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Volumn 195, Issue 23, 2013, Pages 5323-5333

Characterization of the interaction between the chlamydial adhesin omcb and the human host cell

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; ARGININE; BACTERIAL PROTEIN; BACTERIAL PROTEIN OMCB; HEPARAN SULFATE; HEPARIN; NEUTRALIZING ANTIBODY; PROLINE; UNCLASSIFIED DRUG;

EID: 84887530763     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00780-13     Document Type: Article
Times cited : (27)

References (51)
  • 7
    • 0034861175 scopus 로고    scopus 로고
    • Isolation and characterization of a mutant Chinese hamster ovary cell line that is resistant to Chlamydia trachomatis infection at a novel step in the attachment process
    • Carabeo RA, Hackstadt T. 2001. Isolation and characterization of a mutant Chinese hamster ovary cell line that is resistant to Chlamydia trachomatis infection at a novel step in the attachment process. Infect. Immun. 69:5899-5904.
    • (2001) Infect. Immun. , vol.69 , pp. 5899-5904
    • Carabeo, R.A.1    Hackstadt, T.2
  • 8
    • 0029123843 scopus 로고
    • Interaction of outer envelope proteins of Chlamydia psittaci GPIC with the HeLa cell surface
    • Ting LM, Hsia RC, Haidaris CG, Bavoil PM. 1995. Interaction of outer envelope proteins of Chlamydia psittaci GPIC with the HeLa cell surface. Infect. Immun. 63:3600-3608.
    • (1995) Infect. Immun. , vol.63 , pp. 3600-3608
    • Ting, L.M.1    Hsia, R.C.2    Haidaris, C.G.3    Bavoil, P.M.4
  • 9
    • 0031769683 scopus 로고    scopus 로고
    • Topological analysis of Chlamydia trachomatis L2 outer membrane protein 2
    • Mygind P, Christiansen G, Birkelund S. 1998. Topological analysis of Chlamydia trachomatis L2 outer membrane protein 2. J. Bacteriol. 180:5784-5787.
    • (1998) J. Bacteriol. , vol.180 , pp. 5784-5787
    • Mygind, P.1    Christiansen, G.2    Birkelund, S.3
  • 12
    • 33845939630 scopus 로고    scopus 로고
    • Chlamydia trachomatis OmcB protein is a surfaceexposed glycosaminoglycan-dependent adhesin
    • Fadel S, Eley A. 2007. Chlamydia trachomatis OmcB protein is a surfaceexposed glycosaminoglycan-dependent adhesin. J. Med. Microbiol. 56:15-22.
    • (2007) J. Med. Microbiol. , vol.56 , pp. 15-22
    • Fadel, S.1    Eley, A.2
  • 13
    • 37349053423 scopus 로고    scopus 로고
    • The Chlamydia outer membrane protein OmcB is required for adhesion and exhibits biovar-specific differences in glycosaminoglycan binding
    • Moelleken K, Hegemann JH. 2008. The Chlamydia outer membrane protein OmcB is required for adhesion and exhibits biovar-specific differences in glycosaminoglycan binding. Mol. Microbiol. 67:403-419.
    • (2008) Mol. Microbiol. , vol.67 , pp. 403-419
    • Moelleken, K.1    Hegemann, J.H.2
  • 14
    • 0028306744 scopus 로고
    • Trachoma and LGV biovars of Chlamydia trachomatis share the same glycosaminoglycan-dependent mechanism for infection of eukaryotic cells
    • Chen JC, Stephens RS. 1994. Trachoma and LGV biovars of Chlamydia trachomatis share the same glycosaminoglycan-dependent mechanism for infection of eukaryotic cells. Mol. Microbiol. 11:501-507.
    • (1994) Mol. Microbiol. , vol.11 , pp. 501-507
    • Chen, J.C.1    Stephens, R.S.2
  • 15
    • 15844391177 scopus 로고    scopus 로고
    • Structural requirements of heparin binding to Chlamydia trachomatis
    • Chen JC, Zhang JP, Stephens RS. 1996. Structural requirements of heparin binding to Chlamydia trachomatis. J. Biol. Chem. 271:11134-11140.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11134-11140
    • Chen, J.C.1    Zhang, J.P.2    Stephens, R.S.3
  • 16
    • 0031017697 scopus 로고    scopus 로고
    • Chlamydia trachomatis glycosaminoglycan dependent and independent attachment to eukaryotic cells
    • Chen JCR, Stephens RS. 1997. Chlamydia trachomatis glycosaminoglycan dependent and independent attachment to eukaryotic cells. Microb. Pathog. 22(1):23-30.
    • (1997) Microb. Pathog , vol.22 , Issue.1 , pp. 23-30
    • Chen, J.C.R.1    Stephens, R.S.2
  • 17
    • 0029090119 scopus 로고
    • Sulfated polyanions block Chlamydia trachomatis infection of cervix-derived human epithelia
    • Zaretzky FR, Pearce-Pratt R, Phillips DM. 1995. Sulfated polyanions block Chlamydia trachomatis infection of cervix-derived human epithelia. Infect. Immun. 63:3520-3526.
    • (1995) Infect. Immun. , vol.63 , pp. 3520-3526
    • Zaretzky, F.R.1    Pearce-Pratt, R.2    Phillips, D.M.3
  • 18
    • 0030978083 scopus 로고    scopus 로고
    • Differences in the association of Chlamydia trachomatis serovar E and serovar L2 with epithelial cells in vitro may reflect biological differences in vivo
    • Davis CH, Wyrick PB. 1997. Differences in the association of Chlamydia trachomatis serovar E and serovar L2 with epithelial cells in vitro may reflect biological differences in vivo. Infect. Immun. 65:2914-2924.
    • (1997) Infect. Immun. , vol.65 , pp. 2914-2924
    • Davis, C.H.1    Wyrick, P.B.2
  • 19
    • 0035142611 scopus 로고    scopus 로고
    • Infectivity of Chlamydia trachomatis serovar LGV but not E is dependent on host cell heparan sulfate
    • Taraktchoglou M, Pacey AA, Turnbull JE, Eley A. 2001. Infectivity of Chlamydia trachomatis serovar LGV but not E is dependent on host cell heparan sulfate. Infect. Immun. 69:968-976.
    • (2001) Infect. Immun. , vol.69 , pp. 968-976
    • Taraktchoglou, M.1    Pacey, A.A.2    Turnbull, J.E.3    Eley, A.4
  • 20
    • 0035879775 scopus 로고    scopus 로고
    • Heparan sulfate-like glycosaminoglycan is a cellular receptor for Chlamydia pneumoniae
    • Wuppermann FN, Hegemann JH, Jantos CA. 2001. Heparan sulfate-like glycosaminoglycan is a cellular receptor for Chlamydia pneumoniae. J. Infect. Dis. 184:181-187.
    • (2001) J. Infect. Dis. , vol.184 , pp. 181-187
    • Wuppermann, F.N.1    Hegemann, J.H.2    Jantos, C.A.3
  • 22
    • 33646031240 scopus 로고    scopus 로고
    • Inhibitory effect of heparan sulfate-like glycosaminoglycans on the infectivity of Chlamydia pneumoniae in HL cells varies between strains
    • Yan Y, Silvennoinen-Kassinen S, Leinonen M, Saikku P. 2006. Inhibitory effect of heparan sulfate-like glycosaminoglycans on the infectivity of Chlamydia pneumoniae in HL cells varies between strains. Microbes Infect. 8:866-872.
    • (2006) Microbes Infect. , vol.8 , pp. 866-872
    • Yan, Y.1    Silvennoinen-Kassinen, S.2    Leinonen, M.3    Saikku, P.4
  • 23
    • 0025875756 scopus 로고
    • Proteoglycans: structures and interactions
    • Kjellen L, Lindahl U. 1991. Proteoglycans: structures and interactions. Annu. Rev. Biochem. 60:443-475.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellen, L.1    Lindahl, U.2
  • 27
    • 0032006909 scopus 로고    scopus 로고
    • Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding proteins
    • Hileman RE, Fromm JR, Weiler JM, Linhardt RJ. 1998. Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding proteins. Bioessays 20:156-167.
    • (1998) Bioessays , vol.20 , pp. 156-167
    • Hileman, R.E.1    Fromm, J.R.2    Weiler, J.M.3    Linhardt, R.J.4
  • 28
    • 0024584913 scopus 로고
    • Molecular modeling of proteinglycosaminoglycan interactions
    • Cardin AD, Weintraub HJ. 1989. Molecular modeling of proteinglycosaminoglycan interactions. Arteriosclerosis 9:21-32.
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.2
  • 29
    • 0028859853 scopus 로고
    • Architecture of the cell envelope of Chlamydia psittaci 6BC
    • Everett KD, Hatch TP. 1995. Architecture of the cell envelope of Chlamydia psittaci 6BC. J. Bacteriol. 177:877-882.
    • (1995) J. Bacteriol. , vol.177 , pp. 877-882
    • Everett, K.D.1    Hatch, T.P.2
  • 30
    • 0026622894 scopus 로고
    • Mechanism of C. trachomatis attachment to eukaryotic host cells
    • Zhang JP, Stephens RS. 1992. Mechanism of C. trachomatis attachment to eukaryotic host cells. Cell 69:861-869.
    • (1992) Cell , vol.69 , pp. 861-869
    • Zhang, J.P.1    Stephens, R.S.2
  • 31
    • 0037446910 scopus 로고    scopus 로고
    • Comparative studies of glycosaminoglycan involvement in Chlamydia pneumoniae and C. trachomatis invasion of host cells
    • Beswick EJ, Travelstead A, Cooper MD. 2003. Comparative studies of glycosaminoglycan involvement in Chlamydia pneumoniae and C. trachomatis invasion of host cells. J. Infect. Dis. 187:1291-1300.
    • (2003) J. Infect. Dis. , vol.187 , pp. 1291-1300
    • Beswick, E.J.1    Travelstead, A.2    Cooper, M.D.3
  • 32
    • 51149100598 scopus 로고    scopus 로고
    • Differential glycosaminoglycan binding of Chlamydia trachomatis OmcB protein from serovars E and LGV
    • Fadel S, Eley A. 2008. Differential glycosaminoglycan binding of Chlamydia trachomatis OmcB protein from serovars E and LGV. J. Med. Microbiol. 57:1058-1061.
    • (2008) J. Med. Microbiol. , vol.57 , pp. 1058-1061
    • Fadel, S.1    Eley, A.2
  • 33
    • 0033105366 scopus 로고    scopus 로고
    • A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association
    • Dersch P, Isberg RR. 1999. A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association. EMBO J. 18:1199-1213.
    • (1999) EMBO J. , vol.18 , pp. 1199-1213
    • Dersch, P.1    Isberg, R.R.2
  • 35
    • 0032557443 scopus 로고    scopus 로고
    • Generation and application of type-specific antiheparan sulfate antibodies using phage display technology. Further evidence for heparan sulfate heterogeneity in the kidney
    • van Kuppevelt TH, Dennissen MA, van Venrooij WJ, Hoet RM, Veerkamp JH. 1998. Generation and application of type-specific antiheparan sulfate antibodies using phage display technology. Further evidence for heparan sulfate heterogeneity in the kidney. J. Biol. Chem. 273:12960-12966.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12960-12966
    • van Kuppevelt, T.H.1    Dennissen, M.A.2    van Venrooij, W.J.3    Hoet, R.M.4    Veerkamp, J.H.5
  • 39
    • 0027327277 scopus 로고
    • Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues
    • Margalit H, Fischer N, Ben-Sasson SA. 1993. Comparative analysis of structurally defined heparin binding sequences reveals a distinct spatial distribution of basic residues. J. Biol. Chem. 268:19228-19231.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19228-19231
    • Margalit, H.1    Fischer, N.2    Ben-Sasson, S.A.3
  • 40
    • 0034213360 scopus 로고    scopus 로고
    • Heparan sulfate heterogeneity in skeletal muscle basal lamina: demonstration by phage display-derived antibodies
    • Jenniskens GJ, Oosterhof A, Brandwijk R, Veerkamp JH, van Kuppevelt TH. 2000. Heparan sulfate heterogeneity in skeletal muscle basal lamina: demonstration by phage display-derived antibodies. J. Neurosci. 20:4099-4111.
    • (2000) J. Neurosci. , vol.20 , pp. 4099-4111
    • Jenniskens, G.J.1    Oosterhof, A.2    Brandwijk, R.3    Veerkamp, J.H.4    van Kuppevelt, T.H.5
  • 42
    • 84869020025 scopus 로고    scopus 로고
    • ScFv antiheparan sulfate antibodies unexpectedly activate endothelial and cancer cells through p38 MAPK: implications for antibody-based targeting of heparan sulfate proteoglycans in cancer
    • doi:10.1371/journal.pone.0049092
    • Christianson HC, van Kuppevelt TH, Belting M. 2012. ScFv antiheparan sulfate antibodies unexpectedly activate endothelial and cancer cells through p38 MAPK: implications for antibody-based targeting of heparan sulfate proteoglycans in cancer. PLoS One 7:e49092. doi:10.1371/journal.pone.0049092.
    • (2012) PLoS One , vol.7
    • Christianson, H.C.1    van Kuppevelt, T.H.2    Belting, M.3
  • 44
    • 0344838680 scopus 로고    scopus 로고
    • Longitudinal assessment of infecting serovars of Chlamydia trachomatis in Seattle public health clinics: 1988-1996
    • Suchland RJ, Eckert LO, Hawes SE, Stamm WE. 2003. Longitudinal assessment of infecting serovars of Chlamydia trachomatis in Seattle public health clinics: 1988-1996. Sex Transm. Dis. 30:357-361.
    • (2003) Sex Transm. Dis. , vol.30 , pp. 357-361
    • Suchland, R.J.1    Eckert, L.O.2    Hawes, S.E.3    Stamm, W.E.4
  • 46
    • 12744270018 scopus 로고    scopus 로고
    • Characterization of ompA genotypes by sequence analysis of DNA from all detected cases of Chlamydia trachomatis infections during 1 year of contact tracing in a Swedish county
    • Lysen M, Osterlund A, Rubin CJ, Persson T, Persson I, Herrmann B. 2004. Characterization of ompA genotypes by sequence analysis of DNA from all detected cases of Chlamydia trachomatis infections during 1 year of contact tracing in a Swedish county. J. Clin. Microbiol. 42:1641-1647.
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 1641-1647
    • Lysen, M.1    Osterlund, A.2    Rubin, C.J.3    Persson, T.4    Persson, I.5    Herrmann, B.6
  • 47
    • 77957733862 scopus 로고    scopus 로고
    • The prevalence and distribution of Chlamydia trachomatis genotypes among sexually transmitted disease clinic patients in Guangzhou, China, 2005-2008
    • Yang B, Zheng HP, Feng ZQ, Xue YH, Wu XZ, Huang JM, Xue XJ, Jiang HN. 2010. The prevalence and distribution of Chlamydia trachomatis genotypes among sexually transmitted disease clinic patients in Guangzhou, China, 2005-2008. Jpn. J. Infect. Dis. 63:342-345.
    • (2010) Jpn. J. Infect. Dis. , vol.63 , pp. 342-345
    • Yang, B.1    Zheng, H.P.2    Feng, Z.Q.3    Xue, Y.H.4    Wu, X.Z.5    Huang, J.M.6    Xue, X.J.7    Jiang, H.N.8
  • 49
    • 0026076419 scopus 로고
    • Chaperone-assisted assembly and molecular architecture of adhesive pili
    • Hultgren SJ, Normark S, Abraham SN. 1991. Chaperone-assisted assembly and molecular architecture of adhesive pili. Annu. Rev. Microbiol. 45:383-415.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 383-415
    • Hultgren, S.J.1    Normark, S.2    Abraham, S.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.