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Volumn 437, Issue 7059, 2005, Pages 764-769

Structural basis of West Nile virus neutralization by a therapeutic antibody

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; BIOLOGICAL MEMBRANES; CATALYSIS; CONFORMATIONS; IMMUNOLOGY;

EID: 26944454471     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature03956     Document Type: Article
Times cited : (309)

References (30)
  • 1
    • 4344647820 scopus 로고    scopus 로고
    • West Nile virus: Where are we now?
    • Granwehr, B. P. et al. West Nile virus: where are we now? Lancet Infect. Dis. 4, 547-556 (2004).
    • (2004) Lancet Infect. Dis. , vol.4 , pp. 547-556
    • Granwehr, B.P.1
  • 2
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
    • Bressanelli, S. et al. Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J. 23, 728-738 (2004).
    • (2004) EMBO J. , vol.23 , pp. 728-738
    • Bressanelli, S.1
  • 3
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis, Y., Ogata, S., Clements, D. & Harrison, S. C. Structure of the dengue virus envelope protein after membrane fusion. Nature 427, 313-319 (2004).
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 5
    • 0141925650 scopus 로고    scopus 로고
    • Innate and adaptive immune responses determine protection against disseminated infection by West Nile encephalitis virus
    • Diamond, M. S., Shrestha, B., Mehlhop, E., Sitati, E. & Engle, M. Innate and adaptive immune responses determine protection against disseminated infection by West Nile encephalitis virus. Viral Immunol. 16, 259-278 (2003).
    • (2003) Viral Immunol. , vol.16 , pp. 259-278
    • Diamond, M.S.1    Shrestha, B.2    Mehlhop, E.3    Sitati, E.4    Engle, M.5
  • 6
    • 3042854213 scopus 로고    scopus 로고
    • Immunity to West Nile virus
    • Wang, T. & Fikrig, E. Immunity to West Nile virus. Curr. Opin. Immunol. 16, 519-523 (2004).
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 519-523
    • Wang, T.1    Fikrig, E.2
  • 8
    • 21044448356 scopus 로고    scopus 로고
    • Development of a humanized monoclonal antibody with therapeutic potential against West Nile virus
    • Oliphant, T. et al. Development of a humanized monoclonal antibody with therapeutic potential against West Nile virus. Nature Med. 11, 522-530 (2005).
    • (2005) Nature Med. , vol.11 , pp. 522-530
    • Oliphant, T.1
  • 9
    • 0036420965 scopus 로고    scopus 로고
    • Molecular recognition in antibody-antigen complexes
    • Sundberg, E. J. & Mariuzza, R. A. Molecular recognition in antibody-antigen complexes. Adv. Protein Chem. 61, 119-160 (2002).
    • (2002) Adv. Protein Chem. , vol.61 , pp. 119-160
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 10
    • 4344589735 scopus 로고    scopus 로고
    • Fine epitope mapping of antiepidermal growth factor receptor antibodies through random mutagenesis and yeast surface display
    • Chao, G., Cochran, J. R. & Wittrup, K. D. Fine epitope mapping of antiepidermal growth factor receptor antibodies through random mutagenesis and yeast surface display. J. Mol. Biol. 342, 539-550 (2004).
    • (2004) J. Mol. Biol. , vol.342 , pp. 539-550
    • Chao, G.1    Cochran, J.R.2    Wittrup, K.D.3
  • 11
    • 0242580241 scopus 로고    scopus 로고
    • Structural basis of a flavivirus recognized by its neutralizing antibody: Solution structure of the domain III of the Japanese Encephalitis virus envelope protein
    • Wu, K. P. et al. Structural basis of a flavivirus recognized by its neutralizing antibody: Solution structure of the domain III of the Japanese Encephalitis virus envelope protein. J. Biol. Chem. 278, 46007-46013 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 46007-46013
    • Wu, K.P.1
  • 12
    • 4644372800 scopus 로고    scopus 로고
    • Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus
    • Volk, D. E. et al. Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus. J. Biol. Chem. 279, 38755-38761 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 38755-38761
    • Volk, D.E.1
  • 13
    • 0030588217 scopus 로고    scopus 로고
    • Mutational analysis of a neutralization epitope on the dengue type 2 virus (DEN2) envelope protein: Monoclonal antibody resistant DEN2/DEN4 chimeras exhibit reduced mouse neurovirulence
    • Hiramatsu, K., Tadano, M., Men, R. & Lai, C. J. Mutational analysis of a neutralization epitope on the dengue type 2 virus (DEN2) envelope protein: monoclonal antibody resistant DEN2/DEN4 chimeras exhibit reduced mouse neurovirulence. Virology 224, 437-445 (1996).
    • (1996) Virology , vol.224 , pp. 437-445
    • Hiramatsu, K.1    Tadano, M.2    Men, R.3    Lai, C.J.4
  • 14
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis, Y., Ogata, S., Clements, D. & Harrison, S. C. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc. Natl Acad. Sci. USA 100, 6986-6991 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 15
    • 17944380435 scopus 로고    scopus 로고
    • Crystal structure of a neutralizing human IgG against HIV-1: A template for vaccine design
    • Saphire, E. O. et al. Crystal structure of a neutralizing human IgG against HIV-1: a template for vaccine design. Science 293, 1155-1159 (2001).
    • (2001) Science , vol.293 , pp. 1155-1159
    • Saphire, E.O.1
  • 16
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion
    • Kuhn, R. J. et al. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108, 717-725 (2002).
    • (2002) Cell , vol.108 , pp. 717-725
    • Kuhn, R.J.1
  • 17
    • 0032493679 scopus 로고    scopus 로고
    • Two antibodies that neutralize papillomavirus by different mechanisms show distinct binding patterns at 13 Å resolution
    • Booy, F. P., Roden, R. B., Greenstone, H. L., Schiller, J. T. & Trus, B. L. Two antibodies that neutralize papillomavirus by different mechanisms show distinct binding patterns at 13 Å resolution. J. Mol. Biol. 281, 95-106 (1998).
    • (1998) J. Mol. Biol. , vol.281 , pp. 95-106
    • Booy, F.P.1    Roden, R.B.2    Greenstone, H.L.3    Schiller, J.T.4    Trus, B.L.5
  • 18
    • 0037319970 scopus 로고    scopus 로고
    • B cells and antibody play critical roles in the immediate defense of disseminated infection by West Nile encephalitis virus
    • Diamond, M. S., Shrestha, B., Marri, A., Mahan, D. & Engle, M. B cells and antibody play critical roles in the immediate defense of disseminated infection by West Nile encephalitis virus. J. Virol. 77, 2578-2586 (2003).
    • (2003) J. Virol. , vol.77 , pp. 2578-2586
    • Diamond, M.S.1    Shrestha, B.2    Marri, A.3    Mahan, D.4    Engle, M.5
  • 19
    • 0034899311 scopus 로고    scopus 로고
    • Monoclonal antibodies that bind to domain III of dengue virus e glycoprotein are the most efficient blockers of virus adsorption to Vero cells
    • Crill, W. D. & Roehrig, J. T. Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J. Virol. 75, 7769-7773 (2001).
    • (2001) J. Virol. , vol.75 , pp. 7769-7773
    • Crill, W.D.1    Roehrig, J.T.2
  • 20
    • 0033602564 scopus 로고    scopus 로고
    • Analysis of the steps involved in Dengue virus entry into host cells
    • Hung, S. L. et al. Analysis of the steps involved in Dengue virus entry into host cells. Virology 257, 156-167 (1999).
    • (1999) Virology , vol.257 , pp. 156-167
    • Hung, S.L.1
  • 21
    • 0017346381 scopus 로고
    • Antibody-enhanced dengue virus infection in primate leukocytes
    • Halstead, S. B. & O'Rourke, E. J. Antibody-enhanced dengue virus infection in primate leukocytes. Nature 265, 739-741 (1977).
    • (1977) Nature , vol.265 , pp. 739-741
    • Halstead, S.B.1    O'Rourke, E.J.2
  • 22
    • 0022450456 scopus 로고
    • A new mechanism for the neutralization of enveloped viruses by antiviral antibody
    • Gollins, S. W. & Porterfield, J. S. A new mechanism for the neutralization of enveloped viruses by antiviral antibody. Nature 321, 244-246 (1986).
    • (1986) Nature , vol.321 , pp. 244-246
    • Gollins, S.W.1    Porterfield, J.S.2
  • 23
    • 1542615646 scopus 로고    scopus 로고
    • Identifying epitopes of HIV-1 that induce protective antibodies
    • Zolla-Pazner, S. Identifying epitopes of HIV-1 that induce protective antibodies. Nature Rev. Immunol. 4, 199-210 (2004).
    • (2004) Nature Rev. Immunol. , vol.4 , pp. 199-210
    • Zolla-Pazner, S.1
  • 24
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J. & Wiley, D. C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69, 531-569 (2000).
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 26
    • 0030764559 scopus 로고    scopus 로고
    • Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate
    • Chen, Y. et al. Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate. Nature Med. 3, 866-871 (1997).
    • (1997) Nature Med. , vol.3 , pp. 866-871
    • Chen, Y.1
  • 27
    • 0344642934 scopus 로고    scopus 로고
    • DC-SIGN (CD209) mediates dengue virus infection of human dendritic cells
    • Tassaneetrithep, B. et al. DC-SIGN (CD209) mediates dengue virus infection of human dendritic cells. J. Exp. Med. 197, 823-829 (2003).
    • (2003) J. Exp. Med. , vol.197 , pp. 823-829
    • Tassaneetrithep, B.1
  • 28
    • 0642287817 scopus 로고    scopus 로고
    • Neutralization and antibody-dependent enhancement of dengue viruses
    • Halstead, S. B. Neutralization and antibody-dependent enhancement of dengue viruses. Adv. Virus Res. 60, 421-467 (2003).
    • (2003) Adv. Virus Res. , vol.60 , pp. 421-467
    • Halstead, S.B.1
  • 29
    • 18944391706 scopus 로고    scopus 로고
    • Two dimensional VOPBA reveals laminin receptor (LAMRI) interaction with dengue virus serotypes 1, 2 and 3
    • Tio, P. H., Jong, W. W. & Cardosa, M. J. Two dimensional VOPBA reveals laminin receptor (LAMRI) interaction with dengue virus serotypes 1, 2 and 3. Virol. J. 2, 25 (2005).
    • (2005) Virol. J. , vol.2 , pp. 25
    • Tio, P.H.1    Jong, W.W.2    Cardosa, M.J.3
  • 30
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.