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Volumn 77, Issue 2, 2003, Pages 1649-1652

Valency of antibody binding to enveloped virus particles as determined by surface plasmon resonance

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN BINDING; ARTICLE; CONTROLLED STUDY; INFLUENZA VIRUS; METHODOLOGY; NONHUMAN; PRIORITY JOURNAL; SURFACE PLASMON RESONANCE; VIRUS ENVELOPE; VIRUS PARTICLE;

EID: 0037225738     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.2.1649-1652.2003     Document Type: Article
Times cited : (16)

References (20)
  • 1
    • 0025020248 scopus 로고
    • Antibody: The flexible adaptor molecule
    • Burton, D. R. 1990. Antibody: The flexible adaptor molecule. Trends Biochem. Sci. 15:64-69.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 64-69
    • Burton, D.R.1
  • 2
    • 0020416123 scopus 로고
    • The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (HI subtype)
    • Caton, A. J., G. G. Brownlee, J. W. Yewdell, and W. Gerhard. 1982. The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (HI subtype). Cell 31:417-427.
    • (1982) Cell , vol.31 , pp. 417-427
    • Caton, A.J.1    Brownlee, G.G.2    Yewdell, J.W.3    Gerhard, W.4
  • 3
    • 0031902570 scopus 로고    scopus 로고
    • Antibody-mediated neutralization of human rhinovirus 14 explored by means of cryoelectron microscopy and X-ray crystallography of virus-Fab complexes
    • Che, Z., N. H. Olson, D. Leippe, W.-M. Lee, A. G. Mosser, R. R. Rueckert, T. S. Baker, and T. J. Smith. 1998. Antibody-mediated neutralization of human rhinovirus 14 explored by means of cryoelectron microscopy and X-ray crystallography of virus-Fab complexes. J. Virol. 72:4610-4622.
    • (1998) J. Virol. , vol.72 , pp. 4610-4622
    • Che, Z.1    Olson, N.H.2    Leippe, D.3    Lee, W.-M.4    Mosser, A.G.5    Rueckert, R.R.6    Baker, T.S.7    Smith, T.J.8
  • 5
    • 0034535166 scopus 로고    scopus 로고
    • Two influenza A virus haemagglutinin-specific Fabs neutralize by inhibiting virus attachment to target cells, while neutralization by their IgGs is complex and occurs through fusion-inhibition and attachment-inhibition simultaneously
    • Edwards, M. J., and N. J. Dimmock. 2000. Two influenza A virus haemagglutinin-specific Fabs neutralize by inhibiting virus attachment to target cells, while neutralization by their IgGs is complex and occurs through fusion-inhibition and attachment-inhibition simultaneously. Virology 278:423-435.
    • (2000) Virology , vol.278 , pp. 423-435
    • Edwards, M.J.1    Dimmock, N.J.2
  • 6
    • 8244249460 scopus 로고    scopus 로고
    • Structure of the complex of a Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: Positioning of a highly mobile antigenic loop
    • Hewat, E. A., N. Verdaguer, I. Fita, W. Blakemore, S. Brookes, A. King, J. Newman, E. Domingo, M. G. Mateu, and D. Stuart. 1997. Structure of the complex of a Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: Positioning of a highly mobile antigenic loop. EMBO J. 16: 1492-1500.
    • (1997) EMBO J. , vol.16 , pp. 1492-1500
    • Hewat, E.A.1    Verdaguer, N.2    Fita, I.3    Blakemore, W.4    Brookes, S.5    King, A.6    Newman, J.7    Domingo, E.8    Mateu, M.G.9    Stuart, D.10
  • 7
    • 0030007379 scopus 로고    scopus 로고
    • Structure of a neutralizing antibody bound bivalently to human rhinovirus 2
    • Hewat, E. A., and D. Blaas. 1996. Structure of a neutralizing antibody bound bivalently to human rhinovirus 2. EMBO J. 15:1515-1523.
    • (1996) EMBO J. , vol.15 , pp. 1515-1523
    • Hewat, E.A.1    Blaas, D.2
  • 8
    • 0034970430 scopus 로고    scopus 로고
    • Structural studies on antibody interacting with viruses
    • Hewat, E. A., and D. Blaas. 2001. Structural studies on antibody interacting with viruses. Curr. Top. Microbiol. Immunol. 260:29-44.
    • (2001) Curr. Top. Microbiol. Immunol. , vol.260 , pp. 29-44
    • Hewat, E.A.1    Blaas, D.2
  • 9
    • 0031967887 scopus 로고    scopus 로고
    • Structure of a neutralizing antibody bound monovalently to human rhinovirus
    • Hewat, E. A., T. C. Marlovits, and D. Blaas. 1998. Structure of a neutralizing antibody bound monovalently to human rhinovirus. J. Virol. 72:4396-4402.
    • (1998) J. Virol. , vol.72 , pp. 4396-4402
    • Hewat, E.A.1    Marlovits, T.C.2    Blaas, D.3
  • 10
    • 0001438423 scopus 로고
    • Neutralization of picornaviruses: Support for the pentamer bridging hypothesis
    • B.-L. Semler and E. Ehrenfeld (ed.). American Society for Microbiology, Washington, D. C.
    • Mosser, A. G., D. Leippe, and R. R. Rueckert. 1989. Neutralization of picornaviruses: Support for the pentamer bridging hypothesis, p. 155-167. In B.-L. Semler and E. Ehrenfeld (ed.), Molecular Aspects of Picornavirus Infection and Detection. American Society for Microbiology, Washington, D. C.
    • (1989) Molecular Aspects of Picornavirus Infection and Detection , pp. 155-167
    • Mosser, A.G.1    Leippe, D.2    Rueckert, R.R.3
  • 11
    • 0027974229 scopus 로고
    • Direct imaging of interactions between an icosahedral virus and conjugate fragments by cryoelectron microscopy and X-ray crystallography
    • Porta, C., G. Wang, H. Cheng, Z. Chen, T. S. Baker, and J. E. Johnson. 1994. Direct imaging of interactions between an icosahedral virus and conjugate fragments by cryoelectron microscopy and X-ray crystallography. Virology 204:777-778.
    • (1994) Virology , vol.204 , pp. 777-778
    • Porta, C.1    Wang, G.2    Cheng, H.3    Chen, Z.4    Baker, T.S.5    Johnson, J.E.6
  • 12
    • 0034966682 scopus 로고    scopus 로고
    • Antibody interactions with rhinovirus: Lessons for mechanism of neutralization and the role of immunity in viral evolution
    • Smith, T. J. 2001. Antibody interactions with rhinovirus: Lessons for mechanism of neutralization and the role of immunity in viral evolution. Curr. Top. Microbiol. Immunol. 260:1-28.
    • (2001) Curr. Top. Microbiol. Immunol. , vol.260 , pp. 1-28
    • Smith, T.J.1
  • 13
    • 0027306163 scopus 로고
    • Structure of a human rhinovirus-bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility
    • Smith, T. J., N. H. Olson, R. H. Cheng, E. S. Chase, and T. S. Baker. 1993. Structure of a human rhinovirus-bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility. Proc. Natl. Acad. Sci. USA 90:7015-7018.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7015-7018
    • Smith, T.J.1    Olson, N.H.2    Cheng, R.H.3    Chase, E.S.4    Baker, T.S.5
  • 15
    • 0020687429 scopus 로고
    • Generation of antibody diversity in the immune response of BALB/c mice to influenza virus hemagglutinin. I. Significant variation in repertoire expression between individual mice
    • Staudt, L. M., and W. Gerhard. 1983. Generation of antibody diversity in the immune response of BALB/c mice to influenza virus hemagglutinin. I. Significant variation in repertoire expression between individual mice. J. Exp. Med. 157:687-704.
    • (1983) J. Exp. Med. , vol.157 , pp. 687-704
    • Staudt, L.M.1    Gerhard, W.2
  • 16
    • 0023230133 scopus 로고
    • Different virus-precipitating activities of neutralizing monoclonal antibodies that recognise distinct sites on poliovirus particles
    • Taniguchi, K., and S. Urasawa. 1987. Different virus-precipitating activities of neutralizing monoclonal antibodies that recognise distinct sites on poliovirus particles. Arch. Virol. 92:27-40.
    • (1987) Arch. Virol. , vol.92 , pp. 27-40
    • Taniguchi, K.1    Urasawa, S.2
  • 17
    • 0022508567 scopus 로고
    • Relationship between poliovirus neutralization and aggregation
    • Thomas, A. A. M., R. Vrijsen, and A. Boeyé. 1986. Relationship between poliovirus neutralization and aggregation. J. Virol. 59:479-485.
    • (1986) J. Virol. , vol.59 , pp. 479-485
    • Thomas, A.A.M.1    Vrijsen, R.2    Boeyé, A.3
  • 18
    • 0022049447 scopus 로고
    • A monoclonal antibody that neutralizes poliovirus by cross-linking virions
    • Thomas, A. A. M., P. Brioen, and A. Boeyé. 1985. A monoclonal antibody that neutralizes poliovirus by cross-linking virions. J. Virol. 54:7-13.
    • (1985) J. Virol. , vol.54 , pp. 7-13
    • Thomas, A.A.M.1    Brioen, P.2    Boeyé, A.3
  • 19
    • 0033558734 scopus 로고    scopus 로고
    • Flexibility of the major antigenic loop of foot-and-mouth disease virus bound to a Fab fragment of a neutralizing antibody: Structure and neutralisation
    • Verdaguer, N., G. Schoehn, W. F. Ochoa, I. Fita, S. Brookes, A. King, E. Domingo, M. G. Mateu, D. Stuart, and E. A. Hewat. 1999. Flexibility of the major antigenic loop of foot-and-mouth disease virus bound to a Fab fragment of a neutralizing antibody: Structure and neutralisation. Virology 255: 260-268.
    • (1999) Virology , vol.255 , pp. 260-268
    • Verdaguer, N.1    Schoehn, G.2    Ochoa, W.F.3    Fita, I.4    Brookes, S.5    King, A.6    Domingo, E.7    Mateu, M.G.8    Stuart, D.9    Hewat, E.A.10
  • 20
    • 0028773903 scopus 로고
    • The structure of a neutralized virus: Canine parvovirus complexed with neutralizing antibody fragment
    • Wikoff, W. R., G. J. Wang, C. R. Parrish, R. H. Cheng, M. L. Strassheim, T. S. Baker, and M. G. Rossmann. 1994. The structure of a neutralized virus: Canine parvovirus complexed with neutralizing antibody fragment. Structure 2:595-607.
    • (1994) Structure , vol.2 , pp. 595-607
    • Wikoff, W.R.1    Wang, G.J.2    Parrish, C.R.3    Cheng, R.H.4    Strassheim, M.L.5    Baker, T.S.6    Rossmann, M.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.