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Volumn 270, Issue 2, 1997, Pages 238-246

Bivalent binding of a neutralising antibody to a calicivirus involves the torsional flexibility of the antibody hinge

Author keywords

Antibody flexibility; Cryo electron microscopy; mAB E3 RHDV; Virus neutralisation

Indexed keywords

MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY;

EID: 0030739033     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1095     Document Type: Article
Times cited : (73)

References (30)
  • 1
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientation of biological macromolecules imaged by cryoelectron microscopy
    • Baker T., Cheng R. H. A model-based approach for determining orientation of biological macromolecules imaged by cryoelectron microscopy. J Struct. Biol. 116:1996;120-130.
    • (1996) J Struct. Biol. , vol.116 , pp. 120-130
    • Baker, T.1    Cheng, R.H.2
  • 3
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R. A. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Phil. Trans. Roy. Soc. ser. B. 261:1971;221-230.
    • (1971) Phil. Trans. Roy. Soc. Ser. B. , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 4
    • 0014930077 scopus 로고
    • Three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R. A., Amos L. A., Finch J. T., De Rosier D. J., Klug A. Three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Nature. 226:1970a;421-425.
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    De Rosier, D.J.4    Klug, A.5
  • 5
    • 0014894609 scopus 로고
    • The reconstruction of three-dimensional structure from projections and its application to electron microscopy
    • Crowther R. A., De Rosier D. J., Klug A. The reconstruction of three-dimensional structure from projections and its application to electron microscopy. Phil. Trans. Roy. Soc. ser. A. 317:1970b;319-340.
    • (1970) Phil. Trans. Roy. Soc. Ser. A , vol.317 , pp. 319-340
    • Crowther, R.A.1    De Rosier, D.J.2    Klug, A.3
  • 6
    • 0023666171 scopus 로고
    • The T=4 envelope of Sindbis virus is organised by complementary interactions with a T=3 icosahedral capsid
    • Fuller S. D. The T=4 envelope of Sindbis virus is organised by complementary interactions with a T=3 icosahedral capsid. Cell. 48:1987;923-934.
    • (1987) Cell , vol.48 , pp. 923-934
    • Fuller, S.D.1
  • 7
    • 0029924120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of icosahedral particles. The uncommon line
    • Fuller S. D., Butcher S. J., Cheng R. H., Baker T. S. Three-dimensional reconstruction of icosahedral particles. The uncommon line. J. Struct. Biol. 116:1996;48-55.
    • (1996) J. Struct. Biol. , vol.116 , pp. 48-55
    • Fuller, S.D.1    Butcher, S.J.2    Cheng, R.H.3    Baker, T.S.4
  • 9
    • 0030007379 scopus 로고    scopus 로고
    • Structure of a neutralizing antibody bound bivalently to human rhinovirus 2
    • Hewat E. A., Blaas D. Structure of a neutralizing antibody bound bivalently to human rhinovirus 2. EMBO J. 15:1996;1515-1523.
    • (1996) EMBO J , vol.15 , pp. 1515-1523
    • Hewat, E.A.1    Blaas, D.2
  • 10
    • 0026719673 scopus 로고
    • Three dimensional reconstruction of baculovirus expressed bluetongue virus core-like particles by cryo-electron microscopy
    • Hewat E. A., Booth T. F., Loudon P. T., Roy P. Three dimensional reconstruction of baculovirus expressed bluetongue virus core-like particles by cryo-electron microscopy. Virology. 189:1992a;10-20.
    • (1992) Virology , vol.189 , pp. 10-20
    • Hewat, E.A.1    Booth, T.F.2    Loudon, P.T.3    Roy, P.4
  • 11
    • 0027008546 scopus 로고
    • Structure of bluetongue virus particles by cryoelectron microscopy
    • Hewat E. A., Booth T. F., Roy P. Structure of bluetongue virus particles by cryoelectron microscopy. J. Struct. Biol. 109:1992b;61-69.
    • (1992) J. Struct. Biol. , vol.109 , pp. 61-69
    • Hewat, E.A.1    Booth, T.F.2    Roy, P.3
  • 12
    • 8244249460 scopus 로고    scopus 로고
    • Structure of the complex of an Fab fragment of a neutralising antibody with foot-and-mouth disease virus: Positioning of a highly mobile antigenic loop
    • Hewat E. A., Verdaguer N., Fita I., Blakemore W., Brooks S., King A., Newman J., Domingo E., Mateu M. G., Stuart D. Structure of the complex of an Fab fragment of a neutralising antibody with foot-and-mouth disease virus: Positioning of a highly mobile antigenic loop. EMBO J. 16:1997;1492-1500.
    • (1997) EMBO J. , vol.16 , pp. 1492-1500
    • Hewat, E.A.1    Verdaguer, N.2    Fita, I.3    Blakemore, W.4    Brooks, S.5    King, A.6    Newman, J.7    Domingo, E.8    Mateu, M.G.9    Stuart, D.10
  • 13
    • 0017152608 scopus 로고
    • Crystallographic structure studies of an IgG molecule and an Fab fragment
    • Huber R., Deisenhofer J., Colman P. M., Matsushima M. Crystallographic structure studies of an IgG molecule and an Fab fragment. Nature. 264:1976;415-420.
    • (1976) Nature , vol.264 , pp. 415-420
    • Huber, R.1    Deisenhofer, J.2    Colman, P.M.3    Matsushima, M.4
  • 15
    • 0028122560 scopus 로고
    • Recombinant rabbit hemorrhagic disease virus capsid protein expressed in baculovirius self-assembles into virus like particles and induces protection
    • Laurent S., Vautherot J. F., Madelaine M. F., Le Gall G., Rasschaert D. Recombinant rabbit hemorrhagic disease virus capsid protein expressed in baculovirius self-assembles into virus like particles and induces protection. J. Virol. 68:1994;6794-6798.
    • (1994) J. Virol. , vol.68 , pp. 6794-6798
    • Laurent, S.1    Vautherot, J.F.2    Madelaine, M.F.3    Le Gall, G.4    Rasschaert, D.5
  • 16
    • 0028831563 scopus 로고
    • Self-assembly, antigenicity, and immunogenicity of the rabbit haemorrhagic disease virus (Czechoslovakian strain V-351) capsid protein expressed in baculovirus
    • Nagesha H. S., Wang L. F., Hyatt A. D., Morissy C. J., Lenghaus C., Westbury H. A. Self-assembly, antigenicity, and immunogenicity of the rabbit haemorrhagic disease virus (Czechoslovakian strain V-351) capsid protein expressed in baculovirus. Arch. Virol. 140:1995;1095-1108.
    • (1995) Arch. Virol. , vol.140 , pp. 1095-1108
    • Nagesha, H.S.1    Wang, L.F.2    Hyatt, A.D.3    Morissy, C.J.4    Lenghaus, C.5    Westbury, H.A.6
  • 17
    • 0027974229 scopus 로고
    • Direct imaging of interactions between an icosahedral virus and congugate Fab fragments by cryoelectron microscopy and X-ray crystallography
    • Porta C., Wang G., Cheng H., Chen Z., Baker T. S., Johnson J. E. Direct imaging of interactions between an icosahedral virus and congugate Fab fragments by cryoelectron microscopy and X-ray crystallography. Virology. 204:1994;777-788.
    • (1994) Virology , vol.204 , pp. 777-788
    • Porta, C.1    Wang, G.2    Cheng, H.3    Chen, Z.4    Baker, T.S.5    Johnson, J.E.6
  • 18
    • 0025178591 scopus 로고
    • Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy
    • Prasad B. V. V., Burns J. W., Marietta E., Estes M. K., Chiu W. Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy. Nature. 343:1990;476-479.
    • (1990) Nature , vol.343 , pp. 476-479
    • Prasad, B.V.V.1    Burns, J.W.2    Marietta, E.3    Estes, M.K.4    Chiu, W.5
  • 19
    • 0028321481 scopus 로고
    • Three dimensional structure of baculovirus-expressed Norwalk virus capsid
    • Prasad B. V. V., Rothnagel R., Jiang X., Estes M. K. Three dimensional structure of baculovirus-expressed Norwalk virus capsid. J. Virol. 68:1994a;5117-5125.
    • (1994) J. Virol. , vol.68 , pp. 5117-5125
    • Prasad, B.V.V.1    Rothnagel, R.2    Jiang, X.3    Estes, M.K.4
  • 20
    • 0028136813 scopus 로고
    • Three-dimensional structure of calicivirus
    • Prasad B. V. V., Matson D. O., Smith A. W. Three-dimensional structure of calicivirus. J. Mol. Biol. 240:1994b;256-264.
    • (1994) J. Mol. Biol. , vol.240 , pp. 256-264
    • Prasad, B.V.V.1    Matson, D.O.2    Smith, A.W.3
  • 21
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial envelope protein
    • Saxton W. O., Baumeister W. The correlation averaging of a regularly arranged bacterial envelope protein. J. Microscopy. 127:1982;127-138.
    • (1982) J. Microscopy , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 22
    • 0030465607 scopus 로고    scopus 로고
    • Adenovirus 3 penton dodecahedron exhibits structural changes of the base on fibre binding
    • Schoehn G., Fender P., Chroboczek J., Hewat E. A. Adenovirus 3 penton dodecahedron exhibits structural changes of the base on fibre binding. EMBO J. 15:1996;6841-6846.
    • (1996) EMBO J. , vol.15 , pp. 6841-6846
    • Schoehn, G.1    Fender, P.2    Chroboczek, J.3    Hewat, E.A.4
  • 23
    • 0027306163 scopus 로고
    • Structure of a human rhinovirus -bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility
    • Smith T. J., Olson N. H., Cheng R. H., Chase E. S., Baker T. S. Structure of a human rhinovirus -bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility. Proc. Natl Acad. Sci. USA. 90:1993a;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
  • 25
    • 0028304866 scopus 로고
    • Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein
    • Tormo J., Blaas D., Parry N. R., Rowlands D., Stuart D., Fita I. Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein. EMBO J. 13:1994;2247-2256.
    • (1994) EMBO J. , vol.13 , pp. 2247-2256
    • Tormo, J.1    Blaas, D.2    Parry, N.R.3    Rowlands, D.4    Stuart, D.5    Fita, I.6
  • 26
    • 0026490068 scopus 로고
    • Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid
    • Trus B. L., Newcomb W. W., Booy F. P., Brown J. C., Steven A. C. Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid. Proc. Natl Acad. Sci. USA. 89:1992;11508-11512.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 11508-11512
    • Trus, B.L.1    Newcomb, W.W.2    Booy, F.P.3    Brown, J.C.4    Steven, A.C.5
  • 27
    • 0026739013 scopus 로고
    • Bovine coronavirus peplomer glycoproteins: Detailed antigenic analyses of S1, S2, and HE
    • Vautherot J. F., Madelaine M. F., Boireau P., Laporte J. Bovine coronavirus peplomer glycoproteins: detailed antigenic analyses of S1, S2, and HE. J. Gen. Virol. 73:1992;1725-1737.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1725-1737
    • Vautherot, J.F.1    Madelaine, M.F.2    Boireau, P.3    Laporte, J.4
  • 28
    • 0024573950 scopus 로고
    • Concerning the axial rotational flexibility of IgG molecules
    • Wade R. H., Taveau J. C., Lamy J. N. Concerning the axial rotational flexibility of IgG molecules. J. Mol. Biol. 206:1989;349-356.
    • (1989) J. Mol. Biol. , vol.206 , pp. 349-356
    • Wade, R.H.1    Taveau, J.C.2    Lamy, J.N.3
  • 29
    • 0027121512 scopus 로고
    • Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X-ray crystallography
    • Wang G. J., Porta C., Chen Z. G., Baker T. S., Johnson J. E. Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X-ray crystallography. Nature. 355:1992;275-278.
    • (1992) Nature , vol.355 , pp. 275-278
    • Wang, G.J.1    Porta, C.2    Chen, Z.G.3    Baker, T.S.4    Johnson, J.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.