메뉴 건너뛰기




Volumn 189, Issue 13, 2007, Pages 4860-4871

The oxidoreductase DsbA plays a key role in the ability of the Crohn's disease-associated adherent-invasive Escherichia coli strain LF82 to resist macrophage killing

Author keywords

[No Author keywords available]

Indexed keywords

DSBA PROTEIN; OXIDOREDUCTASE;

EID: 34347368520     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00233-07     Document Type: Article
Times cited : (65)

References (74)
  • 2
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J. C., K. McGovern, and J. Beckwith. 1991. Identification of a protein required for disulfide bond formation in vivo. Cell 67:581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 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 N1pI 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 N1pI 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
  • 5
    • 0028593831 scopus 로고
    • The Escherichia coll dsbA gene is partly transcribed from the promoter of a weakly expressed upstream gene
    • Belin, P., and P. L. Boquet. 1994. The Escherichia coll dsbA gene is partly transcribed from the promoter of a weakly expressed upstream gene. Microbiology 140:3337-3348.
    • (1994) Microbiology , vol.140 , pp. 3337-3348
    • Belin, P.1    Boquet, P.L.2
  • 6
    • 0033583239 scopus 로고    scopus 로고
    • In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
    • Bessette, P. H., J. J. Cotto, H. F. Gilbert, and G. Georgiou. 1999. In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG. J. Biol. Chem. 274:7784-7792.
    • (1999) J. Biol. Chem , vol.274 , pp. 7784-7792
    • Bessette, P.H.1    Cotto, J.J.2    Gilbert, H.F.3    Georgiou, G.4
  • 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
    • 12844262949 scopus 로고    scopus 로고
    • HtrA stress protein is involved in imramacrophagic replication of adherent and invasive Escherichia coli strain LF82 isolated from a patient with Crohn's disease
    • Bringer, M. A., N. Barnich, A. L. Glasser, O. Bardot, and A. Darfeuille-Michaud. 2005. HtrA stress protein is involved in imramacrophagic replication of adherent and invasive Escherichia coli strain LF82 isolated from a patient with Crohn's disease. Infect. Immun. 73:712-721.
    • (2005) Infect. Immun , vol.73 , pp. 712-721
    • Bringer, M.A.1    Barnich, N.2    Glasser, A.L.3    Bardot, O.4    Darfeuille-Michaud, A.5
  • 10
    • 33644831090 scopus 로고    scopus 로고
    • The Crohn's disease-associated adherent-invasive Escherichia coli strain LF82 replicates in mature phagolysosomes within J774 macrophages
    • Bringer, M. A., A. L. Glasser, C. H. Tung, S. Meresse, and A. Darfeuille-Michaud. 2006. The Crohn's disease-associated adherent-invasive Escherichia coli strain LF82 replicates in mature phagolysosomes within J774 macrophages. Cell. Microbiol. 8:471-484.
    • (2006) Cell. Microbiol , vol.8 , pp. 471-484
    • Bringer, M.A.1    Glasser, A.L.2    Tung, C.H.3    Meresse, S.4    Darfeuille-Michaud, A.5
  • 11
    • 31844447028 scopus 로고    scopus 로고
    • Adaptation of Legionella pneumophila to the host environment: Role of protein secretion, effectors and eukaryotic-like proteins
    • Bruggemann, H., C. Cazalet, and C. Buchrieser. 2006. Adaptation of Legionella pneumophila to the host environment: role of protein secretion, effectors and eukaryotic-like proteins. Curr. Opin. Microbiol. 9:86-94.
    • (2006) Curr. Opin. Microbiol , vol.9 , pp. 86-94
    • Bruggemann, H.1    Cazalet, C.2    Buchrieser, C.3
  • 12
    • 2142751620 scopus 로고    scopus 로고
    • Proteus mirabilis genes that contribute to pathogenesis of urinary tract infection: Identification of 25 signature-tagged mutants attenuated at least 100-fold
    • Burall, L. S., J. M. Harro, X. Li, C. V. Lockatell, S. D. Himpsl, J. R. Hebel, D. E. Johnson, and H. L. Mobley. 2004. Proteus mirabilis genes that contribute to pathogenesis of urinary tract infection: identification of 25 signature-tagged mutants attenuated at least 100-fold. Infect. Immun. 72:2922-2938.
    • (2004) Infect. Immun , vol.72 , pp. 2922-2938
    • Burall, L.S.1    Harro, J.M.2    Li, X.3    Lockatell, C.V.4    Himpsl, S.D.5    Hebel, J.R.6    Johnson, D.E.7    Mobley, H.L.8
  • 13
    • 32644435882 scopus 로고    scopus 로고
    • Surviving inside a macrophage: The many ways of Brucella
    • Celli, J. 2006. Surviving inside a macrophage: the many ways of Brucella. Res. Microbiol. 157:93-98.
    • (2006) Res. Microbiol , vol.157 , pp. 93-98
    • Celli, J.1
  • 14
    • 0034668869 scopus 로고    scopus 로고
    • A rapid method for efficient gene replacement in the filamentous fungus Aspergillus nidulans
    • 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.
    • (2000) Nucleic Acids Res , vol.28
    • Chaveroche, M.K.1    Ghigo, J.M.2    d'Enfert, C.3
  • 15
    • 0036752926 scopus 로고    scopus 로고
    • The HtrA family of proteases: Implications for protein composition and cell fate
    • Clausen, T., C. Southan, and M. Ehrmann. 2002. The HtrA family of proteases: implications for protein composition and cell fate. Mol. Cell 10:443-455.
    • (2002) Mol. Cell , vol.10 , pp. 443-455
    • Clausen, T.1    Southan, C.2    Ehrmann, M.3
  • 16
    • 0027446271 scopus 로고
    • Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli
    • Dailey, F. E., and H. C. Berg. 1993. Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli. Proc. Natl. Acad. Sci. USA 90:1043-1047.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1043-1047
    • Dailey, F.E.1    Berg, H.C.2
  • 17
    • 0030998321 scopus 로고    scopus 로고
    • The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli
    • Danese, P. N., and T. J. Silhavy. 1997. The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli. Genes Dev. 11:1183-1193.
    • (1997) Genes Dev , vol.11 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 20
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 21
    • 0037135593 scopus 로고    scopus 로고
    • Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli
    • De Wulf, P., A. M. McGuire, X. Liu, and E. C. Lin. 2002. Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli. J. Biol. Chem. 277:26652-26661.
    • (2002) J. Biol. Chem , vol.277 , pp. 26652-26661
    • De Wulf, P.1    McGuire, A.M.2    Liu, X.3    Lin, E.C.4
  • 22
    • 0037384456 scopus 로고    scopus 로고
    • Signal detection and target gene induction by the CpxRA two-component system
    • DiGiuseppe, P. A., and T. J. Silhavy. 2003. Signal detection and target gene induction by the CpxRA two-component system. J. Bacteriol. 185:2432-2440.
    • (2003) J. Bacteriol , vol.185 , pp. 2432-2440
    • DiGiuseppe, P.A.1    Silhavy, T.J.2
  • 23
    • 0031006045 scopus 로고    scopus 로고
    • Biogenesis of the bundle-forming pilus of enteropathogenic Escherichia coli: Reconstitution of fimbriae in recombinant E. coli and role of DsbA in pilin stability - a review
    • Donnenberg, M. S., H. Z. Zhang, and K. D. Stone. 1997. Biogenesis of the bundle-forming pilus of enteropathogenic Escherichia coli: reconstitution of fimbriae in recombinant E. coli and role of DsbA in pilin stability - a review. Gene 192:33-38.
    • (1997) Gene , vol.192 , pp. 33-38
    • Donnenberg, M.S.1    Zhang, H.Z.2    Stone, K.D.3
  • 24
    • 1942440958 scopus 로고    scopus 로고
    • The role of the Shigella flexneri yihE gene in LPS synthesis and virulence
    • Edwards-Jones, B., P. R. Langford, J. S. Kroll, and J. Yu. 2004. The role of the Shigella flexneri yihE gene in LPS synthesis and virulence. Microbiology 150:1079-1084.
    • (2004) Microbiology , vol.150 , pp. 1079-1084
    • Edwards-Jones, B.1    Langford, P.R.2    Kroll, J.S.3    Yu, J.4
  • 25
    • 0033937341 scopus 로고    scopus 로고
    • Commensal bacteria as targets in Crohn's disease
    • Elson, C. O. 2000. Commensal bacteria as targets in Crohn's disease. Gastroenterology 119:254-257.
    • (2000) Gastroenterology , vol.119 , pp. 254-257
    • Elson, C.O.1
  • 26
    • 0033591446 scopus 로고    scopus 로고
    • Type III secretion machines: Bacterial devices for protein delivery into host cells
    • Galan, J. E., and A. Collmer. 1999. Type III secretion machines: bacterial devices for protein delivery into host cells. Science 284:1322-1328.
    • (1999) Science , vol.284 , pp. 1322-1328
    • Galan, J.E.1    Collmer, A.2
  • 27
    • 0034873344 scopus 로고    scopus 로고
    • Adherent invasive Escherichia coli strains from patients with Crohn's disease survive and replicate within macrophages without inducing host cell death
    • Glasser, A. L., J. Boudeau, N. Barnich, M. H. Perruchot, J. F. Colombel, and A. Darfeuille-Michaud. 2001. Adherent invasive Escherichia coli strains from patients with Crohn's disease survive and replicate within macrophages without inducing host cell death. Infect. Immun. 69:5529-5537.
    • (2001) Infect. Immun , vol.69 , pp. 5529-5537
    • Glasser, A.L.1    Boudeau, J.2    Barnich, N.3    Perruchot, M.H.4    Colombel, J.F.5    Darfeuille-Michaud, A.6
  • 29
    • 0035339417 scopus 로고    scopus 로고
    • Adaptation of signature-tagged mutagenesis to Escherichia coli K1 and the infant-rat model of invasive disease
    • Gonzalez, M. D., C. A. Lichtensteiger, and E. R. Vimr. 2001. Adaptation of signature-tagged mutagenesis to Escherichia coli K1 and the infant-rat model of invasive disease. FEMS Microbiol. Lett. 198:125-128.
    • (2001) FEMS Microbiol. Lett , vol.198 , pp. 125-128
    • Gonzalez, M.D.1    Lichtensteiger, C.A.2    Vimr, E.R.3
  • 30
    • 0028971218 scopus 로고
    • Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
    • Guilhot, C., G. Jander, N. L. Martin, and J. Beckwith. 1995. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc. Natl. Acad. Sci. USA 92:9895-9899.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9895-9899
    • Guilhot, C.1    Jander, G.2    Martin, N.L.3    Beckwith, J.4
  • 31
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., D. Belin, M. J. Carson, and J. Beckwith. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 32
    • 0037372822 scopus 로고    scopus 로고
    • DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors
    • Ha, U. H., Y. Wang, and S. Jin. 2003. DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors. Infect. Immun. 71:1590-1595.
    • (2003) Infect. Immun , vol.71 , pp. 1590-1595
    • Ha, U.H.1    Wang, Y.2    Jin, S.3
  • 33
    • 0031585999 scopus 로고    scopus 로고
    • Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae
    • Hu, S. H., J. A. Peek, E. Rattigan, R. K. Taylor, and J. L. Martin. 1997. Structure of TcpG, the DsbA protein folding catalyst from Vibrio cholerae. J. Mol. Biol. 268:137-146.
    • (1997) J. Mol. Biol , vol.268 , pp. 137-146
    • Hu, S.H.1    Peek, J.A.2    Rattigan, E.3    Taylor, R.K.4    Martin, J.L.5
  • 34
    • 0032871341 scopus 로고    scopus 로고
    • DsbA is required for stable expression of outer membrane protein YscC and for efficient Yop secretion in Yersinia pestis
    • Jackson, M. W., and G. V. Piano. 1999. DsbA is required for stable expression of outer membrane protein YscC and for efficient Yop secretion in Yersinia pestis. J. Bacteriol. 181:5126-5130.
    • (1999) J. Bacteriol , vol.181 , pp. 5126-5130
    • Jackson, M.W.1    Piano, G.V.2
  • 36
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • Kadokura, H., F. Katzen, and J. Beckwith. 2003. Protein disulfide bond formation in prokaryotes. Annu. Rev. Biochem. 72:111-135.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 37
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • Katzen, F., and J. Beckwith. 2000. Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell 103:769-779.
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 38
    • 0042357064 scopus 로고    scopus 로고
    • Taking possession: Biogenesis of the Salmonella-containing vacuole
    • Knodler, L. A., and O. Steele-Mortimer. 2003. Taking possession: biogenesis of the Salmonella-containing vacuole. Traffic 4:587-599.
    • (2003) Traffic , vol.4 , pp. 587-599
    • Knodler, L.A.1    Steele-Mortimer, O.2
  • 39
    • 0030671552 scopus 로고    scopus 로고
    • Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
    • Kobayashi, T., S. Kishigami, M. Sone, H. Inokuchi, T. Mogi, and K. Ito. 1997. Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells. Proc. Natl. Acad. Sci. USA 94:11857-11862.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11857-11862
    • Kobayashi, T.1    Kishigami, S.2    Sone, M.3    Inokuchi, H.4    Mogi, T.5    Ito, K.6
  • 41
    • 0021359430 scopus 로고
    • Coli surface antigens 1 and 3 of colonization factor antigen II-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, et al. 1984. Coli surface antigens 1 and 3 of colonization factor antigen II-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
  • 42
    • 0035914063 scopus 로고    scopus 로고
    • Influence of the yihE gene of Shigella flexneri on global gene expression: On analysis using DNA arrays
    • Li, M. S., J. S. Kroll, and J. Yu. 2001. Influence of the yihE gene of Shigella flexneri on global gene expression: on analysis using DNA arrays. Biochem. Biophys. Res. Commun. 288:91-100.
    • (2001) Biochem. Biophys. Res. Commun , vol.288 , pp. 91-100
    • Li, M.S.1    Kroll, J.S.2    Yu, J.3
  • 44
    • 4544229875 scopus 로고    scopus 로고
    • Two periplasmic disulfide oxidoreductases, DsbA and SrgA, target outer membrane protein SpiA, a component of the Salmonella pathogenicity island 2 type III secretion system
    • Miki, T., N. Okada, and H. Danbara. 2004. Two periplasmic disulfide oxidoreductases, DsbA and SrgA, target outer membrane protein SpiA, a component of the Salmonella pathogenicity island 2 type III secretion system. J. Biol. Chem. 279:34631-34642.
    • (2004) J. Biol. Chem , vol.279 , pp. 34631-34642
    • Miki, T.1    Okada, N.2    Danbara, H.3
  • 45
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas, D., and S. Raina. 1997. Protein folding in the bacterial periplasm. J. Bacteriol. 179:2465-2471.
    • (1997) J. Bacteriol , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 46
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
    • Missiakas, D., F. Schwager, and S. Raina. 1995. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14:3415-3424.
    • (1995) EMBO J , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2    Raina, S.3
  • 48
    • 0034991242 scopus 로고    scopus 로고
    • Region of heatstable enterotoxin II of Escherichia coli involved in translocation across the outer membrane
    • Okamoto, K., H. Yamanaka, M. Takeji, and Y. Fuji. 2001. Region of heatstable enterotoxin II of Escherichia coli involved in translocation across the outer membrane. Microbiol. Immunol. 45:349-355.
    • (2001) Microbiol. Immunol , vol.45 , pp. 349-355
    • Okamoto, K.1    Yamanaka, H.2    Takeji, M.3    Fuji, Y.4
  • 49
    • 0026668342 scopus 로고
    • Characterization of a periplasmic thiol: Disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae
    • Peek, J. A., and R. K. Taylor. 1992. Characterization of a periplasmic thiol: disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae. Proc. Natl. Acad. Sci. USA 89:6210-6214.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6210-6214
    • Peek, J.A.1    Taylor, R.K.2
  • 50
    • 0037043658 scopus 로고    scopus 로고
    • Inflammatory bowel disease
    • Podolsky, D. K. 2002. Inflammatory bowel disease. N. Engl. J. Med. 347:417-429.
    • (2002) N. Engl. J. Med , vol.347 , pp. 417-429
    • Podolsky, D.K.1
  • 51
    • 0030992719 scopus 로고    scopus 로고
    • Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system
    • Pogliano, J., A. S. Lynch, D. Belin, E. C. Lin, and J. Beckwith. 1997. Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system. Genes Dev. 11:1169-1182.
    • (1997) Genes Dev , vol.11 , pp. 1169-1182
    • Pogliano, J.1    Lynch, A.S.2    Belin, D.3    Lin, E.C.4    Beckwith, J.5
  • 52
    • 19944402536 scopus 로고    scopus 로고
    • Envelope stress responses and Gram-negative bacterial pathogenesis
    • Raivio, T. L. 2005. Envelope stress responses and Gram-negative bacterial pathogenesis. Mol. Microbiol. 56:1119-1128.
    • (2005) Mol. Microbiol , vol.56 , pp. 1119-1128
    • Raivio, T.L.1
  • 53
    • 0029822654 scopus 로고    scopus 로고
    • An in vivo pathway for disulfide bond isomerization in Escherichia coli
    • Rietsch, A., D. Belin, N. Martin, and J. Beckwith. 1996. An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc. Natl. Acad. Sci. USA 93:13048-13053.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13048-13053
    • Rietsch, A.1    Belin, D.2    Martin, N.3    Beckwith, J.4
  • 54
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch, A., P. Bessette, G. Georgiou, and J. Beckwith. 1997. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J. Bacteriol. 179:6602-6608.
    • (1997) J. Bacteriol , vol.179 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 55
    • 15244360470 scopus 로고    scopus 로고
    • 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
    • Rolhion, N., N. Barnich, L. Claret, and A. Darfeuille-Michaud. 2005. 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. J. Bacteriol. 187:2286-2296.
    • (2005) J. Bacteriol , vol.187 , pp. 2286-2296
    • Rolhion, N.1    Barnich, N.2    Claret, L.3    Darfeuille-Michaud, A.4
  • 56
    • 4444306100 scopus 로고    scopus 로고
    • Bacterial DNA within granulomas of patients with Crohn's disease - detection by laser capture microdissection and PCR
    • Ryan, P., R. G. Kelly, G. Lee, J. K. Collins, G. C. O'Sullivan, J. O'Connell, and F. Shanahan. 2004. Bacterial DNA within granulomas of patients with Crohn's disease - detection by laser capture microdissection and PCR. Am. J. Gastroenterol. 99:1539-1543.
    • (2004) Am. J. Gastroenterol , vol.99 , pp. 1539-1543
    • Ryan, P.1    Kelly, R.G.2    Lee, G.3    Collins, J.K.4    O'Sullivan, G.C.5    O'Connell, J.6    Shanahan, F.7
  • 58
    • 0026533111 scopus 로고
    • Growth conditions mediate differential transcription of fim genes involved in phase variation of type 1 pili
    • Schwan, W. R., H. S. Seifert, and J. L. Duncan. 1992. Growth conditions mediate differential transcription of fim genes involved in phase variation of type 1 pili. J. Bacteriol. 174:2367-2375.
    • (1992) J. Bacteriol , vol.174 , pp. 2367-2375
    • Schwan, W.R.1    Seifert, H.S.2    Duncan, J.L.3
  • 59
    • 0037022008 scopus 로고    scopus 로고
    • Crohn's disease
    • Shanahan, F. 2002. Crohn's disease. Lancet 359:62-69.
    • (2002) Lancet , vol.359 , pp. 62-69
    • Shanahan, F.1
  • 60
    • 33749846008 scopus 로고    scopus 로고
    • Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli
    • Skorko-Glonek, J., A. Sobiecka-Szkatula, and B. Lipinska. 2006. Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli. Acta Biochim. Pol. 53:585-589.
    • (2006) Acta Biochim. Pol , vol.53 , pp. 585-589
    • Skorko-Glonek, J.1    Sobiecka-Szkatula, A.2    Lipinska, B.3
  • 61
    • 0036117802 scopus 로고    scopus 로고
    • DsbA and DsbC are required for secretion of pertussis toxin by Bordetella pertussis
    • Stenson, T. H., and A. A. Weiss. 2002. DsbA and DsbC are required for secretion of pertussis toxin by Bordetella pertussis. Infect. Immun. 70:2297-2303.
    • (2002) Infect. Immun , vol.70 , pp. 2297-2303
    • Stenson, T.H.1    Weiss, A.A.2
  • 62
    • 0030918120 scopus 로고    scopus 로고
    • Domains within the Vibrio cholerae toxin coregulated pilin subunit that mediate bacterial colonization
    • Sun, D., M. Lafferty, J. Peek, and R. Taylor. 1997. Domains within the Vibrio cholerae toxin coregulated pilin subunit that mediate bacterial colonization. Gene 192:79-85.
    • (1997) Gene , vol.192 , pp. 79-85
    • Sun, D.1    Lafferty, M.2    Peek, J.3    Taylor, R.4
  • 63
    • 0037224512 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium rdoA is growth phase regulated and involved in relaying Cpx-induced signals
    • Suntharalingam, P., H. Spencer, C. V. Gallant, and N. L. Martin. 2003. Salmonella enterica serovar Typhimurium rdoA is growth phase regulated and involved in relaying Cpx-induced signals. J. Bacteriol. 185:432-443.
    • (2003) J. Bacteriol , vol.185 , pp. 432-443
    • Suntharalingam, P.1    Spencer, H.2    Gallant, C.V.3    Martin, N.L.4
  • 65
    • 3042695340 scopus 로고    scopus 로고
    • Three homologues, including two membrane-bound proteins, of the disulfide oxidoreductase DsbA in Neisseria meningitidis: Effects on bacterial growth and biogenesis of functional type IV pili
    • Tinsley, C. R., R. Voulhoux, J. L. Beretti, J. Tommassen, and X. Nassif. 2004. Three homologues, including two membrane-bound proteins, of the disulfide oxidoreductase DsbA in Neisseria meningitidis: effects on bacterial growth and biogenesis of functional type IV pili. J. Biol. Chem. 279:27078-27087.
    • (2004) J. Biol. Chem , vol.279 , pp. 27078-27087
    • Tinsley, C.R.1    Voulhoux, R.2    Beretti, J.L.3    Tommassen, J.4    Nassif, X.5
  • 66
    • 0030866940 scopus 로고    scopus 로고
    • Fluorescence-based isolation of bacterial genes expressed within host cells
    • Valdivia, R. H., and S. Falkow. 1997. Fluorescence-based isolation of bacterial genes expressed within host cells. Science 277:2007-2011.
    • (1997) Science , vol.277 , pp. 2007-2011
    • Valdivia, R.H.1    Falkow, S.2
  • 67
    • 0029025060 scopus 로고
    • Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells
    • Watarai, M., T. Tobe, M. Yoshikawa, and C. Sasakawa. 1995. Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells. Proc. Natl. Acad. Sci. USA 92:4927-4931.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4927-4931
    • Watarai, M.1    Tobe, T.2    Yoshikawa, M.3    Sasakawa, C.4
  • 68
    • 0347622754 scopus 로고    scopus 로고
    • pH-dependent catabolic protein expression during anaerobic growth of Escherichia coli K-12
    • Yohannes, E., D. M. Barnhart, and J. L. Slonczewski. 2004. pH-dependent catabolic protein expression during anaerobic growth of Escherichia coli K-12. J. Bacteriol. 186:192-199.
    • (2004) J. Bacteriol , vol.186 , pp. 192-199
    • Yohannes, E.1    Barnhart, D.M.2    Slonczewski, J.L.3
  • 69
    • 0033792965 scopus 로고    scopus 로고
    • Key role for DsbA in cell-to-cell spread of Shigella flexneri, permitting secretion of Ipa proteins into interepithelial protrusions
    • Yu, J., B. Edwards-Jones, O. Neyrolles, and J. S. Kroll. 2000. Key role for DsbA in cell-to-cell spread of Shigella flexneri, permitting secretion of Ipa proteins into interepithelial protrusions. Infect. Immun. 68:6449-6456.
    • (2000) Infect. Immun , vol.68 , pp. 6449-6456
    • Yu, J.1    Edwards-Jones, B.2    Neyrolles, O.3    Kroll, J.S.4
  • 70
    • 0032786363 scopus 로고    scopus 로고
    • DsbA: A protein-folding catalyst contributing to bacterial virulence
    • Yu, J., and J. S. Kroll. 1999. DsbA: a protein-folding catalyst contributing to bacterial virulence. Microbes Infect. 1:1221-1228.
    • (1999) Microbes Infect , vol.1 , pp. 1221-1228
    • Yu, J.1    Kroll, J.S.2
  • 71
    • 0035899893 scopus 로고    scopus 로고
    • Inactivation of DsbA alters the behaviour of Shigella flexneri towards murine and human-derived macrophage-like cells
    • Yu, J., E. E. Oragni, A. Stephens, J. S. Kroll, and M. M. Venkatesan. 2001. Inactivation of DsbA alters the behaviour of Shigella flexneri towards murine and human-derived macrophage-like cells. FEMS Microbiol. Lett. 204:81-88.
    • (2001) FEMS Microbiol. Lett , vol.204 , pp. 81-88
    • Yu, J.1    Oragni, E.E.2    Stephens, A.3    Kroll, J.S.4    Venkatesan, M.M.5
  • 72
    • 0026633141 scopus 로고
    • A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae
    • Yu, J., H. Webb, and T. R. Hirst. 1992. A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae. Mol. Microbiol. 6:1949-1958.
    • (1992) Mol. Microbiol , vol.6 , pp. 1949-1958
    • Yu, J.1    Webb, H.2    Hirst, T.R.3
  • 73
    • 0029774730 scopus 로고    scopus 로고
    • DsbA is required for stability of the type IV pilin of enteropathogenic Escherichia coli
    • Zhang, H. Z., and M. S. Donnenberg. 1996. DsbA is required for stability of the type IV pilin of enteropathogenic Escherichia coli. Mol. Microbiol. 21:787-797.
    • (1996) Mol. Microbiol , vol.21 , pp. 787-797
    • Zhang, H.Z.1    Donnenberg, M.S.2
  • 74
    • 19244362559 scopus 로고    scopus 로고
    • Granulomatous infections: Etiology and classification
    • Zumla, A., and D. G. James. 1996. Granulomatous infections: etiology and classification. Clin. Infect. Dis. 23:146-158.
    • (1996) Clin. Infect. Dis , vol.23 , pp. 146-158
    • Zumla, A.1    James, D.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.