메뉴 건너뛰기




Volumn 7, Issue 6, 2011, Pages

A dynamic landscape for antibody binding modulates antibody-mediated neutralization of West Nile virus

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT; EPITOPE; MONOCLONAL ANTIBODY; VIRUS ENVELOPE PROTEIN; WEST NILE VACCINE; GLYCOPROTEIN E, FLAVIVIRUS; NEUTRALIZING ANTIBODY; VIRUS ANTIBODY;

EID: 79959812241     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002111     Document Type: Article
Times cited : (133)

References (69)
  • 1
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: The Viruses and Their Replication
    • In: Knipe DM, Howley PM, editors, 5th Ed, Philadelphia, Lippincott-Williams & Wilkins
    • Lindenbach BD, Thiel HJ, Rice CM, (2007) Flaviviridae: The Viruses and Their Replication. In: Knipe DM, Howley PM, editors. Fields Virology. 5th ed Philadelphia Lippincott-Williams & Wilkins pp. 1101-1152.
    • (2007) Fields Virology , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.J.2    Rice, C.M.3
  • 2
    • 34249914817 scopus 로고    scopus 로고
    • The long-term outcomes of human West Nile virus infection
    • Sejvar JJ, (2007) The long-term outcomes of human West Nile virus infection. Clin Infect Dis 44: 1617-1624.
    • (2007) Clin Infect Dis , vol.44 , pp. 1617-1624
    • Sejvar, J.J.1
  • 3
    • 70349973308 scopus 로고    scopus 로고
    • West Nile virus infection in plasma of blood and plasma donors, United States
    • Planitzer CB, Modrof J, Yu MY, Kreil TR, (2009) West Nile virus infection in plasma of blood and plasma donors, United States. Emerg Infect Dis 15: 1668-1670.
    • (2009) Emerg Infect Dis , vol.15 , pp. 1668-1670
    • Planitzer, C.B.1    Modrof, J.2    Yu, M.Y.3    Kreil, T.R.4
  • 4
    • 64649101780 scopus 로고    scopus 로고
    • Pathogenesis of flavivirus infections: using and abusing the host cell
    • Fernandez-Garcia MD, Mazzon M, Jacobs M, Amara A, (2009) Pathogenesis of flavivirus infections: using and abusing the host cell. Cell Host Microbe 5: 318-328.
    • (2009) Cell Host Microbe , vol.5 , pp. 318-328
    • Fernandez-Garcia, M.D.1    Mazzon, M.2    Jacobs, M.3    Amara, A.4
  • 5
    • 0036407156 scopus 로고    scopus 로고
    • The molecular biology of West Nile Virus: a new invader of the western hemisphere
    • Brinton MA, (2002) The molecular biology of West Nile Virus: a new invader of the western hemisphere. Annu Rev Microbiol 56: 371-402.
    • (2002) Annu Rev Microbiol , vol.56 , pp. 371-402
    • Brinton, M.A.1
  • 6
    • 48749123790 scopus 로고    scopus 로고
    • Structural proteomics of dengue virus
    • Perera R, Kuhn RJ, (2008) Structural proteomics of dengue virus. Curr Opin Microbiol 11: 369-377.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 369-377
    • Perera, R.1    Kuhn, R.J.2
  • 7
    • 34848900462 scopus 로고    scopus 로고
    • Cholesterol manipulation by West Nile virus perturbs the cellular immune response
    • Mackenzie JM, Khromykh AA, Parton RG, (2007) Cholesterol manipulation by West Nile virus perturbs the cellular immune response. Cell Host Microbe 2: 229-239.
    • (2007) Cell Host Microbe , vol.2 , pp. 229-239
    • Mackenzie, J.M.1    Khromykh, A.A.2    Parton, R.G.3
  • 8
    • 33646167045 scopus 로고    scopus 로고
    • Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein
    • Roosendaal J, Westaway EG, Khromykh A, Mackenzie JM, (2006) Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein. J Virol 80: 4623-4632.
    • (2006) J Virol , vol.80 , pp. 4623-4632
    • Roosendaal, J.1    Westaway, E.G.2    Khromykh, A.3    Mackenzie, J.M.4
  • 9
    • 77949373371 scopus 로고    scopus 로고
    • The NS5 protein of the virulent West Nile virus NY99 strain is a potent antagonist of type I interferon-mediated JAK-STAT signaling
    • Laurent-Rolle M, Boer EF, Lubick KJ, Wolfinbarger JB, Carmody AB, et al. (2010) The NS5 protein of the virulent West Nile virus NY99 strain is a potent antagonist of type I interferon-mediated JAK-STAT signaling. J Virol 84: 3503-3515.
    • (2010) J Virol , vol.84 , pp. 3503-3515
    • Laurent-Rolle, M.1    Boer, E.F.2    Lubick, K.J.3    Wolfinbarger, J.B.4    Carmody, A.B.5
  • 11
    • 77951063838 scopus 로고    scopus 로고
    • Antagonism of the complement component C4 by flavivirus nonstructural protein NS1
    • Avirutnan P, Fuchs A, Hauhart RE, Somnuke P, Youn S, et al. (2010) Antagonism of the complement component C4 by flavivirus nonstructural protein NS1. J Exp Med 207: 793-806.
    • (2010) J Exp Med , vol.207 , pp. 793-806
    • Avirutnan, P.1    Fuchs, A.2    Hauhart, R.E.3    Somnuke, P.4    Youn, S.5
  • 14
    • 41349112304 scopus 로고    scopus 로고
    • Structure of the immature dengue virus at low pH primes proteolytic maturation
    • Yu IM, Zhang W, Holdaway HA, Li L, Kostyuchenko VA, et al. (2008) Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 319: 1834-1837.
    • (2008) Science , vol.319 , pp. 1834-1837
    • Yu, I.M.1    Zhang, W.2    Holdaway, H.A.3    Li, L.4    Kostyuchenko, V.A.5
  • 15
    • 41349112506 scopus 로고    scopus 로고
    • The flavivirus precursor membrane-envelope protein complex: structure and maturation
    • Li L, Lok SM, Yu IM, Zhang Y, Kuhn RJ, et al. (2008) The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science 319: 1830-1834.
    • (2008) Science , vol.319 , pp. 1830-1834
    • Li, L.1    Lok, S.M.2    Yu, I.M.3    Zhang, Y.4    Kuhn, R.J.5
  • 16
    • 0028815675 scopus 로고
    • Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH
    • Allison SL, Schalich J, Stiasny K, Mandl CW, Kunz C, et al. (1995) Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH. J Virol 69: 695-700.
    • (1995) J Virol , vol.69 , pp. 695-700
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5
  • 17
    • 0037236396 scopus 로고    scopus 로고
    • Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus
    • Elshuber S, Allison SL, Heinz FX, Mandl CW, (2003) Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus. J Gen Virol 84: 183-191.
    • (2003) J Gen Virol , vol.84 , pp. 183-191
    • Elshuber, S.1    Allison, S.L.2    Heinz, F.X.3    Mandl, C.W.4
  • 18
    • 0027081630 scopus 로고
    • The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein
    • Guirakhoo F, Bolin RA, Roehrig JT, (1992) The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein. Virology 191: 921-931.
    • (1992) Virology , vol.191 , pp. 921-931
    • Guirakhoo, F.1    Bolin, R.A.2    Roehrig, J.T.3
  • 19
    • 31144445030 scopus 로고    scopus 로고
    • West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection
    • Davis CW, Nguyen HY, Hanna SL, Sanchez MD, Doms RW, et al. (2006) West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection. J Virol 80: 1290-1301.
    • (2006) J Virol , vol.80 , pp. 1290-1301
    • Davis, C.W.1    Nguyen, H.Y.2    Hanna, S.L.3    Sanchez, M.D.4    Doms, R.W.5
  • 21
    • 44449143037 scopus 로고    scopus 로고
    • Maturation of West Nile virus modulates sensitivity to antibody-mediated neutralization
    • Nelson S, Jost CA, Xu Q, Ess J, Martin JE, et al. (2008) Maturation of West Nile virus modulates sensitivity to antibody-mediated neutralization. PLoS Pathog 4: e1000060.
    • (2008) PLoS Pathog , vol.4
    • Nelson, S.1    Jost, C.A.2    Xu, Q.3    Ess, J.4    Martin, J.E.5
  • 22
    • 77954972691 scopus 로고    scopus 로고
    • Influence of pr-M cleavage on the heterogeneity of extracellular dengue virus particles
    • Junjhon J, Edwards TJ, Utaipat U, Bowman VD, Holdaway HA, et al. (2010) Influence of pr-M cleavage on the heterogeneity of extracellular dengue virus particles. J Virol 84: 8353-8358.
    • (2010) J Virol , vol.84 , pp. 8353-8358
    • Junjhon, J.1    Edwards, T.J.2    Utaipat, U.3    Bowman, V.D.4    Holdaway, H.A.5
  • 23
    • 0032989258 scopus 로고    scopus 로고
    • Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E
    • Allison SL, Stiasny K, Stadler K, Mandl CW, Heinz FX, (1999) Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E. J Virol 73: 5605-5612.
    • (1999) J Virol , vol.73 , pp. 5605-5612
    • Allison, S.L.1    Stiasny, K.2    Stadler, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 25
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: implications for flavivirus organization, maturation, and fusion
    • Kuhn RJ, Zhang W, Rossmann MG, Pletnev SV, Corver J, 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    Zhang, W.2    Rossmann, M.G.3    Pletnev, S.V.4    Corver, J.5
  • 27
    • 33747607044 scopus 로고    scopus 로고
    • West Nile virus in complex with the Fab fragment of a neutralizing monoclonal antibody
    • Kaufmann B, Nybakken GE, Chipman PR, Zhang W, Diamond MS, et al. (2006) West Nile virus in complex with the Fab fragment of a neutralizing monoclonal antibody. Proc Natl Acad Sci U S A 103: 12400-12404.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 12400-12404
    • Kaufmann, B.1    Nybakken, G.E.2    Chipman, P.R.3    Zhang, W.4    Diamond, M.S.5
  • 28
    • 26944454471 scopus 로고    scopus 로고
    • Structural basis of West Nile virus neutralization by a therapeutic antibody
    • Nybakken GE, Oliphant T, Johnson S, Burke S, Diamond MS, et al. (2005) Structural basis of West Nile virus neutralization by a therapeutic antibody. Nature 437: 764-769.
    • (2005) Nature , vol.437 , pp. 764-769
    • Nybakken, G.E.1    Oliphant, T.2    Johnson, S.3    Burke, S.4    Diamond, M.S.5
  • 29
    • 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
  • 31
    • 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
  • 32
    • 0032505578 scopus 로고    scopus 로고
    • DNA-based and alphavirus-vectored immunisation with prM and E proteins elicits long-lived and protective immunity against the flavivirus, Murray Valley encephalitis virus
    • Colombage G, Hall R, Pavy M, Lobigs M, (1998) DNA-based and alphavirus-vectored immunisation with prM and E proteins elicits long-lived and protective immunity against the flavivirus, Murray Valley encephalitis virus. Virology 250: 151-163.
    • (1998) Virology , vol.250 , pp. 151-163
    • Colombage, G.1    Hall, R.2    Pavy, M.3    Lobigs, M.4
  • 33
    • 0026505138 scopus 로고
    • Recombinant vaccinia virus producing the prM and E proteins of yellow fever virus protects mice from lethal yellow fever encephalitis
    • Pincus S, Mason PW, Konishi E, Fonseca BA, Shope RE, et al. (1992) Recombinant vaccinia virus producing the prM and E proteins of yellow fever virus protects mice from lethal yellow fever encephalitis. Virology 187: 290-297.
    • (1992) Virology , vol.187 , pp. 290-297
    • Pincus, S.1    Mason, P.W.2    Konishi, E.3    Fonseca, B.A.4    Shope, R.E.5
  • 34
    • 0033394257 scopus 로고    scopus 로고
    • Identification of an epitope on the dengue virus membrane (M) protein defined by cross-protective monoclonal antibodies: design of an improved epitope sequence based on common determinants present in both envelope (E and M) proteins
    • Falconar AK, (1999) Identification of an epitope on the dengue virus membrane (M) protein defined by cross-protective monoclonal antibodies: design of an improved epitope sequence based on common determinants present in both envelope (E and M) proteins. Arch Virol 144: 2313-2330.
    • (1999) Arch Virol , vol.144 , pp. 2313-2330
    • Falconar, A.K.1
  • 35
    • 0037086592 scopus 로고    scopus 로고
    • Immune response to synthetic peptides of dengue prM protein
    • Vazquez S, Guzman MG, Guillen G, Chinea G, Perez AB, et al. (2002) Immune response to synthetic peptides of dengue prM protein. Vaccine 20: 1823-1830.
    • (2002) Vaccine , vol.20 , pp. 1823-1830
    • Vazquez, S.1    Guzman, M.G.2    Guillen, G.3    Chinea, G.4    Perez, A.B.5
  • 37
    • 0017913254 scopus 로고
    • A multi-hit model for the neutralization of animal viruses
    • Della-Porta AJ, Westaway EG, (1978) A multi-hit model for the neutralization of animal viruses. J Gen Virol 38: 1-19.
    • (1978) J Gen Virol , vol.38 , pp. 1-19
    • Della-Porta, A.J.1    Westaway, E.G.2
  • 38
    • 34147133789 scopus 로고    scopus 로고
    • The stoichiometry of antibody-mediated neutralization and enhancement of West Nile virus infection
    • Pierson TC, Xu Q, Nelson S, Oliphant T, Nybakken GE, et al. (2007) The stoichiometry of antibody-mediated neutralization and enhancement of West Nile virus infection. Cell Host Microbe 1: 135-145.
    • (2007) Cell Host Microbe , vol.1 , pp. 135-145
    • Pierson, T.C.1    Xu, Q.2    Nelson, S.3    Oliphant, T.4    Nybakken, G.E.5
  • 39
    • 33845389501 scopus 로고    scopus 로고
    • Antibody recognition and neutralization determinants on domains I and II of West Nile Virus envelope protein
    • Oliphant T, Nybakken GE, Engle M, Xu Q, Nelson CA, et al. (2006) Antibody recognition and neutralization determinants on domains I and II of West Nile Virus envelope protein. J Virol 80: 12149-12159.
    • (2006) J Virol , vol.80 , pp. 12149-12159
    • Oliphant, T.1    Nybakken, G.E.2    Engle, M.3    Xu, Q.4    Nelson, C.A.5
  • 40
    • 33748948792 scopus 로고    scopus 로고
    • Cryptic properties of a cluster of dominant flavivirus cross-reactive antigenic sites
    • Stiasny K, Kiermayr S, Holzmann H, Heinz FX, (2006) Cryptic properties of a cluster of dominant flavivirus cross-reactive antigenic sites. J Virol 80: 9557-9568.
    • (2006) J Virol , vol.80 , pp. 9557-9568
    • Stiasny, K.1    Kiermayr, S.2    Holzmann, H.3    Heinz, F.X.4
  • 41
    • 50149096815 scopus 로고    scopus 로고
    • Characterization of Dengue Complex-specific Neutralizing Epitopes on the Envelope Protein Domain III of Dengue 2 Virus
    • Gromowski GD, Barrett ND, Barrett AD, (2008) Characterization of Dengue Complex-specific Neutralizing Epitopes on the Envelope Protein Domain III of Dengue 2 Virus. J Virol 82: 8828-8837.
    • (2008) J Virol , vol.82 , pp. 8828-8837
    • Gromowski, G.D.1    Barrett, N.D.2    Barrett, A.D.3
  • 42
    • 72649088588 scopus 로고    scopus 로고
    • Complement protein C1q reduces the stoichiometric threshold for antibody-mediated neutralization of West Nile virus
    • Mehlhop E, Nelson S, Jost CA, Gorlatov S, Johnson S, et al. (2009) Complement protein C1q reduces the stoichiometric threshold for antibody-mediated neutralization of West Nile virus. Cell Host Microbe 6: 381-391.
    • (2009) Cell Host Microbe , vol.6 , pp. 381-391
    • Mehlhop, E.1    Nelson, S.2    Jost, C.A.3    Gorlatov, S.4    Johnson, S.5
  • 43
    • 0001622630 scopus 로고
    • The neutralization of arboviruses. II. Neutralization in heterologous virus-serum mixtures with four group B arboviruses
    • Westaway EG, (1965) The neutralization of arboviruses. II. Neutralization in heterologous virus-serum mixtures with four group B arboviruses. Virology 26: 528-537.
    • (1965) Virology , vol.26 , pp. 528-537
    • Westaway, E.G.1
  • 44
    • 0018636837 scopus 로고
    • Antibody-mediated enhancement of Flavivirus replication in macrophage-like cell lines
    • Peiris JS, Porterfield JS, (1979) Antibody-mediated enhancement of Flavivirus replication in macrophage-like cell lines. Nature 282: 509-511.
    • (1979) Nature , vol.282 , pp. 509-511
    • Peiris, J.S.1    Porterfield, J.S.2
  • 45
    • 0035558423 scopus 로고    scopus 로고
    • Structural dynamics, an intrinsic property of viral capsids
    • Witz J, Brown F, (2001) Structural dynamics, an intrinsic property of viral capsids. Arch Virol 146: 2263-2274.
    • (2001) Arch Virol , vol.146 , pp. 2263-2274
    • Witz, J.1    Brown, F.2
  • 46
    • 40949161794 scopus 로고    scopus 로고
    • Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins
    • Lok SM, Kostyuchenko V, Nybakken GE, Holdaway HA, Battisti AJ, 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    Kostyuchenko, V.2    Nybakken, G.E.3    Holdaway, H.A.4    Battisti, A.J.5
  • 47
    • 0031985001 scopus 로고    scopus 로고
    • Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry
    • Bothner B, Dong XF, Bibbs L, Johnson JE, Siuzdak G, (1998) Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry. J Biol Chem 273: 673-676.
    • (1998) J Biol Chem , vol.273 , pp. 673-676
    • Bothner, B.1    Dong, X.F.2    Bibbs, L.3    Johnson, J.E.4    Siuzdak, G.5
  • 49
    • 54049109927 scopus 로고    scopus 로고
    • Temperature-dependent production of pseudoinfectious dengue reporter virus particles by complementation
    • Ansarah-Sobrinho C, Nelson S, Jost CA, Whitehead SS, Pierson TC, (2008) Temperature-dependent production of pseudoinfectious dengue reporter virus particles by complementation. Virology 381: 67-74.
    • (2008) Virology , vol.381 , pp. 67-74
    • Ansarah-Sobrinho, C.1    Nelson, S.2    Jost, C.A.3    Whitehead, S.S.4    Pierson, T.C.5
  • 50
    • 0642287817 scopus 로고    scopus 로고
    • Neutralization and antibody-dependent enhancement of dengue viruses
    • Halstead SB, (2003) Neutralization and antibody-dependent enhancement of dengue viruses. Adv Virus Res 60: 421-467.
    • (2003) Adv Virus Res , vol.60 , pp. 421-467
    • Halstead, S.B.1
  • 51
    • 0022345971 scopus 로고
    • Comparison of dengue virus plaque reduction neutralization by macro and "semi-micro' methods in LLC-MK2 cells
    • Morens DM, Halstead SB, Larsen LK, (1985) Comparison of dengue virus plaque reduction neutralization by macro and "semi-micro' methods in LLC-MK2 cells. Microbiol Immunol 29: 1197-1205.
    • (1985) Microbiol Immunol , vol.29 , pp. 1197-1205
    • Morens, D.M.1    Halstead, S.B.2    Larsen, L.K.3
  • 52
    • 70350347088 scopus 로고    scopus 로고
    • Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody
    • Cherrier MV, Kaufmann B, Nybakken GE, Lok SM, Warren JT, et al. (2009) Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody. EMBO J 28: 3269-3276.
    • (2009) EMBO J , vol.28 , pp. 3269-3276
    • Cherrier, M.V.1    Kaufmann, B.2    Nybakken, G.E.3    Lok, S.M.4    Warren, J.T.5
  • 53
    • 21044448356 scopus 로고    scopus 로고
    • Development of a humanized monoclonal antibody with therapeutic potential against West Nile virus
    • Oliphant T, Engle M, Nybakken GE, Doane C, Johnson S, 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    Engle, M.2    Nybakken, G.E.3    Doane, C.4    Johnson, S.5
  • 54
    • 77954039828 scopus 로고    scopus 로고
    • The development of therapeutic antibodies that neutralize homologous and heterologous genotypes of dengue virus type 1
    • Shrestha B, Brien JD, Sukupolvi-Petty S, Austin SK, Edeling MA, et al. (2010) The development of therapeutic antibodies that neutralize homologous and heterologous genotypes of dengue virus type 1. PLoS Pathog 6: e1000823.
    • (2010) PLoS Pathog , vol.6
    • Shrestha, B.1    Brien, J.D.2    Sukupolvi-Petty, S.3    Austin, S.K.4    Edeling, M.A.5
  • 55
    • 0041324572 scopus 로고    scopus 로고
    • Virus particle dynamics
    • Johnson JE, (2003) Virus particle dynamics. Adv Protein Chem 64: 197-218.
    • (2003) Adv Protein Chem , vol.64 , pp. 197-218
    • Johnson, J.E.1
  • 56
    • 0027530735 scopus 로고
    • Mutations in or near the fusion peptide of the influenza virus hemagglutinin affect an antigenic site in the globular region
    • Yewdell JW, Taylor A, Yellen A, Caton A, Gerhard W, et al. (1993) Mutations in or near the fusion peptide of the influenza virus hemagglutinin affect an antigenic site in the globular region. J Virol 67: 933-942.
    • (1993) J Virol , vol.67 , pp. 933-942
    • Yewdell, J.W.1    Taylor, A.2    Yellen, A.3    Caton, A.4    Gerhard, W.5
  • 57
    • 79952732800 scopus 로고    scopus 로고
    • MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1
    • Ruprecht CR, Krarup A, Reynell L, Mann AM, Brandenberg OF, et al. (2011) MPER-specific antibodies induce gp120 shedding and irreversibly neutralize HIV-1. J Exp Med 208: 439-454.
    • (2011) J Exp Med , vol.208 , pp. 439-454
    • Ruprecht, C.R.1    Krarup, A.2    Reynell, L.3    Mann, A.M.4    Brandenberg, O.F.5
  • 58
    • 0036889127 scopus 로고    scopus 로고
    • Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion
    • Finnegan CM, Berg W, Lewis GK, DeVico AL, (2002) Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion. J Virol 76: 12123-12134.
    • (2002) J Virol , vol.76 , pp. 12123-12134
    • Finnegan, C.M.1    Berg, W.2    Lewis, G.K.3    de Vico, A.L.4
  • 59
    • 8644251891 scopus 로고    scopus 로고
    • Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies
    • Binley JM, Wrin T, Korber B, Zwick MB, Wang M, et al. (2004) Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies. J Virol 78: 13232-13252.
    • (2004) J Virol , vol.78 , pp. 13232-13252
    • Binley, J.M.1    Wrin, T.2    Korber, B.3    Zwick, M.B.4    Wang, M.5
  • 61
    • 0021350733 scopus 로고
    • Elucidation of the topography and determination of the protective epitopes on the E glycoprotein of Saint Louis encephalitis virus by passive transfer with monoclonal antibodies
    • Mathews JH, Roehrig JT, (1984) Elucidation of the topography and determination of the protective epitopes on the E glycoprotein of Saint Louis encephalitis virus by passive transfer with monoclonal antibodies. J Immunol 132: 1533-1537.
    • (1984) J Immunol , vol.132 , pp. 1533-1537
    • Mathews, J.H.1    Roehrig, J.T.2
  • 62
    • 77956031215 scopus 로고    scopus 로고
    • Structure and function analysis of therapeutic monoclonal antibodies against dengue virus type 2
    • Sukupolvi-Petty S, Austin SK, Engle M, Brien JD, Dowd KA, et al. (2010) Structure and function analysis of therapeutic monoclonal antibodies against dengue virus type 2. J Virol 84: 9227-9239.
    • (2010) J Virol , vol.84 , pp. 9227-9239
    • Sukupolvi-Petty, S.1    Austin, S.K.2    Engle, M.3    Brien, J.D.4    Dowd, K.A.5
  • 63
    • 36749028784 scopus 로고    scopus 로고
    • Complement protein C1q inhibits antibody-dependent enhancement of flavivirus infection in an IgG subclass-specific manner
    • Mehlhop E, Ansarah-Sobrinho C, Johnson S, Engle M, Fremont DH, et al. (2007) Complement protein C1q inhibits antibody-dependent enhancement of flavivirus infection in an IgG subclass-specific manner. Cell Host Microbe 2: 417-426.
    • (2007) Cell Host Microbe , vol.2 , pp. 417-426
    • Mehlhop, E.1    Ansarah-Sobrinho, C.2    Johnson, S.3    Engle, M.4    Fremont, D.H.5
  • 64
    • 35449004580 scopus 로고    scopus 로고
    • Induction of epitope-specific neutralizing antibodies against West Nile virus
    • Oliphant T, Nybakken GE, Austin SK, Xu Q, Bramson J, 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    Nybakken, G.E.2    Austin, S.K.3    Xu, Q.4    Bramson, J.5
  • 65
    • 32844457056 scopus 로고    scopus 로고
    • A rapid and quantitative assay for measuring antibody-mediated neutralization of West Nile virus infection
    • Pierson TC, Sanchez MD, Puffer BA, Ahmed AA, Geiss BJ, et al. (2006) A rapid and quantitative assay for measuring antibody-mediated neutralization of West Nile virus infection. Virology 346: 53-65.
    • (2006) Virology , vol.346 , pp. 53-65
    • Pierson, T.C.1    Sanchez, M.D.2    Puffer, B.A.3    Ahmed, A.A.4    Geiss, B.J.5
  • 66
    • 33846003511 scopus 로고    scopus 로고
    • The location of asparagine-linked glycans on West Nile virions controls their interactions with CD209 (dendritic cell-specific ICAM-3 grabbing nonintegrin)
    • Davis CW, Mattei LM, Nguyen HY, Ansarah-Sobrinho C, Doms RW, et al. (2006) The location of asparagine-linked glycans on West Nile virions controls their interactions with CD209 (dendritic cell-specific ICAM-3 grabbing nonintegrin). J Biol Chem 281: 37183-37194.
    • (2006) J Biol Chem , vol.281 , pp. 37183-37194
    • Davis, C.W.1    Mattei, L.M.2    Nguyen, H.Y.3    Ansarah-Sobrinho, C.4    Doms, R.W.5
  • 67
    • 0001130198 scopus 로고
    • Observations on anti-phage sera. I. he percentage law
    • Andrewes CH, Elford WJ, (1933) Observations on anti-phage sera. I. he percentage law. Br J Exp Pathol 14: 367-376.
    • (1933) Br J Exp Pathol , vol.14 , pp. 367-376
    • Andrewes, C.H.1    Elford, W.J.2
  • 68
    • 27144498110 scopus 로고    scopus 로고
    • N-linked glycosylation of west nile virus envelope proteins influences particle assembly and infectivity
    • Hanna SL, Pierson TC, Sanchez MD, Ahmed AA, Murtadha MM, et al. (2005) N-linked glycosylation of west nile virus envelope proteins influences particle assembly and infectivity. J Virol 79: 13262-13274.
    • (2005) J Virol , vol.79 , pp. 13262-13274
    • Hanna, S.L.1    Pierson, T.C.2    Sanchez, M.D.3    Ahmed, A.A.4    Murtadha, M.M.5
  • 69
    • 23744432104 scopus 로고    scopus 로고
    • Actively replicating West Nile virus is resistant to cytoplasmic delivery of siRNA
    • Geiss BJ, Pierson TC, Diamond MS, (2005) Actively replicating West Nile virus is resistant to cytoplasmic delivery of siRNA. Virol J 2: 53.
    • (2005) Virol J , vol.2 , pp. 53
    • Geiss, B.J.1    Pierson, T.C.2    Diamond, M.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.