메뉴 건너뛰기




Volumn 82, Issue 5, 2008, Pages 2079-2088

Structure of antibody-neutralized murine norovirus and unexpected differences from viruslike particles

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; NEUTRALIZING ANTIBODY; PROTEIN VP1; PROTEIN VP2;

EID: 39749202900     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02200-07     Document Type: Article
Times cited : (81)

References (36)
  • 2
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker, T. S., and R. H. Cheng. 1996. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116:120-130.
    • (1996) J. Struct. Biol , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 3
    • 17044373783 scopus 로고    scopus 로고
    • The structure of the poliovirus 135S cell entry intermediate at 10-Angstrom resolution reveals the location of an externalized polypeptide that binds to membranes
    • Bubeck, D., D. J. Filman, N. Cheng, A. C. Steven, J. M. Hogle, and D. M. Belnap. 2005. The structure of the poliovirus 135S cell entry intermediate at 10-Angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. J. Virol. 79:7745-7755.
    • (2005) J. Virol , vol.79 , pp. 7745-7755
    • Bubeck, D.1    Filman, D.J.2    Cheng, N.3    Steven, A.C.4    Hogle, J.M.5    Belnap, D.M.6
  • 4
    • 0034625320 scopus 로고    scopus 로고
    • Large conformational changes in the maturation of a simple RNA virus, nudaurelia capensis omega virus (NomegaV)
    • Canady, M. A., M. Tihova, T. N. Hanzlik, J. E. Johnson, and M. Yeager. 2000. Large conformational changes in the maturation of a simple RNA virus, nudaurelia capensis omega virus (NomegaV). J. Mol. Biol. 299:573-584.
    • (2000) J. Mol. Biol , vol.299 , pp. 573-584
    • Canady, M.A.1    Tihova, M.2    Hanzlik, T.N.3    Johnson, J.E.4    Yeager, M.5
  • 5
    • 0031902570 scopus 로고    scopus 로고
    • Antibody-mediated neutralization of human rhinovirus 14 explored by means of cryo-electron microscopy and X-ray crystallography of virus-Fab complexes
    • Che, Z., N. H. Olson, D. Leippe, W.-M. Lee, A. Mosser, R. R. Rueckert, T. S. Baker, and T. J. Smith. 1998. Antibody-mediated neutralization of human rhinovirus 14 explored by means of cryo-electron 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.5    Rueckert, R.R.6    Baker, T.S.7    Smith, T.J.8
  • 6
    • 33744494819 scopus 로고    scopus 로고
    • X-ray structure of a native calicivirus: Structural insights into antigenic diversity and host specificity
    • Chen, R., J. D. Neill, M. K. Estes, and B. V. V. Prasad. 2006. X-ray structure of a native calicivirus: structural insights into antigenic diversity and host specificity. Proc. Natl. Acad. Sci. USA 103:8048-8053.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8048-8053
    • Chen, R.1    Neill, J.D.2    Estes, M.K.3    Prasad, B.V.V.4
  • 7
    • 2642539948 scopus 로고    scopus 로고
    • Inter- and intragenus structural variations in caliciviruses and their functional implications
    • Chen, R., J. D. Neill, J. S. Noel, A. M. Hutson, R. I. Glass, M. K. Estes, and B. V. V. Prasad. 2004. Inter- and intragenus structural variations in caliciviruses and their functional implications. J. Virol. 78:6469-6479.
    • (2004) J. Virol , vol.78 , pp. 6469-6479
    • Chen, R.1    Neill, J.D.2    Noel, J.S.3    Hutson, A.M.4    Glass, R.I.5    Estes, M.K.6    Prasad, B.V.V.7
  • 8
    • 0037292503 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of San Miguel sea lion virus: An animal calicivirus
    • Chen, R., J. D. Neill, and B. V. V. Prasad. 2003. Crystallization and preliminary crystallographic analysis of San Miguel sea lion virus: an animal calicivirus. J. Struct. Biol. 141:143-148.
    • (2003) J. Struct. Biol , vol.141 , pp. 143-148
    • Chen, R.1    Neill, J.D.2    Prasad, B.V.V.3
  • 9
    • 0031017971 scopus 로고    scopus 로고
    • The molecular biology of caliciviruses
    • Clarke, I. N., and P. R. Lambden. 1997. The molecular biology of caliciviruses. J. Gen. Virol. 78:291-301.
    • (1997) J. Gen. Virol , vol.78 , pp. 291-301
    • Clarke, I.N.1    Lambden, P.R.2
  • 10
    • 0024496565 scopus 로고
    • Inhibition of rhinovirus attachment by neutralizing monoclonal antibodies and their Fab fragments
    • Colonno, R. J., P. L. Callahan, D. M. Leippe, and R. R. Rueckert. 1989. Inhibition of rhinovirus attachment by neutralizing monoclonal antibodies and their Fab fragments. J. Virol. 63:36-42.
    • (1989) J. Virol , vol.63 , pp. 36-42
    • Colonno, R.J.1    Callahan, P.L.2    Leippe, D.M.3    Rueckert, R.R.4
  • 11
    • 0028847173 scopus 로고
    • Proteolytic and conformational control of virus capsid maturation: The bacteriophage HK97 system
    • Conway, J. F., R. L. Duda, N. Cheng, R. W. Hendrix, and A. C. Steven. 1995. Proteolytic and conformational control of virus capsid maturation: the bacteriophage HK97 system. J. Mol. Biol. 253:86-99.
    • (1995) J. Mol. Biol , vol.253 , pp. 86-99
    • Conway, J.F.1    Duda, R.L.2    Cheng, N.3    Hendrix, R.W.4    Steven, A.C.5
  • 12
    • 0033372028 scopus 로고    scopus 로고
    • Methods for reconstructing density maps of 'single' particles from cryoelectron micrographs to subnanometer resolution
    • Conway, J. F., and J. M. Steven. 1999. Methods for reconstructing density maps of 'single' particles from cryoelectron micrographs to subnanometer resolution. J. Struct. Biol. 128:106-118.
    • (1999) J. Struct. Biol , vol.128 , pp. 106-118
    • Conway, J.F.1    Steven, J.M.2
  • 13
  • 14
    • 0014930077 scopus 로고
    • Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther, R. A., L. A. Amos, J. T. Finch, D. J. De Rosier, and A. Klug. 1970. Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs. Nature 226:421-425.
    • (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
  • 16
    • 0027162058 scopus 로고
    • Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: Analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction
    • Dryden, K. A., G. Wang, M. Yeager, M. L. Nibert, K. M. Coombs, D. B. Furlong, B. N. Fields, and T. S. Baker. 1993. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J. Cell Biol. 122:1023-1041.
    • (1993) J. Cell Biol , vol.122 , pp. 1023-1041
    • Dryden, K.A.1    Wang, G.2    Yeager, M.3    Nibert, M.L.4    Coombs, K.M.5    Furlong, D.B.6    Fields, B.N.7    Baker, T.S.8
  • 17
    • 0027240069 scopus 로고
    • Comparison of the reactivities of baculovirus-expressed recombinant Norwalk virus capsid antigen with those of the native Norwalk virus antigen in serologic assays and some epidemiologic observations
    • Green, K. Y., J. F. Lew, X. Jiang, A. Z. Kapikian, and M. K. Estes. 1993. Comparison of the reactivities of baculovirus-expressed recombinant Norwalk virus capsid antigen with those of the native Norwalk virus antigen in serologic assays and some epidemiologic observations. J. Clin. Microbiol. 31:2185-2191.
    • (1993) J. Clin. Microbiol , vol.31 , pp. 2185-2191
    • Green, K.Y.1    Lew, J.F.2    Jiang, X.3    Kapikian, A.Z.4    Estes, M.K.5
  • 19
    • 0035783171 scopus 로고    scopus 로고
    • Bsoft: Image and molecular processing in electron microscopy
    • Heymann, J. B. 2001. Bsoft: image and molecular processing in electron microscopy. J. Struct. Biol. 133:156-169.
    • (2001) J. Struct. Biol , vol.133 , pp. 156-169
    • Heymann, J.B.1
  • 20
    • 0027295302 scopus 로고
    • Sequence and genomic organization of Norwalk virus
    • Jiang, X., M. Wang, K. Wang, and M. K. Estes. 1993. Sequence and genomic organization of Norwalk virus. Virology 195:51-61.
    • (1993) Virology , vol.195 , pp. 51-61
    • Jiang, X.1    Wang, M.2    Wang, K.3    Estes, M.K.4
  • 22
    • 34249948004 scopus 로고    scopus 로고
    • Pocket factors unlikely play a major role in the life cycle of human rhinovirus
    • Katpally, U., and T. J. Smith. 2007. Pocket factors unlikely play a major role in the life cycle of human rhinovirus. J. Virol. 81:6307-6315.
    • (2007) J. Virol , vol.81 , pp. 6307-6315
    • Katpally, U.1    Smith, T.J.2
  • 23
    • 36048986725 scopus 로고    scopus 로고
    • A single amino acid substitution in the P2 domain of VP1 of murine norovirus is sufficient for escape from antibody neutralization
    • Lochridge, V. P., and M. E. Hardy. 2007. A single amino acid substitution in the P2 domain of VP1 of murine norovirus is sufficient for escape from antibody neutralization. J. Virol. 81:12316-12322.
    • (2007) J. Virol , vol.81 , pp. 12316-12322
    • Lochridge, V.P.1    Hardy, M.E.2
  • 27
    • 0028136813 scopus 로고
    • Three-dimensional structure of calicivirus
    • Prasad, B. V., D. O. Matson, and A. W. Smith. 1994. Three-dimensional structure of calicivirus. J. Mol. Biol. 240:256-264.
    • (1994) J. Mol. Biol , vol.240 , pp. 256-264
    • Prasad, B.V.1    Matson, D.O.2    Smith, A.W.3
  • 28
    • 0034123117 scopus 로고    scopus 로고
    • Structural studies of recombinant Norwalk capsids
    • Prasad, B. V. V., M. E. Hardy, and M. K. Estes. 2000. Structural studies of recombinant Norwalk capsids. J. Infect. Dis. 181:S317-S321.
    • (2000) J. Infect. Dis , vol.181
    • Prasad, B.V.V.1    Hardy, M.E.2    Estes, M.K.3
  • 29
    • 0041323243 scopus 로고    scopus 로고
    • Structural studies on antibody-virus complexes
    • Smith, T. J. 2003. Structural studies on antibody-virus complexes. Adv. Protein Chem. 64:409-443.
    • (2003) Adv. Protein Chem , vol.64 , pp. 409-443
    • Smith, T.J.1
  • 30
    • 0027306163 scopus 로고
    • Structure of a human rhinovirus-bivalently bound antibody complex: Implications for virus 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 virus 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
  • 31
    • 0023194972 scopus 로고
    • Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle
    • Sturzenbecker, L. J., M. Nibert, D. Furlong, and B. N. Fields. 1987. Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle. J. Virol. 61:2351-2361.
    • (1987) J. Virol , vol.61 , pp. 2351-2361
    • Sturzenbecker, L.J.1    Nibert, M.2    Furlong, D.3    Fields, B.N.4
  • 32
    • 0030739033 scopus 로고    scopus 로고
    • Bivalent binding of a neutralizing antibody to a calicivirus involves the torsional flexibility of the antibody hinge
    • Thouvenin, E., S. Laurent, M.-F. Madelaine, D. Rasschaert, J.-F. Vautherot, and E. A. Hewat. 1997. Bivalent binding of a neutralizing antibody to a calicivirus involves the torsional flexibility of the antibody hinge. J. Mol. Biol. 270:238-246.
    • (1997) J. Mol. Biol , vol.270 , pp. 238-246
    • Thouvenin, E.1    Laurent, S.2    Madelaine, M.-F.3    Rasschaert, D.4    Vautherot, J.-F.5    Hewat, E.A.6
  • 34
    • 0029843157 scopus 로고    scopus 로고
    • Attachment and entry of recombinant Norwalk virus capsids to cultured human and animal cell lines
    • White, L. J., J. M. Ball, M. E. Hardy, T. N. Tanaka, N. Kitamoto, and M. K. Estes. 1996. Attachment and entry of recombinant Norwalk virus capsids to cultured human and animal cell lines. J. Virol. 70:6589-6597.
    • (1996) J. Virol , vol.70 , pp. 6589-6597
    • White, L.J.1    Ball, J.M.2    Hardy, M.E.3    Tanaka, T.N.4    Kitamoto, N.5    Estes, M.K.6
  • 35
    • 32544460955 scopus 로고    scopus 로고
    • Time-resolved molecular dynamics of bacteriophage HK97 capsid maturation interpreted by electron cryo-microscopy and X-ray crystallography
    • Wikoff, W. R., J. F. Conway, J. Tang, K. K. Lee, L. Gan, N. Cheng, R. L. Duda, R. W. Hendrix, A. C. Steven, and J. E. Johnson. 2006. Time-resolved molecular dynamics of bacteriophage HK97 capsid maturation interpreted by electron cryo-microscopy and X-ray crystallography. J. Struct. Biol. 153:300-306.
    • (2006) J. Struct. Biol , vol.153 , pp. 300-306
    • Wikoff, W.R.1    Conway, J.F.2    Tang, J.3    Lee, K.K.4    Gan, L.5    Cheng, N.6    Duda, R.L.7    Hendrix, R.W.8    Steven, A.C.9    Johnson, J.E.10
  • 36
    • 20044387761 scopus 로고    scopus 로고
    • Wobus, C. E., S. M. Karst, L. B. Thackray, K.-O. Chang, S. V. Sosnovtsev, G. Belliot, A. Krug, J. M. Mackensie, K. Y. Green, and H. W. Virgin IV. 2004. Replication of norovirus in cell culture reveals a tropism for dendritic cells and macrophages. PLoS Biol. 2:e432.
    • Wobus, C. E., S. M. Karst, L. B. Thackray, K.-O. Chang, S. V. Sosnovtsev, G. Belliot, A. Krug, J. M. Mackensie, K. Y. Green, and H. W. Virgin IV. 2004. Replication of norovirus in cell culture reveals a tropism for dendritic cells and macrophages. PLoS Biol. 2:e432.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.