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Volumn 98, Issue 12, 1996, Pages 2813-2818

An N-linked high-mannose type oligosaccharide, expressed at the major outer membrane protein of Chlamydia trachomatis, mediates attachment and infectivity of the microorganism to HeLa cells

Author keywords

bacterial glycoprotein; carbohydrate; intracellular organism; ligand; parasite host cell interaction

Indexed keywords

ASPARAGINE LINKED OLIGOSACCHARIDE; MANNOSE; OUTER MEMBRANE PROTEIN; OVALBUMIN; SIALIC ACID;

EID: 0030455618     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI119109     Document Type: Article
Times cited : (104)

References (20)
  • 2
    • 0020459579 scopus 로고
    • Structural analysis of chlamydial major outer membrane protein
    • Caldwell, H.D., and R. Judd. 1982. Structural analysis of chlamydial major outer membrane protein. Infect. Immun. 38:960-968.
    • (1982) Infect. Immun. , vol.38 , pp. 960-968
    • Caldwell, H.D.1    Judd, R.2
  • 3
    • 0020584902 scopus 로고
    • Disulfide-linked oligomers of the major outer membrane protein of chlamydiae
    • Newhall, W.J., V. and R.B. Jones. 1983. Disulfide-linked oligomers of the major outer membrane protein of chlamydiae. J. Bacteriol. 154:998-1001.
    • (1983) J. Bacteriol. , vol.154 , pp. 998-1001
    • Newhall, W.J.V.1    Jones, R.B.2
  • 4
    • 0019906434 scopus 로고
    • Neutralization of Chlamydia trachomatis infectivity with antibodies to the major outer membrane protein
    • Caldwell, H.D., and L.J. Perry. 1982. Neutralization of Chlamydia trachomatis infectivity with antibodies to the major outer membrane protein. Infect. Immun. 38:745-754.
    • (1982) Infect. Immun. , vol.38 , pp. 745-754
    • Caldwell, H.D.1    Perry, L.J.2
  • 5
    • 0022360537 scopus 로고
    • Neutralization of Chlamydia trachomatis cell culture infection by serovar-specific monoclonal antibodies
    • Lucero, M.E., and C.-C. Kuo. 1985. Neutralization of Chlamydia trachomatis cell culture infection by serovar-specific monoclonal antibodies. Infect. Immun. 50:595-597.
    • (1985) Infect. Immun. , vol.50 , pp. 595-597
    • Lucero, M.E.1    Kuo, C.-C.2
  • 6
    • 0025012654 scopus 로고
    • Identification of lectin-binding proteins in Chlamydia species
    • Swanson, A.F., and C.-C. Kuo. 1990. Identification of lectin-binding proteins in Chlamydia species. Infect. Immun. 58:502-507.
    • (1990) Infect. Immun. , vol.58 , pp. 502-507
    • Swanson, A.F.1    Kuo, C.-C.2
  • 7
    • 0025851780 scopus 로고
    • Evidence that the major outer membrane protein of Chlamydia trachomatis is glycosylated
    • Swanson, A.F., and C.-C. Kuo. 1991. Evidence that the major outer membrane protein of Chlamydia trachomatis is glycosylated. Infect. Immun. 59: 2120-2125.
    • (1991) Infect. Immun. , vol.59 , pp. 2120-2125
    • Swanson, A.F.1    Kuo, C.-C.2
  • 8
    • 0026167729 scopus 로고
    • The characterization of lectin-binding proteins of Chlamydia trachomatis as glycoproteins
    • Swanson, A.F., and C.-C. Kuo. 1991. The characterization of lectin-binding proteins of Chlamydia trachomatis as glycoproteins. Microb. Pathog. 10: 465-473.
    • (1991) Microb. Pathog. , vol.10 , pp. 465-473
    • Swanson, A.F.1    Kuo, C.-C.2
  • 9
    • 0024120902 scopus 로고
    • Structure and biosynthesis of prokaryocytic glycoproteins
    • Wieland, F. 1988. Structure and biosynthesis of prokaryocytic glycoproteins. Biochimie (Paris). 70:1493-1504.
    • (1988) Biochimie (Paris) , vol.70 , pp. 1493-1504
    • Wieland, F.1
  • 10
    • 0027955026 scopus 로고
    • Binding of the glycan of the major outer membrane protein of Chlamydia trachomatis to HeLa cells
    • Swanson, A.F., and C.-C. Kuo. 1994. Binding of the glycan of the major outer membrane protein of Chlamydia trachomatis to HeLa cells. Infect. Immun. 62:24-28.
    • (1994) Infect. Immun. , vol.62 , pp. 24-28
    • Swanson, A.F.1    Kuo, C.-C.2
  • 11
    • 0023948708 scopus 로고
    • Analyses of N-linked oligosaccharides using a two-dimensional mapping technique
    • Tomiya, N., J. Awaya, M. Kurono, S. Endo, Y. Arata, and N. Takahashi. 1988. Analyses of N-linked oligosaccharides using a two-dimensional mapping technique. Anal. Biochem. 171:73-90.
    • (1988) Anal. Biochem. , vol.171 , pp. 73-90
    • Tomiya, N.1    Awaya, J.2    Kurono, M.3    Endo, S.4    Arata, Y.5    Takahashi, N.6
  • 12
    • 0001296607 scopus 로고
    • Chapter 8. Analysis of N-linked oligosaccharides: Application of glycosaminidase A
    • N. Takahashi and T. Muramatsu, editors. CRC Press, Boca Raton, FL
    • Takahashi, N., and N. Tomiya. 1992. Chapter 8. Analysis of N-linked oligosaccharides: Application of glycosaminidase A. In Handbook of Endoglycosidases and Glycosaminidase. N. Takahashi and T. Muramatsu, editors. CRC Press, Boca Raton, FL. 183-332.
    • (1992) Handbook of Endoglycosidases and Glycosaminidase , pp. 183-332
    • Takahashi, N.1    Tomiya, N.2
  • 13
    • 0002698044 scopus 로고
    • Growth of trachoma organism in HeLa 229 cell culture
    • D. Hobson and K.K. Holmes, editors. American Society for Microbiology, Washington, D.C.
    • Kuo, C.-C., S.-P. Wang, and J.T. Crayston. 1977. Growth of trachoma organism in HeLa 229 cell culture. In Nongonococcal urethritis and related infections, D. Hobson and K.K. Holmes, editors. American Society for Microbiology, Washington, D.C. 328-336.
    • (1977) Nongonococcal Urethritis and Related Infections , pp. 328-336
    • Kuo, C.-C.1    Wang, S.-P.2    Crayston, J.T.3
  • 14
    • 0020020636 scopus 로고
    • Complex carbohydrates. D. Preparation and fractionation of glycopeptides
    • Academic Press, New York
    • Finne, J., and T. Krusius. 1982. Complex carbohydrates. D. Preparation and fractionation of glycopeptides. In Methods in Enzymology. Academic Press, New York. 83:269-277.
    • (1982) Methods in Enzymology , vol.83 , pp. 269-277
    • Finne, J.1    Krusius, T.2
  • 15
    • 0017146754 scopus 로고
    • The structural basis of the different affinities of two type of acidic N-glycosidic glycopeptides for concanavalin A-Sepharose
    • Krusius, T., J. Finne, and H. Rauvala. 1976. The structural basis of the different affinities of two type of acidic N-glycosidic glycopeptides for concanavalin A-Sepharose. FEBS Lett. 71:117-120.
    • (1976) FEBS Lett. , vol.71 , pp. 117-120
    • Krusius, T.1    Finne, J.2    Rauvala, H.3
  • 18
    • 0017261977 scopus 로고
    • Interaction of Chlamydia trachomatis organisms and HeLa 229 cells
    • Kuo, C.-C., and J.T. Grayston. 1976. Interaction of Chlamydia trachomatis organisms and HeLa 229 cells. Infect. Immun. 13:1103-1109.
    • (1976) Infect. Immun. , vol.13 , pp. 1103-1109
    • Kuo, C.-C.1    Grayston, J.T.2
  • 19
    • 0025362207 scopus 로고
    • Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains
    • Taylor, M.E., J.T. Conary, M.R. Lennart, P.D. Stahl, and K. Drickamer. 1990. Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains. J. Biol. Chem. 265:12156-12162.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12156-12162
    • Taylor, M.E.1    Conary, J.T.2    Lennart, M.R.3    Stahl, P.D.4    Drickamer, K.5
  • 20
    • 0015840102 scopus 로고
    • Effect of polycations, polyanions, and neuraminidase on the infectivity of trachoma-inclusion conjunctivitis and lymphogranuloma venereum organisms in HeLa cells: Sialic acid residues as possible receptors for trachoma-inclusion conjunctivitis
    • Kuo, C.-C., S.-P. Wang, and J.T. Grayston. 1973. Effect of polycations, polyanions, and neuraminidase on the infectivity of trachoma-inclusion conjunctivitis and lymphogranuloma venereum organisms in HeLa cells: sialic acid residues as possible receptors for trachoma-inclusion conjunctivitis. Infect. Immun. 8:74-79.
    • (1973) Infect. Immun. , vol.8 , pp. 74-79
    • Kuo, C.-C.1    Wang, S.-P.2    Grayston, J.T.3


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