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Volumn 80, Issue 12, 2012, Pages 4089-4098

Campylobacter jejuni outer membrane vesicles play an important role in bacterial interactions with human intestinal epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

CYTOLETHAL DISTENDING TOXIN; GLYCOPROTEIN; INTERLEUKIN 8; METHYL BETA CYCLODEXTRIN; OUTER MEMBRANE PROTEIN; PERIPLASMIC PROTEIN; POLYMYXIN B; PROTEINASE K;

EID: 84870828377     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00161-12     Document Type: Article
Times cited : (134)

References (77)
  • 1
    • 0035424901 scopus 로고    scopus 로고
    • Decreased expression of Toll-like receptor-4 and MD-2 correlates with intestinal epithelial cell protection against dysregu-lated proinflammatory gene expression in response to bacterial lipopoly-saccharide
    • Abreu MT, et al. 2001. Decreased expression of Toll-like receptor-4 and MD-2 correlates with intestinal epithelial cell protection against dysregu-lated proinflammatory gene expression in response to bacterial lipopoly-saccharide. J. Immunol. 167:1609-1616.
    • (2001) J. Immunol. , vol.167 , pp. 1609-1616
    • Abreu, M.T.1
  • 2
    • 0035870985 scopus 로고    scopus 로고
    • Campylobacter jejuni infections: update on emerging issues and trends
    • Allos BM. 2001. Campylobacter jejuni infections: update on emerging issues and trends. Clin. Infect. Dis. 32:1201-1206.
    • (2001) Clin. Infect. Dis. , vol.32 , pp. 1201-1206
    • Allos, B.M.1
  • 3
  • 4
    • 84860652903 scopus 로고    scopus 로고
    • HtrA chaperone activity contributesto host cell binding in Campylobacter jejuni
    • doi:10.1186/1757-4749-3-13
    • Baek KT, Vegge CS, Brondsted L. 2011. HtrA chaperone activity contributes
    • (2011) Gut Pathog , vol.3 , pp. 13
    • Baek, K.T.1    Vegge, C.S.2    Brondsted, L.3
  • 5
    • 33745914259 scopus 로고    scopus 로고
    • Ultra-fast tandem mass spectrometry scanning combined with monolithic column liquid chromatography increases throughput in proteomic analysis
    • Batycka M, et al. 2006. Ultra-fast tandem mass spectrometry scanning combined with monolithic column liquid chromatography increases throughput in proteomic analysis. Rapid Commun. Mass Spectrom. 20: 2074-2080.
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 2074-2080
    • Batycka, M.1
  • 6
    • 33749353869 scopus 로고    scopus 로고
    • Purification of outer membrane vesicles from Pseudomonas aeruginosa and their activation of an IL-8 response
    • Bauman SJ, Kuehn MJ. 2006. Purification of outer membrane vesicles from Pseudomonas aeruginosa and their activation of an IL-8 response. Microbes Infect. 8:2400-2408.
    • (2006) Microbes Infect. , vol.8 , pp. 2400-2408
    • Bauman, S.J.1    Kuehn, M.J.2
  • 9
    • 84864681437 scopus 로고    scopus 로고
    • Rapid paracellular transmigration of Campylobac-ter jejuni across polarized epithelial cells without affecting TER: role of proteolytic-active HtrA cleaving E-cadherin but not fibronectin
    • doi:10.1186/1757-4749-4-3
    • Boehm M, et al. 2012. Rapid paracellular transmigration of Campylobac-ter jejuni across polarized epithelial cells without affecting TER: role of proteolytic-active HtrA cleaving E-cadherin but not fibronectin. Gut Pat-hog. 4:3. doi:10.1186/1757-4749-4-3.
    • (2012) Gut Pat-hog , vol.4 , pp. 3
    • Boehm, M.1
  • 10
    • 66349107694 scopus 로고    scopus 로고
    • Long-distance delivery of bacterial virulence factors by Pseudomonas aeruginosa outer membrane vesicles
    • doi:10.1371/journal.ppat.1000382
    • Bomberger JM, et al. 2009. Long-distance delivery of bacterial virulence factors by Pseudomonas aeruginosa outer membrane vesicles. PLoS Pat-hog. 5:e1000382. doi:10.1371/journal.ppat.1000382.
    • (2009) PLoS Pat-hog , vol.5 , pp. 1000382
    • Bomberger, J.M.1
  • 11
    • 79957464852 scopus 로고    scopus 로고
    • Campylobacter jejuni survival within human epithelial cells is enhanced by the secreted protein CiaI
    • Buelow DR, Christensen JE, Neal-McKinney JM, Konkel ME. 2011. Campylobacter jejuni survival within human epithelial cells is enhanced by the secreted protein CiaI. Mol. Microbiol. 80:1296-1312.
    • (2011) Mol. Microbiol. , vol.80 , pp. 1296-1312
    • Buelow, D.R.1    Christensen, J.E.2    Neal-mckinney, J.M.3    Konkel, M.E.4
  • 12
    • 66849134757 scopus 로고    scopus 로고
    • Galleria mellonella as an alternative infection model for Yersinia pseudotuberculosis
    • Champion OL, et al. 2009. Galleria mellonella as an alternative infection model for Yersinia pseudotuberculosis. Microbiology 155:1516-1522.
    • (2009) Microbiology , vol.155 , pp. 1516-1522
    • Champion, O.L.1
  • 13
    • 76449093065 scopus 로고    scopus 로고
    • Insect infection model for Campylobacter jejuni reveals that O-methyl phosphoramidate has insecticidal activity
    • Champion OL, et al. 2010. Insect infection model for Campylobacter jejuni reveals that O-methyl phosphoramidate has insecticidal activity. J. Infect. Dis. 201:776-782.
    • (2010) J. Infect. Dis. , vol.201 , pp. 776-782
    • Champion, O.L.1
  • 14
    • 33845477453 scopus 로고    scopus 로고
    • Disruption of tight junctions and induction of proinflammatory cytokine responses in colonic epithelial cells by Campylobacter jejuni
    • Chen ML, Ge Z, Fox JG, Schauer DB. 2006. Disruption of tight junctions and induction of proinflammatory cytokine responses in colonic epithelial cells by Campylobacter jejuni. Infect. Immun. 74:6581-6589.
    • (2006) Infect. Immun. , vol.74 , pp. 6581-6589
    • Chen, M.L.1    Ge, Z.2    Fox, J.G.3    Schauer, D.B.4
  • 15
    • 70350181746 scopus 로고    scopus 로고
    • Identification of a Cam-pylobacter jejuni-secreted protein required for maximal invasion of host cells
    • Christensen JE, Pacheco SA, Konkel ME. 2009. Identification of a Cam-pylobacter jejuni-secreted protein required for maximal invasion of host cells. Mol. Microbiol. 73:650-662.
    • (2009) Mol. Microbiol. , vol.73 , pp. 650-662
    • Christensen, J.E.1    Pacheco, S.A.2    Konkel, M.E.3
  • 16
    • 66949180763 scopus 로고    scopus 로고
    • Biogenesis of bacterial membrane vesicles
    • Deatherage BL, et al. 2009. Biogenesis of bacterial membrane vesicles. Mol. Microbiol. 72:1395-1407.
    • (2009) Mol. Microbiol. , vol.72 , pp. 1395-1407
    • Deatherage, B.L.1
  • 17
    • 77956303574 scopus 로고    scopus 로고
    • Helicobacter pylori-induced histone modification, associated gene expression in gastric epithelial cells, and its implication in pathogenesis
    • doi:10.1371/journal.pone.0009875
    • Ding SZ, et al. 2010. Helicobacter pylori-induced histone modification, associated gene expression in gastric epithelial cells, and its implication in pathogenesis. PLoS One 5:e9875. doi:10.1371/journal.pone.0009875.
    • (2010) PLoS One , vol.5 , pp. 9875
    • Ding, S.Z.1
  • 18
    • 34548458056 scopus 로고    scopus 로고
    • The second century of Campylobacter research:recent advances, new opportunities and old problems
    • Dorrell N, Wren BW. 2007. The second century of Campylobacter research:
    • (2007) Curr. Opin. Infect. Dis. , vol.20 , pp. 514-518
    • Dorrell, N.1    Wren, B.W.2
  • 19
    • 77749309281 scopus 로고    scopus 로고
    • Virulence and immunomodulatory roles of bacterial outer membrane vesicles
    • Ellis TN, Kuehn MJ. 2010. Virulence and immunomodulatory roles of bacterial outer membrane vesicles. Microbiol. Mol. Biol. Rev. 74:81-94.
    • (2010) Microbiol. Mol. Biol. Rev. , vol.74 , pp. 81-94
    • Ellis, T.N.1    Kuehn, M.J.2
  • 20
    • 79551485538 scopus 로고    scopus 로고
    • Production of secretory and extracellular N-linked glycoproteins in Escherichia coli
    • Fisher AC, et al. 2011. Production of secretory and extracellular N-linked glycoproteins in Escherichia coli. Appl. Environ. Microbiol. 77:871-881.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 871-881
    • Fisher, A.C.1
  • 22
    • 63149161192 scopus 로고    scopus 로고
    • Campylobacter jejuni drives MyD88-independent interleukin-6 secretion via Toll-like receptor 2
    • Friis LM, Keelan M, Taylor DE. 2009. Campylobacter jejuni drives MyD88-independent interleukin-6 secretion via Toll-like receptor 2. Infect. Immun. 77:1553-1560.
    • (2009) Infect. Immun , vol.77 , pp. 1553-1560
    • Friis, L.M.1    Keelan, M.2    Taylor, D.E.3
  • 23
    • 77956289822 scopus 로고    scopus 로고
    • Genetic modulation of TLR8 response following bacterial phagocytosis
    • Gantier MP, et al. 2010. Genetic modulation of TLR8 response following bacterial phagocytosis. Hum. Mutat. 31:1069-1079.
    • (2010) Hum. Mutat. , vol.31 , pp. 1069-1079
    • Gantier, M.P.1
  • 24
    • 47549092184 scopus 로고    scopus 로고
    • In vivo virulence properties of bacterial cytolethal-distending toxin
    • Ge Z, Schauer DB, Fox JG. 2008. In vivo virulence properties of bacterial cytolethal-distending toxin. Cell. Microbiol. 10:1599-1607.
    • (2008) Cell. Microbiol. , vol.10 , pp. 1599-1607
    • Ge, Z.1    Schauer, D.B.2    Fox, J.G.3
  • 25
    • 77954332543 scopus 로고    scopus 로고
    • The innate immune molecule, NOD1, regulates direct killing of Helicobacter pylori by antimicrobial peptides
    • Grubman A, et al. 2010. The innate immune molecule, NOD1, regulates direct killing of Helicobacter pylori by antimicrobial peptides. Cell. Micro-biol. 12:626-639.
    • (2010) Cell. Micro-biol. , vol.12 , pp. 626-639
    • Grubman, A.1
  • 26
    • 79961151311 scopus 로고    scopus 로고
    • The Campylobacter jejuni transcriptional regulator Cj1556 plays a role in the oxidative and aerobic stress response and is important for bacterial survival in vivo
    • Gundogdu O, et al. 2011. The Campylobacter jejuni transcriptional regulator Cj1556 plays a role in the oxidative and aerobic stress response and is important for bacterial survival in vivo. J. Bacteriol. 193:4238-4249.
    • (2011) J. Bacteriol. , vol.193 , pp. 4238-4249
    • Gundogdu, O.1
  • 27
    • 0037219984 scopus 로고    scopus 로고
    • Campylobacter jejuni cytolethal distending toxin promotes DNA repair responses in normal human cells
    • Hassane DC, Lee RB, Pickett CL. 2003. Campylobacter jejuni cytolethal distending toxin promotes DNA repair responses in normal human cells. Infect. Immun. 71:541-545.
    • (2003) Infect. Immun. , vol.71 , pp. 541-545
    • Hassane, D.C.1    Lee, R.B.2    Pickett, C.L.3
  • 28
    • 78651393562 scopus 로고    scopus 로고
    • Selective sorting of cargo proteins into bacterial membrane vesicles
    • Haurat MF, et al. 2011. Selective sorting of cargo proteins into bacterial membrane vesicles. J. Biol. Chem. 286:1269-1276.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1269-1276
    • Haurat, M.F.1
  • 30
    • 0034444893 scopus 로고    scopus 로고
    • Campylobacter jejuni cytolethal distending toxin mediates release of interleukin-8 from intestinal epithelial cells
    • Hickey TE, et al. 2000. Campylobacter jejuni cytolethal distending toxin mediates release of interleukin-8 from intestinal epithelial cells. Infect. Immun. 68:6535-6541.
    • (2000) Infect. Immun. , vol.68 , pp. 6535-6541
    • Hickey, T.E.1
  • 31
    • 23344435789 scopus 로고    scopus 로고
    • Intracellular survival of Campy-lobacter jejuni in human monocytic cells and induction of apoptotic death by cytolethal distending toxin
    • Hickey TE, Majam G, Guerry P. 2005. Intracellular survival of Campy-lobacter jejuni in human monocytic cells and induction of apoptotic death by cytolethal distending toxin. Infect. Immun. 73:5194-5197.
    • (2005) Infect Immun. , vol.73 , pp. 5194-5197
    • Hickey, T.E.1    Majam, G.2    Guerry, P.3
  • 32
    • 78049434748 scopus 로고    scopus 로고
    • Helicobacter pylori exploits cholesterol-rich mi-crodomains for induction of NF-kappaB-dependent responses and pep-tidoglycan delivery in epithelial cells
    • Hutton ML, et al. 2010. Helicobacter pylori exploits cholesterol-rich mi-crodomains for induction of NF-kappaB-dependent responses and pep-tidoglycan delivery in epithelial cells. Infect. Immun. 78:4523-4531.
    • (2010) Infect. Immun. , vol.78 , pp. 4523-4531
    • Hutton, M.L.1
  • 33
    • 0141780971 scopus 로고    scopus 로고
    • Helicobacter pylori outer membrane vesicles modulate proliferation and interleukin-8 production by gastric epithelial cells
    • Ismail S, Hampton MB, Keenan JI. 2003. Helicobacter pylori outer membrane vesicles modulate proliferation and interleukin-8 production by gastric epithelial cells. Infect. Immun. 71:5670-5675.
    • (2003) Infect. Immun. , vol.71 , pp. 5670-5675
    • Ismail, S.1    Hampton, M.B.2    Keenan, J.I.3
  • 34
    • 47949123705 scopus 로고    scopus 로고
    • Host-pathogen interactions in Campylobacter infections: the host perspective
    • Janssen R, et al. 2008. Host-pathogen interactions in Campylobacter infections: the host perspective. Clin. Microbiol. Rev. 21:505-518.
    • (2008) Clin. Microbiol. Rev. , vol.21 , pp. 505-518
    • Janssen, R.1
  • 35
    • 3042544332 scopus 로고    scopus 로고
    • Adaptation of Campylobacter jejuni NCTC11168 to high-level colonization of the avian gastrointestinal tract
    • Jones MA, et al. 2004. Adaptation of Campylobacter jejuni NCTC11168 to high-level colonization of the avian gastrointestinal tract. Infect. Immun. 72:3769-3776.
    • (2004) Infect. Immun. , vol.72 , pp. 3769-3776
    • Jones, M.A.1
  • 36
    • 0041341888 scopus 로고    scopus 로고
    • Prediction of lipoprotein signal peptides in Gram-negative bacteria
    • Juncker AS, et al. 2003. Prediction of lipoprotein signal peptides in Gram-negative bacteria. Protein Sci. 12:1652-1662
    • (2003) Protein Sci. , vol.12 , pp. 1652-1662
    • Juncker, A.S.1
  • 37
    • 77950621399 scopus 로고    scopus 로고
    • Bacterial membrane vesicles deliver peptidogly-can to NOD1 in epithelial cells
    • Kaparakis M, et al. 2010. Bacterial membrane vesicles deliver peptidogly-can to NOD1 in epithelial cells. Cell. Microbiol. 12:372-385.
    • (2010) Cell. Microbiol. , vol.12 , pp. 372-385
    • Kaparakis, M.1
  • 38
    • 0034861129 scopus 로고    scopus 로고
    • Demonstration of polysaccharide capsule in Campylobacter jejuni using electron microscopy
    • Karlyshev AV, McCrossan MV, Wren BW. 2001. Demonstration of polysaccharide capsule in Campylobacter jejuni using electron microscopy.
    • (2001) Infect. Immun. , vol.69 , pp. 5921-5924
    • Karlyshev, A.V.1    Mccrossan, M.V.2    Wren, B.W.3
  • 39
    • 0346457133 scopus 로고    scopus 로고
    • Incorporation of heterologous outer membrane and periplasmic proteins into Escherichia coli outer membrane vesicles
    • Kesty NC, Kuehn MJ. 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
  • 40
    • 10644226878 scopus 로고    scopus 로고
    • Entero-toxigenic Escherichia coli vesicles target toxin delivery into mammalian cells
    • Kesty NC, Mason KM, Reedy M, Miller SE, Kuehn MJ. 2004. Entero-toxigenic 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
  • 41
    • 0037394609 scopus 로고    scopus 로고
    • Insecticidal activity associated with the outer membrane vesicles of Xenorhabdus nematophilus
    • Khandelwal P, Banerjee-Bhatnagar N. 2003. Insecticidal activity associated with the outer membrane vesicles of Xenorhabdus nematophilus. Appl. Environ. Microbiol. 69:2032-2037.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2032-2037
    • Khandelwal, P.1    Banerjee-bhatnagar, N.2
  • 42
    • 0033016809 scopus 로고    scopus 로고
    • Bacterial secreted proteins are required for the internalization of Campylobacter jejuni into cultured mammalian cells
    • Konkel ME, Kim BJ, Rivera-Amill V, Garvis SG. 1999. Bacterial secreted proteins are required for the internalization of Campylobacter jejuni into cultured mammalian cells. Mol. Microbiol. 32:691-701.
    • (1999) Mol. Microbiol. , vol.32 , pp. 691-701
    • Konkel, M.E.1    Kim, B.J.2    Rivera-amill, V.3    Garvis, S.G.4
  • 43
    • 2442705402 scopus 로고    scopus 로고
    • Secretion of virulence proteins from Campylo-bacter jejuni is dependent on a functional flagellar export apparatus
    • Konkel ME, et al. 2004. Secretion of virulence proteins from Campylo-bacter jejuni is dependent on a functional flagellar export apparatus. J. Bacteriol. 186:3296-3303.
    • (2004) J. Bacteriol. , vol.186 , pp. 3296-3303
    • Konkel, M.E.1
  • 44
    • 23744505064 scopus 로고    scopus 로고
    • Identification of a fibronectin-binding domain within the Campylobacter jejuni CadF protein
    • Konkel ME, et al. 2005. Identification of a fibronectin-binding domain within the Campylobacter jejuni CadF protein. Mol. Microbiol. 57:1022-1035.
    • (2005) Mol. Microbiol. , vol.57 , pp. 1022-1035
    • Konkel, M.E.1
  • 45
    • 73849129236 scopus 로고    scopus 로고
    • Campylobacter jejuni FlpA binds fibronectin and is required for maximal host cell adherence
    • Konkel ME, Larson CL, Flanagan RC. 2010. Campylobacter jejuni FlpA binds fibronectin and is required for maximal host cell adherence. J. Bac-teriol. 192:68-76.
    • (2010) J. Bac-teriol. , vol.192 , pp. 68-76
    • Konkel, M.E.1    Larson, C.L.2    Flanagan, R.C.3
  • 46
    • 27744480818 scopus 로고    scopus 로고
    • Bacterial outer membrane vesicles and the host-pathogen interaction
    • Kuehn MJ, Kesty NC. 2005. Bacterial outer membrane vesicles and the host-pathogen interaction. Genes Dev. 19:2645-2655.
    • (2005) Genes Dev. , vol.19 , pp. 2645-2655
    • Kuehn, M.J.1    Kesty, N.C.2
  • 47
    • 77957959533 scopus 로고    scopus 로고
    • Biological functions and biogenesis of secreted bacterial outer membrane vesicles
    • Kulp A, Kuehn MJ. 2010. Biological functions and biogenesis of secreted bacterial outer membrane vesicles. Annu. Rev. Microbiol. 64:163-184.
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 163-184
    • Kulp, A.1    Kuehn, M.J.2
  • 48
    • 0034967972 scopus 로고    scopus 로고
    • CdtA, CdtB, and CdtC form a tripartite complex that is required for cytolethal distending toxin activity
    • Lara-Tejero M, Galan JE. 2001. CdtA, CdtB, and CdtC form a tripartite complex that is required for cytolethal distending toxin activity. Infect. Immun. 69:4358-4365.
    • (2001) Infect. Immun. , vol.69 , pp. 4358-4365
    • Lara-tejero, M.1    Galan, J.E.2
  • 49
    • 70449381000 scopus 로고    scopus 로고
    • Outer membrane vesicle-mediated release of cytolethal distending toxin (CDT) from Campylobacter jejuni
    • doi:10.1186/1471-2180-9-220
    • Lindmark B, et al. 2009. Outer membrane vesicle-mediated release of cytolethal distending toxin (CDT) from Campylobacter jejuni. BMC Mi-crobiol. 9:220. doi:10.1186/1471-2180-9-220.
    • (2009) BMC Mi-crobiol. , vol.9 , pp. 220
    • Lindmark, B.1
  • 50
    • 0036173114 scopus 로고    scopus 로고
    • Identification of N-acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni
    • Linton D, Allan E, Karlyshev AV, Cronshaw AD, Wren BW. 2002. Identification of N-acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni. Mol. Microbiol. 43:497-508.
    • (2002) Mol. Microbiol. , vol.43 , pp. 497-508
    • Linton, D.1    Allan, E.2    Karlyshev, A.V.3    Cronshaw, A.D.4    Wren, B.W.5
  • 51
    • 20244371925 scopus 로고    scopus 로고
    • Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway
    • Linton D, et al. 2005. Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway. Mol. Microbiol. 55:1695-1703.
    • (2005) Mol. Microbiol. , vol.55 , pp. 1695-1703
    • Linton, D.1
  • 52
    • 0020333257 scopus 로고
    • Outer membrane characteristics of Campylo-bacter jejuni
    • Logan SM, Trust TJ. 1982. Outer membrane characteristics of Campylo-bacter jejuni. Infect. Immun. 38:898-906.
    • (1982) Infect. Immun. , vol.38 , pp. 898-906
    • Logan, S.M.1    Trust, T.J.2
  • 53
    • 33845969857 scopus 로고    scopus 로고
    • Campylobacter jejuni-infected human epithelial cell lines vary in their ability to secrete interleukin-8 compared to in vitro-infected primary human intestinal tissue
    • MacCallum AJ, Harris D, Haddock G, Everest PH. 2006. Campylobacter jejuni-infected human epithelial cell lines vary in their ability to secrete interleukin-8 compared to in vitro-infected primary human intestinal tissue. Microbiology 152:3661-3665.
    • (2006) Microbiology , vol.152 , pp. 3661-3665
    • Maccallum, A.J.1    Harris, D.2    Haddock, G.3    Everest, P.H.4
  • 54
    • 44349184252 scopus 로고    scopus 로고
    • Gram-negative outer membrane vesicles: beyond the cell surface
    • Mashburn-Warren L, McLean RJ, Whiteley M. 2008. Gram-negative outer membrane vesicles: beyond the cell surface. Geobiology 6:214-219.
    • (2008) Geobiology , vol.6 , pp. 214-219
    • Mashburn-warren, L.1    Mclean, R.J.2    Whiteley, M.3
  • 55
    • 65249146047 scopus 로고    scopus 로고
    • Specificity of Campylobacter jejuni adhesin PEB3 for phosphates and structural differences among its ligand complexes
    • Min T, et al. 2009. Specificity of Campylobacter jejuni adhesin PEB3 for phosphates and structural differences among its ligand complexes. Biochemistry 48:3057-3067.
    • (2009) Biochemistry , vol.48 , pp. 3057-3067
    • Min, T.1
  • 56
    • 79551682373 scopus 로고    scopus 로고
    • Expression and characterization of cell-signalling molecules in Campylobacter jejuni
    • Moorhead SM, Griffiths MW. 2011. Expression and characterization of cell-signalling molecules in Campylobacter jejuni. J. Appl. Microbiol. 110: 786-800.
    • (2011) J. Appl. Microbiol. , vol.110 , pp. 786-800
    • Moorhead, S.M.1    Griffiths, M.W.2
  • 57
    • 0031852829 scopus 로고    scopus 로고
    • Campylobacter species and Guil-lain-Barre syndrome
    • Nachamkin I, Allos BM, Ho T. 1998. Campylobacter species and Guil-lain-Barre syndrome. Clin. Microbiol. Rev. 11:555-567.
    • (1998) Clin. Microbiol. Rev. , vol.11 , pp. 555-567
    • Nachamkin, I.1    Allos, B.M.2    Ho, T.3
  • 58
    • 77955294240 scopus 로고    scopus 로고
    • Identification of Campylobacter jejuni genes involved in its interaction with epithelial cells
    • Novik V, Hofreuter D, Galan JE. 2010. Identification of Campylobacter jejuni genes involved in its interaction with epithelial cells. Infect. Immun. 78:3540-3553.
    • (2010) Infect. Immun. , vol.78 , pp. 3540-3553
    • Novik, V.1    Hofreuter, D.2    Galan, J.E.3
  • 59
    • 1842453218 scopus 로고    scopus 로고
    • Defensin-mediated innate immunity in the small intestine
    • Ouellette AJ. 2004. Defensin-mediated innate immunity in the small intestine. Best Pract. Res. Clin. Gastroenterol. 18:405-419.
    • (2004) Best Pract. Res. Clin. Gastroenterol. , vol.18 , pp. 405-419
    • Ouellette, A.J.1
  • 60
    • 0034628526 scopus 로고    scopus 로고
    • The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences
    • Parkhill J, et al. 2000. The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences. Nature 403:665-668.
    • (2000) Nature , vol.403 , pp. 665-668
    • Parkhill, J.1
  • 61
    • 0025994829 scopus 로고
    • Identification, purification, and characterization of major antigenic proteins of Campylobacter jejuni
    • Pei ZH, Ellison RT III, Blaser MJ. 1991. Identification, purification, and characterization of major antigenic proteins of Campylobacter jejuni. J. Biol. Chem. 266:16363-16369.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16363-16369
    • Pei, Z.H.1    Ellison, R.T.2    Blaser, M.J.3
  • 62
    • 34547617364 scopus 로고    scopus 로고
    • Heterogeneity of a Campylobacter jejuni protein that is secreted through the flagellar filament
    • Poly F, et al. 2007. Heterogeneity of a Campylobacter jejuni protein that is secreted through the flagellar filament. Infect. Immun. 75:3859-3867.
    • (2007) Infect. Immun. , vol.75 , pp. 3859-3867
    • Poly, F.1
  • 63
    • 54849435016 scopus 로고    scopus 로고
    • Dendritic cells from C57BL/6 mice undergo activation and induce Th1-effector cell responses against Campylobacter jejuni
    • Rathinam VA, Hoag KA, Mansfield LS. 2008. Dendritic cells from C57BL/6 mice undergo activation and induce Th1-effector cell responses against Campylobacter jejuni. Microbes Infect. 10:1316-1324.
    • (2008) Microbes Infect. , vol.10 , pp. 1316-1324
    • Rathinam, V.A.1    Hoag, K.A.2    Mansfield, L.S.3
  • 64
    • 41149091707 scopus 로고    scopus 로고
    • Campylobacter and IFNgamma interact to cause a rapid loss of epithelial barrier integrity
    • Rees LE, et al. 2008. Campylobacter and IFNgamma interact to cause a rapid loss of epithelial barrier integrity. Inflamm. Bowel Dis. 14:303-309.
    • (2008) Inflamm. Bowel Dis. , vol.14 , pp. 303-309
    • Rees, L.E.1
  • 65
    • 79953174969 scopus 로고    scopus 로고
    • Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni
    • M000031-MCP201. doi:10.1074/ mcp. M000031-MCP201
    • Scott NE, et al. 2011. Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni. Mol. Cell. Proteomics 10(2):M000031-MCP201. doi:10.1074/ mcp. M000031-MCP201.
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.2
    • Scott, N.E.1
  • 66
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M. 1996. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68:850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 67
    • 33845222309 scopus 로고    scopus 로고
    • The contribution of cytolethal distending toxin to bacterial pathogenesis
    • Smith JL, Bayles DO. 2006. The contribution of cytolethal distending toxin to bacterial pathogenesis. Crit. Rev. Microbiol. 32:227-248.
    • (2006) Crit. Rev. Microbiol. , vol.32 , pp. 227-248
    • Smith, J.L.1    Bayles, D.O.2
  • 68
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • Szymanski CM, Yao R, Ewing CP, Trust TJ, Guerry P. 1999. Evidence for a system of general protein glycosylation in Campylobacter jejuni. Mol. Microbiol. 32:1022-1030.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1022-1030
    • Szymanski, C.M.1    Yao, R.2    Ewing, C.P.3    Trust, T.J.4    Guerry, P.5
  • 70
    • 0042902833 scopus 로고    scopus 로고
    • The COG database: an updated version includes eukaryotes
    • doi:10.1186/1471-2105-4-41
    • Tatusov RL, et al. 2003. The COG database: an updated version includes eukaryotes. BMC Bioinformatics 4:41. doi:10.1186/1471-2105-4-41.
    • (2003) BMC Bioinformatics , vol.4 , pp. 41
    • Tatusov, R.L.1
  • 71
    • 28044461531 scopus 로고    scopus 로고
    • Rules governing protein identification by mass spectrometry
    • doi: 10.1002/rcm.2225
    • Taylor GK, Goodlett DR. 2005. Rules governing protein identification by mass spectrometry. Rapid Commun. Mass Spectrom. 19:3420. doi: 10.1002/rcm.2225.
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 3420
    • Taylor, G.K.1    Goodlett, D.R.2
  • 72
    • 38949103470 scopus 로고    scopus 로고
    • Campylobacter jejuni survives within epithelialcells by avoiding delivery to lysosomes
    • doi: 10.1371/journal.ppat.0040014
    • Watson RO, Galan JE. 2008. Campylobacter jejuni survives within epithelial
    • (2008) PLoS Pathog. , vol.4 , pp. 14
    • Watson, R.O.1    Galan, J.E.2
  • 73
    • 0031924312 scopus 로고    scopus 로고
    • Campylobacter jejuni cytolethal distending toxin causes a G2-phase cell cycle block
    • Whitehouse CA, et al. 1998. Campylobacter jejuni cytolethal distending toxin causes a G2-phase cell cycle block. Infect. Immun. 66:1934-1940.
    • (1998) Infect. Immun. , vol.66 , pp. 1934-1940
    • Whitehouse, C.A.1
  • 74
    • 34548028239 scopus 로고    scopus 로고
    • Campylobacter jejuni: molecular biology and pathogenesis
    • Young KT, Davis LM, Dirita VJ. 2007. Campylobacter jejuni: molecular biology and pathogenesis. Nat. Rev. Microbiol. 5:665-679.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 665-679
    • Young, K.T.1    Davis, L.M.2    Dirita, V.J.3
  • 75
    • 0037044765 scopus 로고    scopus 로고
    • Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni
    • Young NM, et al. 2002. Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni. J. Biol. Chem. 277:42530-42539.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42530-42539
    • Young, N.M.1
  • 76
    • 53649091724 scopus 로고    scopus 로고
    • Campylobacter-induced interleukin-8 secretion in polarized human intestinal epithelial cells requires Campylobacter-secreted cytolethal distending toxin- and Toll-like receptor-mediated activation of NF-kappaB
    • Zheng J, Meng J, Zhao S, Singh R, Song W. 2008. Campylobacter-induced interleukin-8 secretion in polarized human intestinal epithelial cells requires Campylobacter-secreted cytolethal distending toxin- and Toll-like receptor-mediated activation of NF-kappaB. Infect. Immun. 76: 4498-4508.
    • (2008) Infect. Immun. , vol.76 , pp. 4498-4508
    • Zheng, J.1    Meng, J.2    Zhao, S.3    Singh, R.4    Song, W.5
  • 77
    • 27744564199 scopus 로고    scopus 로고
    • Intestinal innate immunity to Campylobacter jejuni results in induction of bactericidal human beta-defensins 2 and 3
    • Zilbauer M, et al. 2005. Intestinal innate immunity to Campylobacter jejuni results in induction of bactericidal human beta-defensins 2 and 3. Infect. Immun. 73:7281-7289.
    • (2005) Infect. Immun. , vol.73 , pp. 7281-7289
    • Zilbauer, M.1


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