메뉴 건너뛰기




Volumn 3, Issue 1, 2011, Pages

HtrA chaperone activity contributes to host cell binding in Campylobacter jejuni

Author keywords

Campylobacter jejuni; chaperone; HtrA; INT 407; phagocytosis; protease; virulence

Indexed keywords


EID: 84860652903     PISSN: None     EISSN: 17574749     Source Type: Journal    
DOI: 10.1186/1757-4749-3-13     Document Type: Article
Times cited : (43)

References (46)
  • 1
    • 0035870985 scopus 로고    scopus 로고
    • Campylobacter jejuni infections: Update on emerging issues and trends
    • DOI 10.1086/319760
    • Campylobacter jejuni Infections: update on emerging issues and trends. Allos BM, Clin Infect Dis 2001 32 1201 1206 10.1086/319760 11283810 (Pubitemid 32381123)
    • (2001) Clinical Infectious Diseases , vol.32 , Issue.8 , pp. 1201-1206
    • Allos, B.M.1
  • 2
    • 34548028239 scopus 로고    scopus 로고
    • Campylobacter jejuni: Molecular biology and pathogenesis
    • DOI 10.1038/nrmicro1718, PII NRMICRO1718
    • Campylobacter jejuni: molecular biology and pathogenesis. Young KT, Davis LM, Dirita VJ, NatRevMicrobiol 2007 5 665 679 (Pubitemid 47278861)
    • (2007) Nature Reviews Microbiology , vol.5 , Issue.9 , pp. 665-679
    • Young, K.T.1    Davis, L.M.2    DiRita, V.J.3
  • 3
    • 0021998499 scopus 로고
    • Campylobacter colitis: Histological immunohistochemical and ultrastructural findings
    • Campylobacter colitis: histological immunohistochemical and ultrastructural findings. van Spreeuwel JP, Duursma GC, Meijer CJ, Bax R, Rosekrans PC, Lindeman J, Gut 1985 26 945 951 10.1136/gut.26.9.945 4029720 (Pubitemid 15229645)
    • (1985) Gut , vol.26 , Issue.9 , pp. 945-951
    • Van Spreeuwel, J.P.1    Duursma, G.C.2    Meijer, C.J.L.M.3
  • 4
    • 0027287348 scopus 로고
    • Early colonic damage and invasion of Campylobacter jejuni in experimentally challenged infant Macaca mulatta
    • Early colonic damage and invasion of Campylobacter jejuni in experimentally challenged infant Macaca mulatta. Russell RG, O'Donnoghue M, Blake DC Jr, Zulty J, DeTolla LJ, J Infect Dis 1993 168 210 215 10.1093/infdis/168.1.210 8515112 (Pubitemid 23178752)
    • (1993) Journal of Infectious Diseases , vol.168 , Issue.1 , pp. 210-215
    • Russell, R.G.1    O'Donnoghue, M.2    Blake Jr., D.C.3    Zulty, J.4    DeTolla, L.J.5
  • 5
    • 0033942331 scopus 로고    scopus 로고
    • Involvement of a plasmid in virulence of Campylobacter jejuni 81-176
    • DOI 10.1128/IAI.68.8.4384-4390.2000
    • Involvement of a plasmid in virulence of Campylobacter jejuni 81-176. Bacon DJ, Alm RA, Burr DH, Hu L, Kopecko DJ, Ewing CP, Trust TJ, Guerry P, Infect Immun 2000 68 4384 4390 10.1128/IAI.68.8.4384-4390.2000 10899834 (Pubitemid 30497702)
    • (2000) Infection and Immunity , vol.68 , Issue.8 , pp. 4384-4390
    • Bacon, D.J.1    Alm, R.2    Burr, D.H.3    Hu, L.4    Kopecko, D.J.5    Ewing, C.P.6    Trust, T.J.7    Guerry, P.8
  • 6
    • 0031017405 scopus 로고    scopus 로고
    • CheY-mediated modulation of campylobacter jejuni virulence
    • CheY-mediated modulation of Campylobacter jejuni virulence. Yao R, Burr DH, Guerry P, Mol Microbiol 1997 23 1021 1031 10.1046/j.1365-2958.1997.2861650.x 9076738 (Pubitemid 27096737)
    • (1997) Molecular Microbiology , vol.23 , Issue.5 , pp. 1021-1031
    • Yao, R.1    Burr, D.H.2    Guerry, P.3
  • 7
    • 0030661833 scopus 로고    scopus 로고
    • Differential uptake and killing potential of Campylobacter jejuni by human peripheral monocytes/macrophages
    • DOI 10.1007/s004300050056
    • Differential uptake and killing potential of Campylobacter jejuni by human peripheral monocytes/macrophages. Wassenaar TM, Engelskirchen M, Park S, Lastovica A, Med Microbiol Immunol 1997 186 139 144 10.1007/s004300050056 9403842 (Pubitemid 27477882)
    • (1997) Medical Microbiology and Immunology , vol.186 , Issue.2-3 , pp. 139-144
    • Wassenaar, T.M.1    Engelskirchen, M.2    Park, S.3    Lastovica, A.4
  • 8
    • 0028073696 scopus 로고
    • Isolation of motile and non-motile insertional mutants of Campylobacter jejuni: The role of motility in adherence and invasion of eukaryotic cells
    • DOI 10.1111/j.1365-2958.1994.tb01324.x
    • Isolation of motile and non-motile insertional mutants of Campylobacter jejuni: the role of motility in adherence and invasion of eukaryotic cells. Yao R, Burr DH, Doig P, Trust TJ, Niu H, Guerry P, Mol Microbiol 1994 14 883 893 10.1111/j.1365-2958.1994.tb01324.x 7715450 (Pubitemid 24376126)
    • (1994) Molecular Microbiology , vol.14 , Issue.5 , pp. 883-893
    • Yao, R.1    Burr, D.H.2    Doig, P.3    Trust, T.J.4    Niu, H.5    Guerry, P.6
  • 9
    • 33846477198 scopus 로고    scopus 로고
    • Knockout mutagenesis of the kpsE gene of Campylobacter jejuni 81116 and its involvement in bacterium-host interactions
    • DOI 10.1111/j.1574-695X.2006.00182.x
    • Knockout mutagenesis of the kpsE gene of Campylobacter jejuni 81116 and its involvement in bacterium-host interactions. Bachtiar BM, Coloe PJ, Fry BN, FEMS Immunol Med Microbiol 2007 49 149 154 10.1111/j.1574-695X.2006.00182.x 17266722 (Pubitemid 46160597)
    • (2007) FEMS Immunology and Medical Microbiology , vol.49 , Issue.1 , pp. 149-154
    • Bachtiar, B.M.1    Coloe, P.J.2    Fry, B.N.3
  • 10
    • 0027244003 scopus 로고
    • Isolation and characterization of two Campylobacter glycine-extracted proteins that bind to HeLa cell membranes
    • Isolation and characterization of two Campylobacter glycine-extracted proteins that bind to HeLa cell membranes. Kervella M, Pages JM, Pei Z, Grollier G, Blaser MJ, Fauchere JL, Infect Immun 1993 61 3440 3448 8335374 (Pubitemid 23223437)
    • (1993) Infection and Immunity , vol.61 , Issue.8 , pp. 3440-3448
    • Kervella, M.1    Pages, J.-M.2    Pei, Z.3    Grollier, G.4    Blaser, M.J.5    Fauchere, J.-L.6
  • 11
    • 0037256265 scopus 로고    scopus 로고
    • Maximal adherence and invasion of INT 407 cells by Campylobacter jejuni requires the CadF outermembrane protein and microfilament reorganization
    • DOI 10.1099/mic.0.25820-0
    • Maximal adherence and invasion of INT 407 cells by Campylobacter jejuni requires the CadF outer-membrane protein and microfilament reorganization. Monteville MR, Yoon JE, Konkel ME, Microbiology 2003 149 153 165 10.1099/mic.0.25820-0 12576589 (Pubitemid 36175686)
    • (2003) Microbiology , vol.149 , Issue.1 , pp. 153-165
    • Monteville, M.R.1    Yoon, J.E.2    Konkel, M.E.3
  • 12
    • 73849129236 scopus 로고    scopus 로고
    • Campylobacter jejuni FlpA binds fibronectin and is required for maximal host cell adherence
    • 10.1128/JB.00969-09 19880595
    • Campylobacter jejuni FlpA binds fibronectin and is required for maximal host cell adherence. Konkel ME, Larson CL, Flanagan RC, J Bacteriol 2010 192 68 76 10.1128/JB.00969-09 19880595
    • (2010) J Bacteriol , vol.192 , pp. 68-76
    • Konkel, M.E.1    Larson, C.L.2    Flanagan, R.C.3
  • 13
    • 33947407705 scopus 로고    scopus 로고
    • CapA, an autotransporter protein of Campylobacter jejuni, mediates association with human epithelial cells and colonization of the chicken gut
    • DOI 10.1128/JB.01427-06
    • CapA, an autotransporter protein of Campylobacter jejuni, mediates association with human epithelial cells and colonization of the chicken gut. Ashgar SS, Oldfield NJ, Wooldridge KG, Jones MA, Irving GJ, Turner DP, Ala'Aldeen DA, J Bacteriol 2007 189 1856 1865 10.1128/JB.01427-06 17172331 (Pubitemid 46446148)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1856-1865
    • Ashgar, S.S.A.1    Oldfield, N.J.2    Wooldridge, K.G.3    Jones, M.A.4    Irving, G.J.5    Turner, D.P.J.6    Ala'Aldeen, D.A.A.7
  • 14
    • 0035103994 scopus 로고    scopus 로고
    • JlpA, a novel surface-exposed lipoprotein specific to Campylobacter jejuni, mediates adherence to host epithelial cells
    • DOI 10.1046/j.1365-2958.2001.02294.x
    • JlpA, a novel surface-exposed lipoprotein specific to Campylobacter jejuni, mediates adherence to host epithelial cells. Jin S, Joe A, Lynett J, Hani EK, Sherman P, Chan VL, Mol Microbiol 2001 39 1225 1236 10.1111/j.1365-2958.2001.02294.x 11251839 (Pubitemid 32225133)
    • (2001) Molecular Microbiology , vol.39 , Issue.5 , pp. 1225-1236
    • Jin, S.1    Joe, A.2    Lynett, J.3    Hani, E.K.4    Sherman, P.5    Chan, V.L.6
  • 15
    • 34548658907 scopus 로고    scopus 로고
    • Glutamyl transpeptidase has a role in the persistent colonization of the avian gut by Campylobacter jejuni
    • DOI 10.1016/j.micpath.2007.05.007, PII S0882401007000678
    • Gamma-glutamyl transpeptidase has a role in the persistent colonization of the avian gut by Campylobacter jejuni. Barnes IH, Bagnall MC, Browning DD, Thompson SA, Manning G, Newell DG, Microb Pathog 2007 43 198 207 10.1016/j.micpath.2007.05.007 17600669 (Pubitemid 47405152)
    • (2007) Microbial Pathogenesis , vol.43 , Issue.5-6 , pp. 198-207
    • Barnes, I.H.A.1    Bagnall, M.C.2    Browning, D.D.3    Thompson, S.A.4    Manning, G.5    Newell, D.G.6
  • 16
    • 77955294240 scopus 로고    scopus 로고
    • Identification of Campylobacter jejuni genes involved in its interaction with epithelial cells
    • 10.1128/IAI.00109-10 20515930
    • Identification of Campylobacter jejuni genes involved in its interaction with epithelial cells. Novik V, Hofreuter D, Galan JE, Infect Immun 2010 78 3540 3553 10.1128/IAI.00109-10 20515930
    • (2010) Infect Immun , vol.78 , pp. 3540-3553
    • Novik, V.1    Hofreuter, D.2    Galan, J.E.3
  • 17
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • DOI 10.1016/S0092-8674(00)80743-6
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Spiess C, Beil A, Ehrmann M, Cell 1999 97 339 347 10.1016/S0092-8674(00)80743-6 10319814 (Pubitemid 29214590)
    • (1999) Cell , vol.97 , Issue.3 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 18
    • 79251632433 scopus 로고    scopus 로고
    • Different Contributions of HtrA Protease and Chaperone Activities to Campylobacter jejuni Stress Tolerance and Physiology
    • 10.1128/AEM.01603-10 21075890
    • Different Contributions of HtrA Protease and Chaperone Activities to Campylobacter jejuni Stress Tolerance and Physiology. Bæk KT, Vegge CS, Skorko-Glonek J, Brondsted L, Appl Environ Microbiol 2011 77 57 66 10.1128/AEM.01603-10 21075890
    • (2011) Appl Environ Microbiol , vol.77 , pp. 57-66
    • Bæk, K.T.1    Vegge, C.S.2    Skorko-Glonek, J.3    Brondsted, L.4
  • 19
    • 0033051014 scopus 로고    scopus 로고
    • The alternative sigma factor, (E), is critically important for the virulence of Salmonella typhimurium
    • The alternative sigma factor, sigmaE, is critically important for the virulence of Salmonella typhimurium. Humphreys S, Stevenson A, Bacon A, Weinhardt AB, Roberts M, Infect Immun 1999 67 1560 1568 10084987 (Pubitemid 29144366)
    • (1999) Infection and Immunity , vol.67 , Issue.4 , pp. 1560-1568
    • Humphreys, S.1    Stevenson, A.2    Bacon, A.3    Weinhardt, A.B.4    Roberts, M.5
  • 21
    • 0036716436 scopus 로고    scopus 로고
    • Role of the htrA gene in Klebsiella pneumoniae virulence
    • 10.1128/IAI.70.9.4772-4776.2002 12183518
    • Role of the htrA gene in Klebsiella pneumoniae virulence. Cortes G, de Astorza B, Benedi VJ, Alberti S, Infect Immun 2002 70 4772 4776 10.1128/IAI.70.9.4772-4776.2002 12183518
    • (2002) Infect Immun , vol.70 , pp. 4772-4776
    • Cortes, G.1    De Astorza, B.2    Benedi, V.J.3    Alberti, S.4
  • 22
    • 0029947971 scopus 로고    scopus 로고
    • Construction and characterization of a Yersinia enterocolitica O:8 high-temperature requirement (htrA) isogenic mutant
    • 8675311
    • Construction and characterization of a Yersinia enterocolitica O:8 high-temperature requirement (htrA) isogenic mutant. Li SR, Dorrell N, Everest PH, Dougan G, Wren BW, Infect Immun 1996 64 2088 2094 8675311
    • (1996) Infect Immun , vol.64 , pp. 2088-2094
    • Li, S.R.1    Dorrell, N.2    Everest, P.H.3    Dougan, G.4    Wren, B.W.5
  • 23
    • 0029852402 scopus 로고    scopus 로고
    • Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro
    • Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro. Laskowska E, Kuczynska-wisnik D, Skorko-Glonek J, Taylor A, MolMicrobiol 1996 22 555 571 (Pubitemid 26373839)
    • (1996) Molecular Microbiology , vol.22 , Issue.3 , pp. 555-571
    • Laskowska, E.1    Kuczynska-Wisnik, D.2    Skorko-Glonek, J.3    Taylor, A.4
  • 24
    • 34447644224 scopus 로고    scopus 로고
    • Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock
    • Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock. Skorko-Glonek J, Laskowska E, Sobiecka-Szkatula A, Lipinska B, Arch Biochem Biophys 2007
    • (2007) Arch Biochem Biophys
    • Skorko-Glonek, J.1    Laskowska, E.2    Sobiecka-Szkatula, A.3    Lipinska, B.4
  • 25
    • 0024673026 scopus 로고
    • Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature
    • 2540154
    • Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature. Strauch KL, Johnson K, Beckwith J, J Bacteriol 1989 171 2689 2696 2540154
    • (1989) J Bacteriol , vol.171 , pp. 2689-2696
    • Strauch, K.L.1    Johnson, K.2    Beckwith, J.3
  • 27
    • 34547643207 scopus 로고    scopus 로고
    • IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA
    • DOI 10.1128/JB.00483-07
    • IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA. Purdy GE, Fisher CR, Payne SM, J Bacteriol 2007 189 5566 5573 10.1128/JB.00483-07 17526712 (Pubitemid 47206402)
    • (2007) Journal of Bacteriology , vol.189 , Issue.15 , pp. 5566-5573
    • Purdy, G.E.1    Fisher, C.R.2    Payne, S.M.3
  • 28
    • 0036839640 scopus 로고    scopus 로고
    • Shigella flexneri DegP facilitates IcsA surface expression and is required for efficient intercellular spread
    • DOI 10.1128/IAI.70.11.6355-6364.2002
    • Shigella flexneri DegP facilitates IcsA surface expression and is required for efficient intercellular spread. Purdy GE, Hong M, Payne SM, Infect Immun 2002 70 6355 6364 10.1128/IAI.70.11.6355-6364.2002 12379715 (Pubitemid 35192728)
    • (2002) Infection and Immunity , vol.70 , Issue.11 , pp. 6355-6364
    • Purdy, G.E.1    Hong, M.2    Payne, S.M.3
  • 29
    • 34948827356 scopus 로고    scopus 로고
    • Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
    • DOI 10.1101/gad.1581007
    • Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Sklar JG, Wu T, Kahne D, Silhavy TJ, Genes Dev 2007 21 2473 2484 10.1101/gad.1581007 17908933 (Pubitemid 47529375)
    • (2007) Genes and Development , vol.21 , Issue.19 , pp. 2473-2484
    • Sklar, J.G.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 31
    • 20444380287 scopus 로고    scopus 로고
    • The HtrA protease of Campylobacter jejuni is required for heat and oxygen tolerance and for optimal interaction with human epithelial cells
    • DOI 10.1128/AEM.71.6.3205-3212.2005
    • The HtrA protease of Campylobacter jejuni is required for heat and oxygen tolerance and for optimal interaction with human epithelial cells. Brøndsted L, Andersen MT, Parker M, Jorgensen K, Ingmer H, Appl Environ Microbiol 2005 71 3205 3212 10.1128/AEM.71.6.3205-3212.2005 15933023 (Pubitemid 40807232)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.6 , pp. 3205-3212
    • Brondsted, L.1    Andersen, M.T.2    Parker, M.3    Jorgensen, K.4    Ingmer, H.5
  • 32
    • 70350157388 scopus 로고    scopus 로고
    • Campylobacter jejuni secretes proteins via the flagellar type III secretion system that contribute to host cell invasion and gastroenteritis
    • Washington, DC: ASM Press Nachamkin I, Szymanski CM, Blaser MJ
    • Campylobacter jejuni secretes proteins via the flagellar type III secretion system that contribute to host cell invasion and gastroenteritis. Larson CL, Christensen JE, Pacheco SA, Minnich SA, Konkel ME, Campylobacter Washington, DC: ASM Press, Nachamkin I, Szymanski CM, Blaser MJ, 2008 315331
    • (2008) Campylobacter , pp. 315331
    • Larson, C.L.1    Christensen, J.E.2    Pacheco, S.A.3    Minnich, S.A.4    Konkel, M.E.5
  • 33
    • 37349055095 scopus 로고    scopus 로고
    • Contribution of conserved ATP-dependent proteases of Campylobacter jejuni to stress tolerance and virulence
    • DOI 10.1128/AEM.00698-07
    • Contribution of conserved ATP-dependent proteases of Campylobacter jejuni to stress tolerance and virulence. Cohn MT, Ingmer H, Mulholland F, Jorgensen K, Wells JM, Brondsted L, Appl Environ Microbiol 2007 73 7803 7813 10.1128/AEM.00698-07 17933920 (Pubitemid 350308795)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.24 , pp. 7803-7813
    • Cohn, M.T.1    Ingmer, H.2    Mulholland, F.3    Jorgensen, K.4    Wells, J.M.5    Brondsted, L.6
  • 34
    • 34548799195 scopus 로고    scopus 로고
    • Deletion of peb4 gene impairs cell adhesion and biofilm formation in Campylobacter jejuni
    • DOI 10.1111/j.1574-6968.2007.00893.x
    • Deletion of peb4 gene impairs cell adhesion and biofilm formation in Campylobacter jejuni. Asakura H, Yamasaki M, Yamamoto S, Igimi S, FEMS Microbiol Lett 2007 275 278 285 10.1111/j.1574-6968.2007.00893.x 17714477 (Pubitemid 47437862)
    • (2007) FEMS Microbiology Letters , vol.275 , Issue.2 , pp. 278-285
    • Asakura, H.1    Yamasaki, M.2    Yamamoto, S.3    Igimi, S.4
  • 35
    • 33748307473 scopus 로고    scopus 로고
    • Novel surface polypeptides of Campylobacter jejuni as traveller's diarrhoea vaccine candidates discovered by proteomics
    • DOI 10.1016/j.vaccine.2006.05.085, PII S0264410X06006736
    • Novel surface polypeptides of Campylobacter jejuni as traveller's diarrhoea vaccine candidates discovered by proteomics. Prokhorova TA, Nielsen PN, Petersen J, Kofoed T, Crawford JS, Morsczeck C, Boysen A, Schrotz-King P, Vaccine 2006 24 6446 6455 10.1016/j.vaccine.2006.05.085 16824653 (Pubitemid 44331993)
    • (2006) Vaccine , vol.24 , Issue.40-41 , pp. 6446-6455
    • Prokhorova, T.A.1    Nielsen, P.N.2    Petersen, J.3    Kofoed, T.4    Crawford, J.S.5    Morsczeck, C.6    Boysen, A.7    Schrotz-King, P.8
  • 36
    • 0016651969 scopus 로고
    • Superficial antigens of Campylobacter (Vibrio) fetus: Characterization of antiphagocytic component
    • 46843
    • Superficial antigens of Campylobacter (Vibrio) fetus: characterization of antiphagocytic component. McCoy EC, Doyle D, Burda K, Corbeil LB, Winter AJ, Infect Immun 1975 11 517 525 46843
    • (1975) Infect Immun , vol.11 , pp. 517-525
    • McCoy, E.C.1    Doyle, D.2    Burda, K.3    Corbeil, L.B.4    Winter, A.J.5
  • 37
    • 0021027902 scopus 로고
    • Molecular identification of surface protein antigens of Campylobacter jejuni
    • Molecular identification of surface protein antigens of Campylobacter jejuni. Logan SM, Trust TJ, Infect Immun 1983 42 675 682 6642648 (Pubitemid 14230264)
    • (1983) Infection and Immunity , vol.42 , Issue.2 , pp. 675-682
    • Logan, S.M.1    Trust, T.J.2
  • 38
    • 0025312883 scopus 로고
    • Identification of Campylobacter jejuni surface proteins that bind to eucaryotic cells in vitro
    • Identification of Campylobacter jejuni surface proteins that bind to Eucaryotic cells in vitro. de Melo MA, Pechere JC, Infect Immun 1990 58 1749 1756 2160431 (Pubitemid 20176366)
    • (1990) Infection and Immunity , vol.58 , Issue.6 , pp. 1749-1756
    • De Melo, M.A.1    Pechere, J.-C.2
  • 40
    • 70350470007 scopus 로고    scopus 로고
    • Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae
    • 10.1128/JB.00754-09 19734313
    • Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae. Ruiz-Perez F, Henderson IR, Leyton DL, Rossiter AE, Zhang Y, Nataro JP, J Bacteriol 2009 191 6571 6583 10.1128/JB.00754-09 19734313
    • (2009) J Bacteriol , vol.191 , pp. 6571-6583
    • Ruiz-Perez, F.1    Henderson, I.R.2    Leyton, D.L.3    Rossiter, A.E.4    Zhang, Y.5    Nataro, J.P.6
  • 41
    • 0036127088 scopus 로고    scopus 로고
    • Campylobacter protein glycosylation affects host cell interactions
    • DOI 10.1128/IAI.70.4.2242-2244.2002
    • Campylobacter protein glycosylation affects host cell interactions. Szymanski CM, Burr DH, Guerry P, Infect Immun 2002 70 2242 2244 10.1128/IAI.70.4.2242-2244.2002 11895996 (Pubitemid 34242232)
    • (2002) Infection and Immunity , vol.70 , Issue.4 , pp. 2242-2244
    • Szymanski, C.M.1    Burr, D.H.2    Guerry, P.3
  • 42
    • 77954594416 scopus 로고    scopus 로고
    • Modification of the Campylobacter jejuni flagellin glycan by the product of the Cj1295 homopolymeric-tract-containing gene
    • 10.1099/mic.0.038091-0 20338909
    • Modification of the Campylobacter jejuni flagellin glycan by the product of the Cj1295 homopolymeric-tract-containing gene. Hitchen P, Brzostek J, Panico M, Butler JA, Morris HR, Dell A, Linton D, Microbiology 2010 156 1953 1962 10.1099/mic.0.038091-0 20338909
    • (2010) Microbiology , vol.156 , pp. 1953-1962
    • Hitchen, P.1    Brzostek, J.2    Panico, M.3    Butler, J.A.4    Morris, H.R.5    Dell, A.6    Linton, D.7
  • 43
    • 0026492055 scopus 로고
    • Altered synthetic response of Campylobacter jejuni to cocultivation with human epithelial cells is associated with enhanced internalization
    • Altered synthetic response of Campylobacter jejuni to cocultivation with human epithelial cells is associated with enhanced internalization. Konkel ME, Cieplak W Jr, InfectImmun 1992 60 4945 4949
    • (1992) InfectImmun , vol.60 , pp. 4945-4949
    • Konkel, M.E.1    Cieplak Jr., W.2
  • 44
    • 0033016809 scopus 로고    scopus 로고
    • Bacterial secreted proteins are required for the internalization of Campylobacter jejuni into cultured mammalian cells
    • DOI 10.1046/j.1365-2958.1999.01376.x
    • Bacterial secreted proteins are required for the internaliztion of Campylobacter jejuni into cultured mammalian cells. Konkel ME, Kim BJ, Rivera-amill V, Garvis SG, MolMicrobiol 1999 32 691 701 (Pubitemid 29241511)
    • (1999) Molecular Microbiology , vol.32 , Issue.4 , pp. 691-701
    • Konkel, M.E.1    Kim, B.J.2    Rivera-Amill, V.3    Garvis, S.G.4
  • 45
    • 41549097842 scopus 로고    scopus 로고
    • Culture of Campylobacter jejuni with sodium deoxycholate induces virulence gene expression
    • DOI 10.1128/JB.01736-07
    • Culture of Campylobacter jejuni with sodium deoxycholate induces virulence gene expression. Malik-Kale P, Parker CT, Konkel ME, J Bacteriol 2008 190 2286 2297 10.1128/JB.01736-07 18223090 (Pubitemid 351466323)
    • (2008) Journal of Bacteriology , vol.190 , Issue.7 , pp. 2286-2297
    • Malik-Kale, P.1    Parker, C.T.2    Konkel, M.E.3
  • 46
    • 0025911942 scopus 로고
    • Inactivation of Campylobacter jejuni flagellin genes by homologous recombination demonstrates that flaA but not flaB is required for invasion
    • Inactivation of Campylobacter jejuni flagellin genes by homologous recombination demonstrates that flaA but not flaB is required for invasion. Wassenaar TM, Bleumink-Pluym NM, van der Zeijst BA, EMBO J 1991 10 2055 2061 2065653 (Pubitemid 21905676)
    • (1991) EMBO Journal , vol.10 , Issue.8 , pp. 2055-2061
    • Wassenaar, T.M.1    Bleumink-Pluym, N.M.C.2    Van Der Zeijst, B.A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.