 39:1272-1284.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1272-1284
    • Boudeau, J.1    Barnich, N.2    Darfeuille-Michaud, A.3
  • 8
    • 0032768352 scopus 로고    scopus 로고
    • Invasive ability of an Escherichia coli strain isolated from the ileal mucosa of a patient with Crohn's disease
    • Boudeau, J., A. L. Glasser, E. Masseret, B. Joly, and A. Darfeuille-Michaud. 1999. Invasive ability of an Escherichia coli strain isolated from the ileal mucosa of a patient with Crohn's disease. Infect. Immun. 67:4499-4509.
    • (1999) Infect. Immun. , vol.67 , pp. 4499-4509
    • Boudeau, J.1    Glasser, A.L.2    Masseret, E.3    Joly, B.4    Darfeuille-Michaud, A.5
  • 9
    • 0023912441 scopus 로고
    • Adhesive Escherichia coli in inflammatory bowel disease and infective diarrhoea
    • Burke, D. A., and A. T. Axon. 1988. Adhesive Escherichia coli in inflammatory bowel disease and infective diarrhoea. BMJ 297:102-104.
    • (1988) BMJ , vol.297 , pp. 102-104
    • Burke, D.A.1    Axon, A.T.2
  • 10
    • 0034650563 scopus 로고    scopus 로고
    • The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9
    • Carr, S., C. N. Penfold, V. Bamford, R. James, and A. M. Hemmings. 2000. The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9. Structure Fold. Des. 8:57-66.
    • (2000) Structure Fold. Des. , vol.8 , pp. 57-66
    • Carr, S.1    Penfold, C.N.2    Bamford, V.3    James, R.4    Hemmings, A.M.5
  • 11
    • 0036180995 scopus 로고    scopus 로고
    • Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity
    • Cascales, E., A. Bernadac, M. Gavioli, J. C. Lazzaroni, and R. Lloubes. 2002. Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity. J. Bacteriol. 184:754-759.
    • (2002) J. Bacteriol. , vol.184 , pp. 754-759
    • Cascales, E.1    Bernadac, A.2    Gavioli, M.3    Lazzaroni, J.C.4    Lloubes, R.5
  • 12
    • 0034668869 scopus 로고    scopus 로고
    • A rapid method for efficient gene replacement in the filamentous fungus Aspergillus nidulans
    • Online
    • Chaveroche, M. K., J. M. Ghigo, and C. d'Enfert. 2000. A rapid method for efficient gene replacement in the filamentous fungus Aspergillus nidulans. Nucleic Acids Res. 28:E97. [Online.] http://nar.oupjournals.org/cgi/content /full/28/22/e97.
    • (2000) Nucleic Acids Res. , vol.28
    • Chaveroche, M.K.1    Ghigo, J.M.2    D'Enfert, C.3
  • 15
    • 0037303720 scopus 로고    scopus 로고
    • Interaction of Actinobacillus actinomycetemcomitans outer membrane vesicles with HL60 cells does not require leukotoxin
    • Demuth, D. R., D. James, Y. Kowashi, and S. Kato. 2003. Interaction of Actinobacillus actinomycetemcomitans outer membrane vesicles with HL60 cells does not require leukotoxin. Cell. Microbiol. 5:111-121.
    • (2003) Cell. Microbiol. , vol.5 , pp. 111-121
    • Demuth, D.R.1    James, D.2    Kowashi, Y.3    Kato, S.4
  • 16
    • 0025428207 scopus 로고
    • A comparison of HEp-2 cell invasion by enteropathogenic and enteroinvasive Escherichia coli
    • Donnenberg, M. S., A. Donohue-Rolfe, and G. T. Keusch. 1990. A comparison of HEp-2 cell invasion by enteropathogenic and enteroinvasive Escherichia coli. FEMS Microbiol. Lett. 57:83-86.
    • (1990) FEMS Microbiol. Lett. , vol.57 , pp. 83-86
    • Donnenberg, M.S.1    Donohue-Rolfe, A.2    Keusch, G.T.3
  • 17
    • 0033576418 scopus 로고    scopus 로고
    • Crohn disease, ulcerative colitis. When bacteria attack the intestinal wall
    • In German
    • Duchmann, R., H. Lochs, and W. Kruis. 1999. Crohn disease, ulcerative colitis. When bacteria attack the intestinal wall. MMW Fortschr. Med. 141:48-51. [In German.]
    • (1999) MMW Fortschr. Med. , vol.141 , pp. 48-51
    • Duchmann, R.1    Lochs, H.2    Kruis, W.3
  • 18
    • 0035850868 scopus 로고    scopus 로고
    • Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin
    • Eggert, U. S., N. Ruiz, B. V. Falcone, A. A. Branstrom, R. C. Goldman, T. J. Silhavy, and D. Kahne. 2001. Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin. Science 294:361-364.
    • (2001) Science , vol.294 , pp. 361-364
    • Eggert, U.S.1    Ruiz, N.2    Falcone, B.V.3    Branstrom, A.A.4    Goldman, R.C.5    Silhavy, T.J.6    Kahne, D.7
  • 19
    • 0032982467 scopus 로고    scopus 로고
    • Release of Helicobacter pylori vacuolating cytotoxin by both a specific secretion pathway and budding of outer membrane vesicles. Uptake of released toxin and vesicles by gastric epithelium
    • Fiocca, R., V. Necchi, P. Sommi, V. Ricci, J. Telford, T. L. Cover, and E. Solcia. 1999. Release of Helicobacter pylori vacuolating cytotoxin by both a specific secretion pathway and budding of outer membrane vesicles. Uptake of released toxin and vesicles by gastric epithelium. J. Pathol. 188:220-226.
    • (1999) J. Pathol. , vol.188 , pp. 220-226
    • Fiocca, R.1    Necchi, V.2    Sommi, P.3    Ricci, V.4    Telford, J.5    Cover, T.L.6    Solcia, E.7
  • 21
    • 0037031850 scopus 로고    scopus 로고
    • Bacterial surface association of heat-labile enterotoxin through lipopolysaceharide after secretion via the general secretory pathway
    • Horstman, A. L., and M. J. Kuehn. 2002. Bacterial surface association of heat-labile enterotoxin through lipopolysaceharide after secretion via the general secretory pathway. J. Biol. Chem. 277:32538-32545.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32538-32545
    • Horstman, A.L.1    Kuehn, M.J.2
  • 22
    • 0030844077 scopus 로고    scopus 로고
    • Natural release of virulence factors in membrane vesicles by Pseudomonas aeruginosa and the effect of aminoglycoside antibiotics on their release
    • Kadurugamuwa, J. L., and T. J. Beveridge. 1997. Natural release of virulence factors in membrane vesicles by Pseudomonas aeruginosa and the effect of aminoglycoside antibiotics on their release. J. Antimicrob. Chemother. 40:615-621.
    • (1997) J. Antimicrob. Chemother. , vol.40 , pp. 615-621
    • Kadurugamuwa, J.L.1    Beveridge, T.J.2
  • 23
    • 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, J. L., and T. J. Beveridge. 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. J. Bacteriol. 177:3998-4008.
    • (1995) J. Bacteriol. , vol.177 , pp. 3998-4008
    • Kadurugamuwa, J.L.1    Beveridge, T.J.2
  • 24
    • 0036157198 scopus 로고    scopus 로고
    • Outer membrane-like vesicles secreted by Actinobacillus actinomycetemcomitans are enriched in leukotoxin
    • Kato, S., Y. Kowashi, and D. R. Demuth. 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
  • 25
    • 0346457133 scopus 로고    scopus 로고
    • Incorporation of heterologous outer membrane and periplasmic proteins into Escherichia coli outer membrane vesicles
    • Kesty, N. C., and M. J. Kuehn. 2004. Incorporation of heterologous outer membrane and periplasmic proteins into Escherichia coli outer membrane vesicles. J. Biol. Chem. 279:2069-2076.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2069-2076
    • Kesty, N.C.1    Kuehn, M.J.2
  • 26
    • 10644226878 scopus 로고    scopus 로고
    • Enterotoxigenic Escherichia coli vesicles target toxin delivery into mammalian cells
    • Kesty, N. C., K. M. Mason, M. Reedy, S. E. Miller, and M. J. Kuehn. 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
  • 27
    • 0032959537 scopus 로고    scopus 로고
    • Export of virulence genes and Shiga toxin by membrane vesicles of Escherichia coli O157:H7
    • Kolling, G. L., and K. R. Matthews. 1999. Export of virulence genes and Shiga toxin by membrane vesicles of Escherichia coli O157:H7. Appl. Environ. Microbiol. 65:1843-1848.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1843-1848
    • Kolling, G.L.1    Matthews, K.R.2
  • 29
    • 0021359430 scopus 로고
    • Coli surface antigens 1 and 3 of colonization factor antigen H-positive enterotoxigenic Escherichia coli: Morphology, purification, and immune responses in humans
    • Levine, M. M., P. Ristaino, G. Marley, C. Smyth, S. Knutton, E. Boedeker, R. Black, C. Young, M. L. Clements, C. Cheney, and R. Patnaik. 1984. Coli surface antigens 1 and 3 of colonization factor antigen H-positive enterotoxigenic Escherichia coli: morphology, purification, and immune responses in humans. Infect. Immun. 44:409-420.
    • (1984) Infect. Immun. , vol.44 , pp. 409-420
    • Levine, M.M.1    Ristaino, P.2    Marley, G.3    Smyth, C.4    Knutton, S.5    Boedeker, E.6    Black, R.7    Young, C.8    Clements, M.L.9    Cheney, C.10    Patnaik, R.11
  • 30
    • 0031663159 scopus 로고    scopus 로고
    • Gram-negative bacteria produce membrane vesicles which are capable of killing other bacteria
    • Li, Z., A. J. Clarke, and T. J. Beveridge. 1998. Gram-negative bacteria produce membrane vesicles which are capable of killing other bacteria. J. Bacteriol. 180:5478-5483.
    • (1998) J. Bacteriol. , vol.180 , pp. 5478-5483
    • Li, Z.1    Clarke, A.J.2    Beveridge, T.J.3
  • 31
    • 0028901664 scopus 로고
    • Immunocytochemical evidence of Listeria, Escherichia coli, and Streptococcus antigens in Crohn's disease
    • Liu, Y., H. J. van Kruiningen, A. B. West, R. W. Cartun, A. Cortot, and J. F. Colombel. 1995. Immunocytochemical evidence of Listeria, Escherichia coli, and Streptococcus antigens in Crohn's disease. Gastroenterology 108:1396-1404.
    • (1995) Gastroenterology , vol.108 , pp. 1396-1404
    • Liu, Y.1    Van Kruiningen, H.J.2    West, A.B.3    Cartun, R.W.4    Cortot, A.5    Colombel, J.F.6
  • 32
    • 0017648083 scopus 로고
    • Factors regulating cell wall thickening and intracellular iodophilic polysaccharide storage in Streptococcus mutans
    • Mattingly, S. J., L. Daneo-Moore, and G. D. Shockman. 1977. Factors regulating cell wall thickening and intracellular iodophilic polysaccharide storage in Streptococcus mutans. Infect. Immun. 16:967-973.
    • (1977) Infect. Immun. , vol.16 , pp. 967-973
    • Mattingly, S.J.1    Daneo-Moore, L.2    Shockman, G.D.3
  • 33
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., D. J. Pappin, D. M. Creasy, and J. S. Cottrell. 1999. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 34
    • 0038010148 scopus 로고    scopus 로고
    • Protein-peptidoglycan interactions modulate the assembly of the needle complex in the Salmonella invasion-associated type III secretion system
    • Pucciarelli, M. G., and F. Garcia-del Portillo. 2003. Protein-peptidoglycan interactions modulate the assembly of the needle complex in the Salmonella invasion-associated type III secretion system. Mol. Microbiol. 48:573-585.
    • (2003) Mol. Microbiol. , vol.48 , pp. 573-585
    • Pucciarelli, M.G.1    Garcia-del Portillo, F.2
  • 35
    • 0018723647 scopus 로고
    • Factors affecting the electrophoretic mobility of the major outer membrane proteins of Escherichia coli in polyacrylamide gels
    • Pugsley, A. P., and C. A. Schnaitman. 1979. Factors affecting the electrophoretic mobility of the major outer membrane proteins of Escherichia coli in polyacrylamide gels. Biochim. Biophys. Acta 581:163-178.
    • (1979) Biochim. Biophys. Acta , vol.581 , pp. 163-178
    • Pugsley, A.P.1    Schnaitman, C.A.2
  • 38
    • 0030747584 scopus 로고    scopus 로고
    • Frequency of pathogenic and enteroadherent Escherichia coli in patients with inflammatory bowel disease and controls
    • Schultsz, C., M. Moussa, R. van Ketel, G. N. Tytgat, and J. Dankert. 1997. Frequency of pathogenic and enteroadherent Escherichia coli in patients with inflammatory bowel disease and controls. J. Clin. Pathol. 50:573-579.
    • (1997) J. Clin. Pathol. , vol.50 , pp. 573-579
    • Schultsz, C.1    Moussa, M.2    Van Ketel, R.3    Tytgat, G.N.4    Dankert, J.5
  • 39
    • 0023571657 scopus 로고
    • High-copy-number and low-copy-number plasmid vectors for lacZ alpha-complementation and chloramphenicol- or kanamycin-resistance selection
    • Takeshita, S., M. Sato, M. Toba, W. Masahashi, and T. Hashimoto-Gotoh. 1987. High-copy-number and low-copy-number plasmid vectors for lacZ alpha-complementation and chloramphenicol- or kanamycin-resistance selection. Gene 61:63-74.
    • (1987) Gene , vol.61 , pp. 63-74
    • Takeshita, S.1    Sato, M.2    Toba, M.3    Masahashi, W.4    Hashimoto-Gotoh, T.5
  • 40
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 41
    • 0033525526 scopus 로고    scopus 로고
    • Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli
    • Vollmer, W., M. von Rechenberg, and J. V. Holtje. 1999. Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli. J. Biol. Chem. 274:6726-6734.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6726-6734
    • Vollmer, W.1    Von Rechenberg, M.2    Holtje, J.V.3
  • 43
    • 0019795018 scopus 로고
    • Outer-membrane vesicles released by normally growing Escherichia coli contain very little lipoprotein
    • Wensink, J., and B. Witholt. 1981. Outer-membrane vesicles released by normally growing Escherichia coli contain very little lipoprotein. Eur. J. Biochem. 116:331-335.
    • (1981) Eur. J. Biochem. , vol.116 , pp. 331-335
    • Wensink, J.1    Witholt, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.