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Volumn 83, Issue 7, 2009, Pages 2883-2891

The primed ebolavirus glycoprotein (19-Kilodalton GP 1,2): Sequence and residues critical for host cell binding

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN; GLYCOPROTEIN; GLYCOPROTEIN 1; GLYCOPROTEIN 1 2; GLYCOPROTEIN 2; LYSINE; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS FUSION PROTEIN;

EID: 63149192804     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01956-08     Document Type: Article
Times cited : (129)

References (35)
  • 1
    • 0036278649 scopus 로고    scopus 로고
    • C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans
    • Alvarez, C. P., F. Lasala. J. Carrillo, O. Muniz, A. L. Corbi, and R. Delgado. 2002. C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans. J. Virol. 76:6841-6844.
    • (2002) J. Virol , vol.76 , pp. 6841-6844
    • Alvarez, C.P.1    Lasala, F.2    Carrillo, J.3    Muniz, O.4    Corbi, A.L.5    Delgado, R.6
  • 3
    • 34447278575 scopus 로고    scopus 로고
    • Ebola virus glycoprotein 1: Identification of residues important for binding and postbinding events
    • Brindley, M. A., L. Hughes, A. Ruiz, P. B. McCray, Jr., A. Sanchez, D. A. Sanders, and W. Maury. 2007. Ebola virus glycoprotein 1: identification of residues important for binding and postbinding events. J. Virol. 81:7702-7709.
    • (2007) J. Virol , vol.81 , pp. 7702-7709
    • Brindley, M.A.1    Hughes, L.2    Ruiz, A.3    McCray Jr., P.B.4    Sanchez, A.5    Sanders, D.A.6    Maury, W.7
  • 4
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran, K., N. J. Sullivan, U. Felbor, S. P. Whelan, and J. M. Cunningham. 2005. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308:1643-1645.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 5
  • 8
    • 0032849336 scopus 로고    scopus 로고
    • Mutational analysis of the putative fusion domain of Ebola virus glycoprotein
    • Ito, H., S. Watanabe, A. Sanchez, M. A. Whitt, and Y. Kawaoka. 1999. Mutational analysis of the putative fusion domain of Ebola virus glycoprotein. J. Virol. 73:8907-8912.
    • (1999) J. Virol , vol.73 , pp. 8907-8912
    • Ito, H.1    Watanabe, S.2    Sanchez, A.3    Whitt, M.A.4    Kawaoka, Y.5
  • 9
    • 0035148629 scopus 로고    scopus 로고
    • Ebola virus glycoprotein: Proteolytic processing, acylation, cell tropism, and detection of neutralizing antibodies
    • Ito, H., S. Watanabe, A. Takada, and Y. Kawaoka. 2001. Ebola virus glycoprotein: proteolytic processing, acylation, cell tropism, and detection of neutralizing antibodies. J. Virol. 75:1576-1580.
    • (2001) J. Virol , vol.75 , pp. 1576-1580
    • Ito, H.1    Watanabe, S.2    Takada, A.3    Kawaoka, Y.4
  • 10
    • 0036893140 scopus 로고    scopus 로고
    • Covalent modifications of the Ebola virus glycoprotein
    • Jeffers, S. A. D. A. Sanders, and A. Sanchez. 2002. Covalent modifications of the Ebola virus glycoprotein. J. Virol. 76:12463-12472.
    • (2002) J. Virol , vol.76 , pp. 12463-12472
    • Jeffers, S.A.D.A.S.1    Sanchez, A.2
  • 11
    • 37049006295 scopus 로고    scopus 로고
    • Proteolysis of the Ebola virus glycoproteins enhances virus binding and infectivity
    • Kaletsky, R. L., G. Simmons, and P. Bates. 2007. Proteolysis of the Ebola virus glycoproteins enhances virus binding and infectivity. J. Virol. 81:13378-13384.
    • (2007) J. Virol , vol.81 , pp. 13378-13384
    • Kaletsky, R.L.1    Simmons, G.2    Bates, P.3
  • 14
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor
    • Lee, J. E., M. L. Fusco, A. J. Hessell, W. B. Oswald, D. R. Burton, and E. O. Saphire. 2008. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 454:177-182.
    • (2008) Nature , vol.454 , pp. 177-182
    • Lee, J.E.1    Fusco, M.L.2    Hessell, A.J.3    Oswald, W.B.4    Burton, D.R.5    Saphire, E.O.6
  • 15
    • 16244391124 scopus 로고    scopus 로고
    • Comprehensive analysis of Ebola virus GP1 in viral entry
    • Manicassamy, B., J. Wang, H. Jiang, and L. Rong. 2005. Comprehensive analysis of Ebola virus GP1 in viral entry. J. Virol. 79:4793-4805.
    • (2005) J. Virol , vol.79 , pp. 4793-4805
    • Manicassamy, B.1    Wang, J.2    Jiang, H.3    Rong, L.4
  • 16
    • 38449102893 scopus 로고    scopus 로고
    • Analysis of the interaction of Ebola virus glycoprotein with DC-SIGN (dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin) and its homologue DC-SIGNR
    • Marzi, A., P. Moller, S. L. Hanna, T. Harrer, J. Eisemann, A. Steinkasserer, S. Becker, F. Baribaud, and S. Pohlmann. 2007. Analysis of the interaction of Ebola virus glycoprotein with DC-SIGN (dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin) and its homologue DC-SIGNR. J. Infect. Dis. 196(Suppl. 2):S237-S246.
    • (2007) J. Infect. Dis , vol.196 , Issue.SUPPL. 2
    • Marzi, A.1    Moller, P.2    Hanna, S.L.3    Harrer, T.4    Eisemann, J.5    Steinkasserer, A.6    Becker, S.7    Baribaud, F.8    Pohlmann, S.9
  • 17
    • 33749133853 scopus 로고    scopus 로고
    • Identification of two amino acid residues on Ebola virus glycoprotein 1 critical for cell entry
    • Mpanju, O. M, J. S. Towner, J. E. Dover, S. T. Nichol, and C. A. Wilson. 2006. Identification of two amino acid residues on Ebola virus glycoprotein 1 critical for cell entry. Virus Res. 121:205-214.
    • (2006) Virus Res , vol.121 , pp. 205-214
    • Mpanju, O.M.1    Towner, J.S.2    Dover, J.E.3    Nichol, S.T.4    Wilson, C.A.5
  • 19
    • 38449106461 scopus 로고    scopus 로고
    • Analysis of filovirus entry into Vero E6 cells, using inhibitors of endocytosis, endosomal acidification, structural integrity, and cathep-sin (B and L) activity
    • Sanchez, A. 2007. Analysis of filovirus entry into Vero E6 cells, using inhibitors of endocytosis, endosomal acidification, structural integrity, and cathep-sin (B and L) activity. J. Infect. Dis. 196(Suppl. 2):S251-S258.
    • (2007) J. Infect. Dis , vol.196 , Issue.SUPPL. 2
    • Sanchez, A.1
  • 20
    • 34548512432 scopus 로고    scopus 로고
    • Filoviridae: Marburg and Ebola viruses
    • D. M. Knipe et al, ed, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • Sanchez, A., T. W. Geisbert, and H. Feldmann. 2007. Filoviridae: Marburg and Ebola viruses, p. 1409-1448. In D. M. Knipe et al. (ed.), Fields virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields virology , pp. 1409-1448
    • Sanchez, A.1    Geisbert, T.W.2    Feldmann, H.3
  • 21
    • 33645788357 scopus 로고    scopus 로고
    • Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein
    • Schornberg, K., S. Matsuyama. K. Kabsch, S. Delos, A. Bouton, and J. White. 2006. Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein. J. Virol. 80:4174-4178.
    • (2006) J. Virol , vol.80 , pp. 4174-4178
    • Schornberg, K.1    Matsuyama, S.2    Kabsch, K.3    Delos, S.4    Bouton, A.5    White, J.6
  • 24
    • 0036171135 scopus 로고    scopus 로고
    • Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence
    • Simmons, G., R. J. Wool-Lewis, F. Baribaud, R. C. Netter, and P. Bates. 2002. Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence. J. Virol. 76:2518-2528.
    • (2002) J. Virol , vol.76 , pp. 2518-2528
    • Simmons, G.1    Wool-Lewis, R.J.2    Baribaud, F.3    Netter, R.C.4    Bates, P.5
  • 27
    • 0034610176 scopus 로고    scopus 로고
    • Downregulation of betal integrins by Ebola virus glycoprotein: Implication for virus entry
    • Takada, A., S. Watanabe, H. Ito, K. Okazaki, H. Kida, and Y. Kawaoka. 2000. Downregulation of betal integrins by Ebola virus glycoprotein: implication for virus entry. Virology 278:20-26.
    • (2000) Virology , vol.278 , pp. 20-26
    • Takada, A.1    Watanabe, S.2    Ito, H.3    Okazaki, K.4    Kida, H.5    Kawaoka, Y.6
  • 29
    • 0033771310 scopus 로고    scopus 로고
    • Functional importance of the coiled coil of the Ebola virus glycoprotein
    • Watanabe, S., A. Takada, T. Watanabe, H. Ito, H. Kida, and Y. Kawaoka. 2000. Functional importance of the coiled coil of the Ebola virus glycoprotein. J. Virol. 74:10194-10201.
    • (2000) J. Virol , vol.74 , pp. 10194-10201
    • Watanabe, S.1    Takada, A.2    Watanabe, T.3    Ito, H.4    Kida, H.5    Kawaoka, Y.6
  • 30
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • White, J. M., S. E. Delos, M. Brecher, and K. Schornberg. 2008. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43:189-219.
    • (2008) Crit. Rev. Biochem. Mol. Biol , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 31
    • 64249129586 scopus 로고    scopus 로고
    • WHO. 2007. Ebola haemorrhagic fever in Uganda. World Health Organization, Geneva, Switzerland.
    • WHO. 2007. Ebola haemorrhagic fever in Uganda. World Health Organization, Geneva, Switzerland.
  • 32
    • 0031954296 scopus 로고    scopus 로고
    • Characterization of Ebola virus entry by using pseudotyped viruses: Identification of receptor-deficient cell lines
    • Wool-Lewis, R. J., and P. Bates. 1998. Characterization of Ebola virus entry by using pseudotyped viruses: identification of receptor-deficient cell lines. J. Virol. 72:3155-3160.
    • (1998) J. Virol , vol.72 , pp. 3155-3160
    • Wool-Lewis, R.J.1    Bates, P.2
  • 33
    • 0032949982 scopus 로고    scopus 로고
    • Endoproteolytic processing of the Ebola virus envelope glycoprotein: Cleavage is not required for function
    • Wool-Lewis, R. J., and P. Bates. 1999. Endoproteolytic processing of the Ebola virus envelope glycoprotein: cleavage is not required for function. J. Virol. 73:1419-1426.
    • (1999) J. Virol , vol.73 , pp. 1419-1426
    • Wool-Lewis, R.J.1    Bates, P.2
  • 34
    • 0033831191 scopus 로고    scopus 로고
    • Identification of the Ebola virus glycoprotein as the main viral determinant of vascular cell cytotoxicity and injury
    • Yang, Z. Y., H. J. Duckers, N. J. Sullivan, A. Sanchez, E. G. Nabel, and G. J. Nabel. 2000. Identification of the Ebola virus glycoprotein as the main viral determinant of vascular cell cytotoxicity and injury. Nat. Med. 6:886-889.
    • (2000) Nat. Med , vol.6 , pp. 886-889
    • Yang, Z.Y.1    Duckers, H.J.2    Sullivan, N.J.3    Sanchez, A.4    Nabel, E.G.5    Nabel, G.J.6
  • 35
    • 11144221586 scopus 로고    scopus 로고
    • Studies of Ebola virus glycoprotein-mediated entry and fusion by using pseudotyped human immunodeficiency virus type 1 virions: Involvement of cytoskeletal proteins and enhancement by tumor necrosis factor alpha
    • Yonezawa, A., M. Cavrois, and W. C. Greene. 2005. Studies of Ebola virus glycoprotein-mediated entry and fusion by using pseudotyped human immunodeficiency virus type 1 virions: involvement of cytoskeletal proteins and enhancement by tumor necrosis factor alpha. J. Virol. 79:918-926.
    • (2005) J. Virol , vol.79 , pp. 918-926
    • Yonezawa, A.1    Cavrois, M.2    Greene, W.C.3


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