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Volumn 107, Issue 44, 2010, Pages 18950-18955

Neutralization of West Nile virus by cross-linking of its surface proteins with Fab fragments of the human monoclonal antibody CR4354

Author keywords

Antibody; Cryoelectron microscopy; Flavivirus

Indexed keywords

CR 4354; EPITOPE; GLYCOPROTEIN; HOMODIMER; MONOCLONAL ANTIBODY; MONOMER; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 78650495030     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1011036107     Document Type: Article
Times cited : (116)

References (45)
  • 1
    • 55049096521 scopus 로고    scopus 로고
    • West Nile virus in the Americas
    • Petersen LR, Hayes EB (2008) West Nile virus in the Americas. Med Clin North Am 92: 1307-1322, ix.
    • (2008) Med Clin North Am , vol.92 , Issue.1307-1322 , pp. 9
    • Petersen, L.R.1    Hayes, E.B.2
  • 2
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey FA, Heinz FX, Mandl C, Kunz C, Harrison SC (1995) The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375:291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 3
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis Y, Ogata S, Clements D, Harrison SC (2003) A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc Natl Acad Sci USA 100:6986-6991.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 5
    • 33750744140 scopus 로고    scopus 로고
    • Crystal structure of West Nile virus envelope glycoprotein reveals viral surface epitopes
    • Kanai R, et al. (2006) Crystal structure of West Nile virus envelope glycoprotein reveals viral surface epitopes. J Virol 80:11000-11008.
    • (2006) J Virol , vol.80 , pp. 11000-11008
    • Kanai, R.1
  • 6
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis Y, Ogata S, Clements D, Harrison SC (2004) Structure of the dengue virus envelope protein after membrane fusion. Nature 427:313-319.
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 7
    • 0035088293 scopus 로고    scopus 로고
    • Biophysical characterization and vector-specific antagonist activity of domain III of the tick-borne flavivirus envelope protein
    • Bhardwaj S, Holbrook M, Shope RE, Barrett AD, Watowich SJ (2001) Biophysical characterization and vector-specific antagonist activity of domain III of the tick-borne flavivirus envelope protein. J Virol 75:4002-4007.
    • (2001) J Virol , vol.75 , pp. 4002-4007
    • Bhardwaj, S.1    Holbrook, M.2    Shope, R.E.3    Barrett, A.D.4    Watowich, S.J.5
  • 8
    • 1542466884 scopus 로고    scopus 로고
    • Flavivirus structure and membrane fusion
    • Heinz FX, Allison SL (2003) Flavivirus structure and membrane fusion. Adv Virus Res 59:63-97.
    • (2003) Adv Virus Res , vol.59 , pp. 63-97
    • Heinz, F.X.1    Allison, S.L.2
  • 9
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its low-pHinduced membrane fusion conformation
    • Bressanelli S, et al. (2004) Structure of a flavivirus envelope glycoprotein in its low-pHinduced membrane fusion conformation. EMBO J 23:728-738.
    • (2004) EMBO J , vol.23 , pp. 728-738
    • Bressanelli, S.1
  • 10
    • 0347626038 scopus 로고    scopus 로고
    • An external loop region of domain III of dengue virus type 2 envelope protein is involved in serotype-specific binding to mosquito but not mammalian cells
    • Hung JJ, et al. (2004) An external loop region of domain III of dengue virus type 2 envelope protein is involved in serotype-specific binding to mosquito but not mammalian cells. J Virol 78:378-388.
    • (2004) J Virol , vol.78 , pp. 378-388
    • Hung, J.J.1
  • 11
    • 13644262812 scopus 로고    scopus 로고
    • Inhibition of West Nile virus entry by using a recombinant domain III from the envelope glycoprotein
    • Chu JJ, et al. (2005) Inhibition of West Nile virus entry by using a recombinant domain III from the envelope glycoprotein. J Gen Virol 86:405-412.
    • (2005) J Gen Virol , vol.86 , pp. 405-412
    • Chu, J.J.1
  • 12
    • 33644973069 scopus 로고    scopus 로고
    • Quantifying the specific binding between West Nile virus envelope domain III protein and the cellular receptor alphaVbeta3 integrin
    • Lee JW, Chu JJ, Ng ML (2006) Quantifying the specific binding between West Nile virus envelope domain III protein and the cellular receptor alphaVbeta3 integrin. J Biol Chem 281:1352-1360.
    • (2006) J Biol Chem , vol.281 , pp. 1352-1360
    • Lee, J.W.1    Chu, J.J.2    Ng, M.L.3
  • 13
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion
    • Kuhn RJ, et al. (2002) Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion. Cell 108:717-725.
    • (2002) Cell , vol.108 , pp. 717-725
    • Kuhn, R.J.1
  • 14
    • 50849120046 scopus 로고    scopus 로고
    • Structural insights into the mechanisms of antibody-mediated neutralization of flavivirus infection: Implications for vaccine development
    • Pierson TC, Fremont DH, Kuhn RJ, Diamond MS (2008) Structural insights into the mechanisms of antibody-mediated neutralization of flavivirus infection: Implications for vaccine development. Cell Host Microbe 4:229-238.
    • (2008) Cell Host Microbe , vol.4 , pp. 229-238
    • Pierson, T.C.1    Fremont, D.H.2    Kuhn, R.J.3    Diamond, M.S.4
  • 15
    • 63849262694 scopus 로고    scopus 로고
    • The host immunologic response to West Nile encephalitis virus
    • Diamond MS, Mehlhop E, Oliphant T, Samuel MA (2009) The host immunologic response to West Nile encephalitis virus. Front Biosci 14:3024-3034.
    • (2009) Front Biosci , vol.14 , pp. 3024-3034
    • Diamond, M.S.1    Mehlhop, E.2    Oliphant, T.3    Samuel, M.A.4
  • 16
    • 1542466883 scopus 로고    scopus 로고
    • Antigenic structure of flavivirus proteins
    • Roehrig JT (2003) Antigenic structure of flavivirus proteins. Adv Virus Res 59:141-175.
    • (2003) Adv Virus Res , vol.59 , pp. 141-175
    • Roehrig, J.T.1
  • 17
    • 0036891872 scopus 로고    scopus 로고
    • Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein
    • Beasley DW, Barrett AD (2002) Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein. J Virol 76:13097-13100.
    • (2002) J Virol , vol.76 , pp. 13097-13100
    • Beasley, D.W.1    Barrett, A.D.2
  • 18
    • 21044448356 scopus 로고    scopus 로고
    • Development of a humanized monoclonal antibody with therapeutic potential against West Nile virus
    • Oliphant T, et al. (2005) Development of a humanized monoclonal antibody with therapeutic potential against West Nile virus. Nat Med 11:522-530.
    • (2005) Nat Med , vol.11 , pp. 522-530
    • Oliphant, T.1
  • 19
    • 18044396710 scopus 로고    scopus 로고
    • Characterization of neutralizing antibodies to West Nile virus
    • Sánchez MD, et al. (2005) Characterization of neutralizing antibodies to West Nile virus. Virology 336:70-82.
    • (2005) Virology , vol.336 , pp. 70-82
    • Sánchez, M.D.1
  • 20
    • 35449004580 scopus 로고    scopus 로고
    • Induction of epitope-specific neutralizing antibodies against West Nile virus
    • Oliphant T, et al. (2007) Induction of epitope-specific neutralizing antibodies against West Nile virus. J Virol 81:11828-11839.
    • (2007) J Virol , vol.81 , pp. 11828-11839
    • Oliphant, T.1
  • 21
    • 67449096209 scopus 로고    scopus 로고
    • Human monoclonal antibodies against West Nile virus induced by natural infection neutralize at a postattachment step
    • Vogt MR, et al. (2009) Human monoclonal antibodies against West Nile virus induced by natural infection neutralize at a postattachment step. J Virol 83:6494-6507.
    • (2009) J Virol , vol.83 , pp. 6494-6507
    • Vogt, M.R.1
  • 22
    • 40949161794 scopus 로고    scopus 로고
    • Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins
    • Lok SM, et al. (2008) Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins. Nat Struct Mol Biol 15:312-317.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 312-317
    • Lok, S.M.1
  • 23
    • 0026679890 scopus 로고
    • The three-dimensional structure of an intact monoclonal antibody for canine lymphoma
    • Harris LJ, et al. (1992) The three-dimensional structure of an intact monoclonal antibody for canine lymphoma. Nature 360:369-372.
    • (1992) Nature , vol.360 , pp. 369-372
    • Harris, L.J.1
  • 24
    • 0028798103 scopus 로고
    • Intramolecular signaling upon complexation
    • Guddat LW, et al. (1995) Intramolecular signaling upon complexation. FASEB J 9: 101-106.
    • (1995) FASEB J , vol.9 , pp. 101-106
    • Guddat, L.W.1
  • 25
    • 0036304632 scopus 로고    scopus 로고
    • Contrasting IgG structures reveal extreme asymmetry and flexibility
    • Saphire EO, et al. (2002) Contrasting IgG structures reveal extreme asymmetry and flexibility. J Mol Biol 319:9-18.
    • (2002) J Mol Biol , vol.319 , pp. 9-18
    • Saphire, E.O.1
  • 26
    • 33645049294 scopus 로고    scopus 로고
    • Antibody elbow angles are influenced by their light chain class
    • Stanfield RL, Zemla A,Wilson IA, Rupp B (2006) Antibody elbow angles are influenced by their light chain class. J Mol Biol 357:1566-1574.
    • (2006) J Mol Biol , vol.357 , pp. 1566-1574
    • Stanfield, R.L.1    Zemla A.Wilson., I.A.2    Rupp, B.3
  • 27
    • 33747607044 scopus 로고    scopus 로고
    • West Nile virus in complex with the Fab fragment of a neutralizing monoclonal antibody
    • Kaufmann B, et al. (2006) West Nile virus in complex with the Fab fragment of a neutralizing monoclonal antibody. Proc Natl Acad Sci USA 103:12400-12404.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12400-12404
    • Kaufmann, B.1
  • 30
    • 0035265843 scopus 로고    scopus 로고
    • Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus
    • Ferlenghi I, et al. (2001) Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus. Mol Cell 7:593-602.
    • (2001) Mol Cell , vol.7 , pp. 593-602
    • Ferlenghi, I.1
  • 31
    • 73549095327 scopus 로고    scopus 로고
    • Capturing a flavivirus pre-fusion intermediate
    • Kaufmann B, et al. (2009) Capturing a flavivirus pre-fusion intermediate. PLoS Pathog 5:e1000672.
    • (2009) PLoS Pathog , vol.5
    • Kaufmann, B.1
  • 32
    • 4444338894 scopus 로고    scopus 로고
    • Conformational changes of the flavivirus E glycoprotein
    • Zhang Y, et al. (2004) Conformational changes of the flavivirus E glycoprotein. Structure 12:1607-1618.
    • (2004) Structure , vol.12 , pp. 1607-1618
    • Zhang, Y.1
  • 33
    • 33745767275 scopus 로고    scopus 로고
    • Isolation and characterization of human monoclonal antibodies from individuals infected with West Nile Virus
    • Throsby M, et al. (2006) Isolation and characterization of human monoclonal antibodies from individuals infected with West Nile Virus. J Virol 80:6982-6992.
    • (2006) J Virol , vol.80 , pp. 6982-6992
    • Throsby, M.1
  • 34
    • 0034717212 scopus 로고    scopus 로고
    • Functional human monoclonal antibodies of all isotypes constructed from phage display library-derived single-chain Fv antibody fragments
    • Boel E, et al. (2000) Functional human monoclonal antibodies of all isotypes constructed from phage display library-derived single-chain Fv antibody fragments. J Immunol Methods 239:153-166.
    • (2000) J Immunol Methods , vol.239 , pp. 153-166
    • Boel, E.1
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • eds Carter Jr, CW, Sweet RM (Academic, New York)
    • Otwinowski Z, Minor W, CharlesWC(1997) Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology: Macromolecular Crystallography, Part A, eds Carter Jr, CW, Sweet RM (Academic, New York), Vol 276, pp 307-326.
    • (1997) Methods in Enzymology: Macromolecular Crystallography, Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2    Charles, W.C.3
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 37
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58:1948-1954.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 38
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66:213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 39
  • 41
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for highresolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for highresolution single-particle reconstructions. J Struct Biol 128:82-97.
    • (1999) J Struct Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 42
    • 33845338800 scopus 로고    scopus 로고
    • AUTO3DEM - An automated and high throughput program for image reconstruction of icosahedral particles
    • Yan X, Sinkovits RS, Baker TS (2007) AUTO3DEM - an automated and high throughput program for image reconstruction of icosahedral particles. J Struct Biol 157:73-82.
    • (2007) J Struct Biol , vol.157 , pp. 73-82
    • Yan, X.1    Sinkovits, R.S.2    Baker, T.S.3
  • 43
    • 0035783056 scopus 로고    scopus 로고
    • Combining electron microscopic with x-ray crystallographic structures
    • Rossmann MG, Bernal R, Pletnev SV (2001) Combining electron microscopic with x-ray crystallographic structures. J Struct Biol 136:190-200.
    • (2001) J Struct Biol , vol.136 , pp. 190-200
    • Rossmann, M.G.1    Bernal, R.2    Pletnev, S.V.3
  • 44
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B, Richards FM (1971) The interpretation of protein structures: Estimation of static accessibility. J Mol Biol 55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 45
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera - a visualization system for exploratory research and analysis. J Comput Chem 25:1605-1612.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


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