메뉴 건너뛰기




Volumn 4, Issue 7, 2010, Pages

The first human epitope map of the alphaviral E1 and E2 proteins reveals a new E2 epitope with significant virus neutralizing activity

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; GLYCOPROTEIN E1; GLYCOPROTEIN E2; IMMUNOGLOBULIN G; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; PEPTIDE LIBRARY; VIRUS ANTIBODY; VIRUS ENVELOPE PROTEIN;

EID: 77957923201     PISSN: None     EISSN: None     Source Type: Journal    
DOI: 10.1371/journal.pntd.0000739     Document Type: Article
Times cited : (41)

References (76)
  • 2
    • 0027976963 scopus 로고
    • Medically important arboviruses of the United States and Canada
    • Calisher CH (1994) Medically important arboviruses of the United States and Canada. Clin Microbiol Rev 7: 89-116.
    • (1994) Clin Microbiol Rev , vol.7 , pp. 89-116
    • Calisher, C.H.1
  • 4
    • 16944366857 scopus 로고    scopus 로고
    • Epidemic Venezuelan equine encephalitis in La Guajira, Colombia, 1995
    • Rivas F, Diaz LA, Cardenas VM, Daza E, Bruzon L, et al. (1997) Epidemic Venezuelan equine encephalitis in La Guajira, Colombia, 1995. J Infect Dis 175: 828-832.
    • (1997) J Infect Dis , vol.175 , pp. 828-832
    • Rivas, F.1    Diaz, L.A.2    Cardenas, V.M.3    Daza, E.4    Bruzon, L.5
  • 5
    • 0026786096 scopus 로고
    • Phylogenetic analysis of alphaviruses in the Venezuelan equine encephalitis complex and identification of the source of epizootic viruses
    • Weaver SC, Bellew LA, Rico-Hesse R (1992) Phylogenetic analysis of alphaviruses in the Venezuelan equine encephalitis complex and identification of the source of epizootic viruses. Virology 191: 282-290.
    • (1992) Virology , vol.191 , pp. 282-290
    • Weaver, S.C.1    Bellew, L.A.2    Rico-Hesse, R.3
  • 6
    • 0031943796 scopus 로고    scopus 로고
    • Identification and genetic analysis of Panama-genotype Venezuelan equine encephalitis virus subtype ID in Peru
    • Oberste MS, Weaver SC, Watts DM, Smith JF (1998) Identification and genetic analysis of Panama-genotype Venezuelan equine encephalitis virus subtype ID in Peru. Am J Trop Med Hyg 58: 41-46.
    • (1998) Am J Trop Med Hyg , vol.58 , pp. 41-46
    • Oberste, M.S.1    Weaver, S.C.2    Watts, D.M.3    Smith, J.F.4
  • 7
    • 0030755509 scopus 로고    scopus 로고
    • Venezuelan equine encephalitis and Oropouche virus infections among Peruvian army troops in the Amazon region of Peru
    • Watts DM, Lavera V, Callahan J, Rossi C, Oberste MS, et al. (1997) Venezuelan equine encephalitis and Oropouche virus infections among Peruvian army troops in the Amazon region of Peru. Am J Trop Med Hyg 56: 661-667.
    • (1997) Am J Trop Med Hyg , vol.56 , pp. 661-667
    • Watts, D.M.1    Lavera, V.2    Callahan, J.3    Rossi, C.4    Oberste, M.S.5
  • 8
    • 18344413812 scopus 로고    scopus 로고
    • Venezuelan equine encephalitis febrile cases among humans in the Peruvian Amazon River region
    • Watts DM, Callahan J, Rossi C, Oberste MS, Roehrig JT, et al. (1998) Venezuelan equine encephalitis febrile cases among humans in the Peruvian Amazon River region. Am J Trop Med Hyg 58: 35-40.
    • (1998) Am J Trop Med Hyg , vol.58 , pp. 35-40
    • Watts, D.M.1    Callahan, J.2    Rossi, C.3    Oberste, M.S.4    Roehrig, J.T.5
  • 9
    • 0037327331 scopus 로고    scopus 로고
    • Equine amplification and virulence of subtype IE Venezuelan equine encephalitis viruses isolated during the 1993 and 1996 Mexican epizootics
    • Gonzalez-Salazar D, Estrada-Franco JG, Carrara AS, Aronson JF, Weaver SC (2003) Equine amplification and virulence of subtype IE Venezuelan equine encephalitis viruses isolated during the 1993 and 1996 Mexican epizootics. Emerg Infect Dis 9: 161-168.
    • (2003) Emerg Infect Dis , vol.9 , pp. 161-168
    • Gonzalez-Salazar, D.1    Estrada-Franco, J.G.2    Carrara, A.S.3    Aronson, J.F.4    Weaver, S.C.5
  • 11
    • 0034774473 scopus 로고    scopus 로고
    • Biological weapons-a primer for microbiologists
    • Hawley RJ, Eitzen EM, Jr. (2001) Biological weapons-a primer for microbiologists. Annu Rev Microbiol 55: 235-253.
    • (2001) Annu Rev Microbiol , vol.55 , pp. 235-253
    • Hawley, R.J.1    Eitzen Jr., E.M.2
  • 12
    • 0037154855 scopus 로고    scopus 로고
    • Monoclonal antibody protects mice against infection and disease when given either before or up to 24 h after airborne challenge with virulent Venezuelan equine encephalitis virus
    • Phillpotts RJ, Jones LD, Howard SC (2002) Monoclonal antibody protects mice against infection and disease when given either before or up to 24 h after airborne challenge with virulent Venezuelan equine encephalitis virus. Vaccine 20: 1497-1504.
    • (2002) Vaccine , vol.20 , pp. 1497-1504
    • Phillpotts, R.J.1    Jones, L.D.2    Howard, S.C.3
  • 13
  • 14
    • 0029960102 scopus 로고    scopus 로고
    • Long-term duration of detectable neutralizing antibodies after administration of live-attenuated VEE vaccine and following booster vaccination with inactivated VEE vaccine
    • Pittman PR, Makuch RS, Mangiafico JA, Cannon TL, Gibbs PH, et al. (1996) Long-term duration of detectable neutralizing antibodies after administration of live-attenuated VEE vaccine and following booster vaccination with inactivated VEE vaccine. Vaccine 14: 337-343.
    • (1996) Vaccine , vol.14 , pp. 337-343
    • Pittman, P.R.1    Makuch, R.S.2    Mangiafico, J.A.3    Cannon, T.L.4    Gibbs, P.H.5
  • 15
    • 0025815137 scopus 로고
    • Attenuating mutations in the E2 glycoprotein gene of Venezuelan equine encephalitis virus: Construction of single and multiple mutants in a full-length cDNA clone
    • Davis NL, Powell N, Greenwald GF, Willis LV, Johnson BJ, et al. (1991) Attenuating mutations in the E2 glycoprotein gene of Venezuelan equine encephalitis virus: construction of single and multiple mutants in a full-length cDNA clone. Virology 183: 20-31.
    • (1991) Virology , vol.183 , pp. 20-31
    • Davis, N.L.1    Powell, N.2    Greenwald, G.F.3    Willis, L.V.4    Johnson, B.J.5
  • 16
    • 0242365651 scopus 로고    scopus 로고
    • Genetically engineered, live attenuated vaccines for Venezuelan equine encephalitis: Testing in animal models
    • Pratt WD, Davis NL, Johnston RE, Smith JF (2003) Genetically engineered, live attenuated vaccines for Venezuelan equine encephalitis: testing in animal models. Vaccine 21: 3854-3862.
    • (2003) Vaccine , vol.21 , pp. 3854-3862
    • Pratt, W.D.1    Davis, N.L.2    Johnston, R.E.3    Smith, J.F.4
  • 17
    • 17044362650 scopus 로고    scopus 로고
    • Genetically engineered, live, attenuated vaccines protect nonhuman primates against aerosol challenge with a virulent IE strain of Venezuelan equine encephalitis virus
    • Reed DS, Lind CM, Lackemeyer MG, Sullivan LJ, Pratt WD, et al. (2005) Genetically engineered, live, attenuated vaccines protect nonhuman primates against aerosol challenge with a virulent IE strain of Venezuelan equine encephalitis virus. Vaccine 23: 3139-3147.
    • (2005) Vaccine , vol.23 , pp. 3139-3147
    • Reed, D.S.1    Lind, C.M.2    Lackemeyer, M.G.3    Sullivan, L.J.4    Pratt, W.D.5
  • 18
    • 33846633361 scopus 로고    scopus 로고
    • Venezuelan equine encephalitis virus vaccine candidate (V3526) safety, immunogenecity and efficacy in horses
    • Fine DL, Roberts BA, Teehee ML, Terpening SJ, Kelly CL, et al. (2007) Venezuelan equine encephalitis virus vaccine candidate (V3526) safety, immunogenecity and efficacy in horses. Vaccine 25: 1868-1876.
    • (2007) Vaccine , vol.25 , pp. 1868-1876
    • Fine, D.L.1    Roberts, B.A.2    Teehee, M.L.3    Terpening, S.J.4    Kelly, C.L.5
  • 19
    • 70350566074 scopus 로고    scopus 로고
    • Telemetric analysis to detect febrile responses in mice following vaccination with a liveattenuated virus vaccine
    • Martin SS, Bakken RR, Lind CM, Reed DS, Price JL, et al. (2009) Telemetric analysis to detect febrile responses in mice following vaccination with a liveattenuated virus vaccine. Vaccine 27: 6814-6823.
    • (2009) Vaccine , vol.27 , pp. 6814-6823
    • Martin, S.S.1    Bakken, R.R.2    Lind, C.M.3    Reed, D.S.4    Price, J.L.5
  • 20
    • 44749083368 scopus 로고    scopus 로고
    • Neurovirulence evaluation of Venezuelan equine encephalitis (VEE) vaccine candidate V3526 in nonhuman primates
    • Fine DL, Roberts BA, Terpening SJ, Mott J, Vasconcelos D, et al. (2008) Neurovirulence evaluation of Venezuelan equine encephalitis (VEE) vaccine candidate V3526 in nonhuman primates. Vaccine 26: 3497-3506.
    • (2008) Vaccine , vol.26 , pp. 3497-3506
    • Fine, D.L.1    Roberts, B.A.2    Terpening, S.J.3    Mott, J.4    Vasconcelos, D.5
  • 21
    • 0018141590 scopus 로고
    • Hexagonal glycoprotein arrays from Sindbis virus membranes
    • von Bonsdorff CH, Harrison SC (1978) Hexagonal glycoprotein arrays from Sindbis virus membranes. J Virol 28: 578-583.
    • (1978) J Virol , vol.28 , pp. 578-583
    • von Bonsdorff, C.H.1    Harrison, S.C.2
  • 22
    • 0016821407 scopus 로고
    • Sindbis virus glycoproteins form a regular icosahedral surface lattice
    • von Bonsdorff CH, Harrison SC (1975) Sindbis virus glycoproteins form a regular icosahedral surface lattice. J Virol 16: 141-145.
    • (1975) J Virol , vol.16 , pp. 141-145
    • von Bonsdorff, C.H.1    Harrison, S.C.2
  • 23
    • 0034855251 scopus 로고    scopus 로고
    • Venezuelan equine encephalomyelitis virus structure and its divergence from old world alphaviruses
    • Paredes A, Alwell-Warda K, Weaver SC, Chiu W, Watowich SJ (2001) Venezuelan equine encephalomyelitis virus structure and its divergence from old world alphaviruses. J Virol 75: 9532-9537.
    • (2001) J Virol , vol.75 , pp. 9532-9537
    • Paredes, A.1    Alwell-Warda, K.2    Weaver, S.C.3    Chiu, W.4    Watowich, S.J.5
  • 24
    • 0034117092 scopus 로고    scopus 로고
    • The surface conformation of Sindbis virus glycoproteins E1 and E2 at neutral and low pH, as determined by mass spectrometry-based mapping
    • Phinney BS, Blackburn K, Brown DT (2000) The surface conformation of Sindbis virus glycoproteins E1 and E2 at neutral and low pH, as determined by mass spectrometry-based mapping. J Virol 74: 5667-5678.
    • (2000) J Virol , vol.74 , pp. 5667-5678
    • Phinney, B.S.1    Blackburn, K.2    Brown, D.T.3
  • 26
    • 0026419333 scopus 로고
    • Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion
    • Choi HK, Tong L, Minor W, Dumas P, Boege U, et al. (1991) Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion. Nature 354: 37-43.
    • (1991) Nature , vol.354 , pp. 37-43
    • Choi, H.K.1    Tong, L.2    Minor, W.3    Dumas, P.4    Boege, U.5
  • 27
    • 33644799064 scopus 로고    scopus 로고
    • Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus
    • Roussel A, Lescar J, Vaney MC, Wengler G, Wengler G, et al. (2006) Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus. Structure 14: 75-86.
    • (2006) Structure , vol.14 , pp. 75-86
    • Roussel, A.1    Lescar, J.2    Vaney, M.C.3    Wengler, G.4    Wengler, G.5
  • 28
    • 0035815282 scopus 로고    scopus 로고
    • The Fusion glycoprotein shell of Semliki Forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH
    • Lescar J, Roussel A, Wien MW, Navaza J, Fuller SD, et al. (2001) The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH. Cell 105: 137-148.
    • (2001) Cell , vol.105 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wien, M.W.3    Navaza, J.4    Fuller, S.D.5
  • 30
    • 0033854594 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus
    • Mancini EJ, Clarke M, Gowen BE, Rutten T, Fuller SD (2000) Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus. Mol Cell 5: 255-266.
    • (2000) Mol Cell , vol.5 , pp. 255-266
    • Mancini, E.J.1    Clarke, M.2    Gowen, B.E.3    Rutten, T.4    Fuller, S.D.5
  • 31
    • 0028919758 scopus 로고
    • Nucleocapsid and glycoprotein organization in an enveloped virus
    • Cheng RH, Kuhn RJ, Olson NH, Rossmann MG, Choi HK, et al. (1995) Nucleocapsid and glycoprotein organization in an enveloped virus. Cell 80: 621-630.
    • (1995) Cell , vol.80 , pp. 621-630
    • Cheng, R.H.1    Kuhn, R.J.2    Olson, N.H.3    Rossmann, M.G.4    Choi, H.K.5
  • 32
    • 13144266721 scopus 로고    scopus 로고
    • Heparin binding sites on Ross River virus revealed by electron cryo-microscopy
    • Zhang W, Heil M, Kuhn RJ, Baker TS (2005) Heparin binding sites on Ross River virus revealed by electron cryo-microscopy. Virology 332: 511-518.
    • (2005) Virology , vol.332 , pp. 511-518
    • Zhang, W.1    Heil, M.2    Kuhn, R.J.3    Baker, T.S.4
  • 33
    • 0022283244 scopus 로고
    • The neutralization site on the E2 glycoprotein of Venezuelan equine encephalomyelitis (TC-83) virus is composed of multiple conformationally stable epitopes
    • Roehrig JT, Mathews JH (1985) The neutralization site on the E2 glycoprotein of Venezuelan equine encephalomyelitis (TC-83) virus is composed of multiple conformationally stable epitopes. Virology 142: 347-356.
    • (1985) Virology , vol.142 , pp. 347-356
    • Roehrig, J.T.1    Mathews, J.H.2
  • 34
    • 0020064191 scopus 로고
    • Antigenic analysis of the surface glycoproteins of a Venezuelan equine encephalomyelitis virus (TC-83) using monoclonal antibodies
    • Roehrig JT, Day JW, Kinney RM (1982) Antigenic analysis of the surface glycoproteins of a Venezuelan equine encephalomyelitis virus (TC-83) using monoclonal antibodies. Virology 118: 269-278.
    • (1982) Virology , vol.118 , pp. 269-278
    • Roehrig, J.T.1    Day, J.W.2    Kinney, R.M.3
  • 35
    • 0020421640 scopus 로고
    • Determination of the protective epitopes on the glycoproteins of Venezuelan equine encephalomyelitis virus by passive transfer of monoclonal antibodies
    • Mathews JH, Roehrig JT (1982) Determination of the protective epitopes on the glycoproteins of Venezuelan equine encephalomyelitis virus by passive transfer of monoclonal antibodies. J Immunol 129: 2763-2767.
    • (1982) J Immunol , vol.129 , pp. 2763-2767
    • Mathews, J.H.1    Roehrig, J.T.2
  • 36
    • 0025348447 scopus 로고
    • Variants of Venezuelan equine encephalitis virus that resist neutralization define a domain of the E2 glycoprotein
    • Johnson BJ, Brubaker JR, Roehrig JT, Trent DW (1990) Variants of Venezuelan equine encephalitis virus that resist neutralization define a domain of the E2 glycoprotein. Virology 177: 676-683.
    • (1990) Virology , vol.177 , pp. 676-683
    • Johnson, B.J.1    Brubaker, J.R.2    Roehrig, J.T.3    Trent, D.W.4
  • 37
    • 0025945880 scopus 로고
    • Identification of antigenically important domains in the glycoproteins of Sindbis virus by analysis of antibody escape variants
    • Strauss EG, Stec DS, Schmaljohn AL, Strauss JH (1991) Identification of antigenically important domains in the glycoproteins of Sindbis virus by analysis of antibody escape variants. J Virol 65: 4654-4664.
    • (1991) J Virol , vol.65 , pp. 4654-4664
    • Strauss, E.G.1    Stec, D.S.2    Schmaljohn, A.L.3    Strauss, J.H.4
  • 38
    • 0026517294 scopus 로고
    • Characterization of a major neutralization domain of Ross river virus using anti-viral and anti-peptide antibodies
    • Kerr PJ, Fitzgerald S, Tregear GW, Dalgarno L, Weir RC (1992) Characterization of a major neutralization domain of Ross river virus using anti-viral and anti-peptide antibodies. Virology 187: 338-342.
    • (1992) Virology , vol.187 , pp. 338-342
    • Kerr, P.J.1    Fitzgerald, S.2    Tregear, G.W.3    Dalgarno, L.4    Weir, R.C.5
  • 39
    • 0023858978 scopus 로고
    • Location of a major antigenic site involved in Ross River virus neutralization
    • Vrati S, Fernon CA, Dalgarno L, Weir RC (1988) Location of a major antigenic site involved in Ross River virus neutralization. Virology 162: 346-353.
    • (1988) Virology , vol.162 , pp. 346-353
    • Vrati, S.1    Fernon, C.A.2    Dalgarno, L.3    Weir, R.C.4
  • 40
    • 0023751791 scopus 로고
    • In vitro mechanisms of monoclonal antibody neutralization of alphaviruses
    • Roehrig JT, Hunt AR, Kinney RM, Mathews JH (1988) In vitro mechanisms of monoclonal antibody neutralization of alphaviruses. Virology 165: 66-73.
    • (1988) Virology , vol.165 , pp. 66-73
    • Roehrig, J.T.1    Hunt, A.R.2    Kinney, R.M.3    Mathews, J.H.4
  • 41
    • 0022219684 scopus 로고
    • Role of complement and the Fc portion of immunoglobulin G in immunity to Venezuelan equine encephalomyelitis virus infection with glycoprotein-specific monoclonal antibodies
    • Mathews JH, Roehrig JT, Trent DW (1985) Role of complement and the Fc portion of immunoglobulin G in immunity to Venezuelan equine encephalomyelitis virus infection with glycoprotein-specific monoclonal antibodies. J Virol 55: 594-600.
    • (1985) J Virol , vol.55 , pp. 594-600
    • Mathews, J.H.1    Roehrig, J.T.2    Trent, D.W.3
  • 42
    • 33747015784 scopus 로고    scopus 로고
    • Venezuelan equine encephalitis virus complex-specific monoclonal antibody provides broad protection, in murine models, against airborne challenge with viruses from serogroups I, II and III
    • Phillpotts RJ (2006) Venezuelan equine encephalitis virus complex-specific monoclonal antibody provides broad protection, in murine models, against airborne challenge with viruses from serogroups I, II and III. Virus Res 120: 107-112.
    • (2006) Virus Res , vol.120 , pp. 107-112
    • Phillpotts, R.J.1
  • 43
    • 33747354579 scopus 로고    scopus 로고
    • A humanized murine monoclonal antibody protects mice either before or after challenge with virulent Venezuelan equine encephalomyelitis virus
    • Hunt AR, Frederickson S, Hinkel C, Bowdish KS, Roehrig JT (2006) A humanized murine monoclonal antibody protects mice either before or after challenge with virulent Venezuelan equine encephalomyelitis virus. J Gen Virol 87: 2467-2476.
    • (2006) J Gen Virol , vol.87 , pp. 2467-2476
    • Hunt, A.R.1    Frederickson, S.2    Hinkel, C.3    Bowdish, K.S.4    Roehrig, J.T.5
  • 44
    • 0025910746 scopus 로고
    • Linkage of recognition and replication functions by assembling combinatorial antibody Fab libraries along phage surfaces
    • Kang AS, Barbas CF, Janda KD, Benkovic SJ, Lerner RA (1991) Linkage of recognition and replication functions by assembling combinatorial antibody Fab libraries along phage surfaces. Proc Natl Acad Sci U S A 88: 4363-4366.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 4363-4366
    • Kang, A.S.1    Barbas, C.F.2    Janda, K.D.3    Benkovic, S.J.4    Lerner, R.A.5
  • 45
    • 0025226085 scopus 로고
    • Phage antibodies: Filamentous phage displaying antibody variable domains
    • McCafferty J, Griffiths AD, Winter G, Chiswell DJ (1990) Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348: 552-554.
    • (1990) Nature , vol.348 , pp. 552-554
    • McCafferty, J.1    Griffiths, A.D.2    Winter, G.3    Chiswell, D.J.4
  • 46
    • 0032555214 scopus 로고    scopus 로고
    • A phage display approach for rapid antibody humanization: Designed combinatorial V gene libraries
    • Rader C, Cheresh DA, Barbas CF, 3rd (1998) A phage display approach for rapid antibody humanization: designed combinatorial V gene libraries. Proc Natl Acad Sci U S A 95: 8910-8915.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 8910-8915
    • Rader, C.1    Cheresh, D.A.2    Barbas III, C.F.3
  • 47
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith GP (1985) Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228: 1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 50
    • 0027182031 scopus 로고
    • Expression and localization of two low molecular weight GTP-binding proteins, Rab8 and Rab10, by epitope tag
    • Chen YT, Holcomb C, Moore HP (1993) Expression and localization of two low molecular weight GTP-binding proteins, Rab8 and Rab10, by epitope tag. Proc Natl Acad Sci U S A 90: 6508-6512.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 6508-6512
    • Chen, Y.T.1    Holcomb, C.2    Moore, H.P.3
  • 51
    • 0018841228 scopus 로고
    • Isolation and characterization of hybrid cell lines producing monoclonal antibodies directed against the structural proteins of Sindbis virus
    • Roehrig JT, Corser JA, Schlesinger MJ (1980) Isolation and characterization of hybrid cell lines producing monoclonal antibodies directed against the structural proteins of Sindbis virus. Virology 101: 41-49.
    • (1980) Virology , vol.101 , pp. 41-49
    • Roehrig, J.T.1    Corser, J.A.2    Schlesinger, M.J.3
  • 52
    • 0027474358 scopus 로고
    • Attenuation of Venezuelan equine encephalitis virus strain TC-83 is encoded by the 59-noncoding region and the E2 envelope glycoprotein
    • Kinney RM, Chang GJ, Tsuchiya KR, Sneider JM, Roehrig JT, et al. (1993) Attenuation of Venezuelan equine encephalitis virus strain TC-83 is encoded by the 59-noncoding region and the E2 envelope glycoprotein. J Virol 67: 1269-1277.
    • (1993) J Virol , vol.67 , pp. 1269-1277
    • Kinney, R.M.1    Chang, G.J.2    Tsuchiya, K.R.3    Sneider, J.M.4    Roehrig, J.T.5
  • 53
    • 35948993054 scopus 로고    scopus 로고
    • Gene expression profiling of nonhuman primates exposed to aerosolized Venezuelan equine encephalitis virus
    • Koterski J, Twenhafel N, Porter A, Reed DS, Martino-Catt S, et al. (2007) Gene expression profiling of nonhuman primates exposed to aerosolized Venezuelan equine encephalitis virus. FEMS Immunol Med Microbiol 51: 462-472.
    • (2007) FEMS Immunol Med Microbiol , vol.51 , pp. 462-472
    • Koterski, J.1    Twenhafel, N.2    Porter, A.3    Reed, D.S.4    Martino-Catt, S.5
  • 54
    • 52449088919 scopus 로고    scopus 로고
    • Development of human antibody fragments using antibody phage display for the detection and diagnosis of Venezuelan equine encephalitis virus (VEEV)
    • Kirsch MI, Hulseweh B, Nacke C, Rulker T, Schirrmann T, et al. (2008) Development of human antibody fragments using antibody phage display for the detection and diagnosis of Venezuelan equine encephalitis virus (VEEV). BMC Biotechnol 8: 66.
    • (2008) BMC Biotechnol , vol.8 , pp. 66
    • Kirsch, M.I.1    Hulseweh, B.2    Nacke, C.3    Rulker, T.4    Schirrmann, T.5
  • 55
    • 33847226329 scopus 로고    scopus 로고
    • Characterization of antibodies in singlechain format against the E7 oncoprotein of the human papillomavirus type 16 and their improvement by mutagenesis
    • Dona MG, Giorgi C, Accardi L (2007) Characterization of antibodies in singlechain format against the E7 oncoprotein of the human papillomavirus type 16 and their improvement by mutagenesis. BMC Cancer 7: 25.
    • (2007) BMC Cancer , vol.7 , pp. 25
    • Dona, M.G.1    Giorgi, C.2    Accardi, L.3
  • 56
    • 33947539526 scopus 로고    scopus 로고
    • Selection and characterization of scFv antibodies against the Sin Nombre hantavirus nucleocapsid protein
    • Velappan N, Martinez JS, Valero R, Chasteen L, Ponce L, et al. (2007) Selection and characterization of scFv antibodies against the Sin Nombre hantavirus nucleocapsid protein. J Immunol Methods 321: 60-69.
    • (2007) J Immunol Methods , vol.321 , pp. 60-69
    • Velappan, N.1    Martinez, J.S.2    Valero, R.3    Chasteen, L.4    Ponce, L.5
  • 57
    • 33745767275 scopus 로고    scopus 로고
    • Isolation and characterization of human monoclonal antibodies from individuals infected with West Nile Virus
    • Throsby M, Geuijen C, Goudsmit J, Bakker AQ, Korimbocus J, 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    Geuijen, C.2    Goudsmit, J.3    Bakker, A.Q.4    Korimbocus, J.5
  • 58
    • 20444414884 scopus 로고    scopus 로고
    • Antibody responses against wild-type yellow fever virus and the 17D vaccine strain: Characterization with human monoclonal antibody fragments and neutralization escape variants
    • Daffis S, Kontermann RE, Korimbocus J, Zeller H, Klenk HD, et al. (2005) Antibody responses against wild-type yellow fever virus and the 17D vaccine strain: characterization with human monoclonal antibody fragments and neutralization escape variants. Virology 337: 262-272.
    • (2005) Virology , vol.337 , pp. 262-272
    • Daffis, S.1    Kontermann, R.E.2    Korimbocus, J.3    Zeller, H.4    Klenk, H.D.5
  • 59
    • 22544445243 scopus 로고    scopus 로고
    • The human antibody repertoire specific for rabies virus glycoprotein as selected from immune libraries
    • Kramer RA, Marissen WE, Goudsmit J, Visser TJ, Clijsters-Van der Horst M, et al. (2005) The human antibody repertoire specific for rabies virus glycoprotein as selected from immune libraries. Eur J Immunol 35: 2131-2145.
    • (2005) Eur J Immunol , vol.35 , pp. 2131-2145
    • Kramer, R.A.1    Marissen, W.E.2    Goudsmit, J.3    Visser, T.J.4    Clijsters-van der Horst, M.5
  • 60
    • 20144389700 scopus 로고    scopus 로고
    • Molecular and biological characterization of human monoclonal antibodies binding to the spike and nucleocapsid proteins of severe acute respiratory syndrome coronavirus
    • van den Brink EN, Ter Meulen J, Cox F, Jongeneelen MA, Thijsse A, et al. (2005) Molecular and biological characterization of human monoclonal antibodies binding to the spike and nucleocapsid proteins of severe acute respiratory syndrome coronavirus. J Virol 79: 1635-1644.
    • (2005) J Virol , vol.79 , pp. 1635-1644
    • van den Brink, E.N.1    Ter Meulen, J.2    Cox, F.3    Jongeneelen, M.A.4    Thijsse, A.5
  • 61
    • 1242328734 scopus 로고    scopus 로고
    • Neutralizing human monoclonal antibodies to hepatitis A virus recovered by phage display
    • Kim SJ, Jang MH, Stapleton JT, Yoon SO, Kim KS, et al. (2004) Neutralizing human monoclonal antibodies to hepatitis A virus recovered by phage display. Virology 318: 598-607.
    • (2004) Virology , vol.318 , pp. 598-607
    • Kim, S.J.1    Jang, M.H.2    Stapleton, J.T.3    Yoon, S.O.4    Kim, K.S.5
  • 62
    • 8644238973 scopus 로고    scopus 로고
    • Identification of chimpanzee Fab fragments by repertoire cloning and production of a full-length humanized immunoglobulin G1 antibody that is highly efficient for neutralization of dengue type 4 virus
    • Men R, Yamashiro T, Goncalvez AP, Wernly C, Schofield DJ, et al. (2004) Identification of chimpanzee Fab fragments by repertoire cloning and production of a full-length humanized immunoglobulin G1 antibody that is highly efficient for neutralization of dengue type 4 virus. J Virol 78: 4665-4674.
    • (2004) J Virol , vol.78 , pp. 4665-4674
    • Men, R.1    Yamashiro, T.2    Goncalvez, A.P.3    Wernly, C.4    Schofield, D.J.5
  • 63
    • 4644361635 scopus 로고    scopus 로고
    • Single-chain variable fragment (scFv) antibodies against rotavirus NSP4 enterotoxin generated by phage display
    • Rodriguez-Diaz J, Monedero V, Perez-Martinez G, Buesa J (2004) Single-chain variable fragment (scFv) antibodies against rotavirus NSP4 enterotoxin generated by phage display. J Virol Methods 121: 231-238.
    • (2004) J Virol Methods , vol.121 , pp. 231-238
    • Rodriguez-Diaz, J.1    Monedero, V.2    Perez-Martinez, G.3    Buesa, J.4
  • 64
    • 0037473316 scopus 로고    scopus 로고
    • Human recombinant neutralizing antibodies against hantaan virus G2 protein
    • Koch J, Liang M, Queitsch I, Kraus AA, Bautz EK (2003) Human recombinant neutralizing antibodies against hantaan virus G2 protein. Virology 308: 64-73.
    • (2003) Virology , vol.308 , pp. 64-73
    • Koch, J.1    Liang, M.2    Queitsch, I.3    Kraus, A.A.4    Bautz, E.K.5
  • 66
    • 0025838698 scopus 로고
    • A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals
    • Burton DR, Barbas CF, III, Persson MA, Koenig S, Chanock RM, et al. (1991) A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals. Proc Natl Acad Sci U S A 88: 10134-10137.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10134-10137
    • Burton, D.R.1    Barbas III, C.F.2    Persson, M.A.3    Koenig, S.4    Chanock, R.M.5
  • 67
    • 0030956110 scopus 로고    scopus 로고
    • Monoclonal antibodies capable of distinguishing epizootic from enzootic varieties of subtype 1 Venezuelan equine encephalitis viruses in a rapid indirect immunofluorescence assay
    • Roehrig JT, Bolin RA (1997) Monoclonal antibodies capable of distinguishing epizootic from enzootic varieties of subtype 1 Venezuelan equine encephalitis viruses in a rapid indirect immunofluorescence assay. J Clin Microbiol 35: 1887-1890.
    • (1997) J Clin Microbiol , vol.35 , pp. 1887-1890
    • Roehrig, J.T.1    Bolin, R.A.2
  • 68
    • 0025266519 scopus 로고
    • Antigenic and genetic characterization of Sindbis virus monoclonal antibody escape mutants which define a pathogenesis domain on glycoprotein E2
    • Pence DF, Davis NL, Johnston RE (1990) Antigenic and genetic characterization of Sindbis virus monoclonal antibody escape mutants which define a pathogenesis domain on glycoprotein E2. Virology 175: 41-49.
    • (1990) Virology , vol.175 , pp. 41-49
    • Pence, D.F.1    Davis, N.L.2    Johnston, R.E.3
  • 69
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution
    • Amit AG, Mariuzza RA, Phillips SE, Poljak RJ (1986) Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution. Science 233: 747-753.
    • (1986) Science , vol.233 , pp. 747-753
    • Amit, A.G.1    Mariuzza, R.A.2    Phillips, S.E.3    Poljak, R.J.4
  • 70
    • 34247612875 scopus 로고    scopus 로고
    • Functional characterization of the Sindbis virus E2 glycoprotein by transposon linker-insertion mutagenesis
    • Navaratnarajah CK, Kuhn RJ (2007) Functional characterization of the Sindbis virus E2 glycoprotein by transposon linker-insertion mutagenesis. Virology 363: 134-147.
    • (2007) Virology , vol.363 , pp. 134-147
    • Navaratnarajah, C.K.1    Kuhn, R.J.2
  • 71
    • 0034633834 scopus 로고    scopus 로고
    • Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapid clearance from blood of mice
    • Bernard KA, Klimstra WB, Johnston RE (2000) Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapid clearance from blood of mice. Virology 276: 93-103.
    • (2000) Virology , vol.276 , pp. 93-103
    • Bernard, K.A.1    Klimstra, W.B.2    Johnston, R.E.3
  • 72
    • 33644815756 scopus 로고    scopus 로고
    • Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses
    • Mukhopadhyay S, Zhang W, Gabler S, Chipman PR, Strauss EG, et al. (2006) Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses. Structure 14: 63-73.
    • (2006) Structure , vol.14 , pp. 63-73
    • Mukhopadhyay, S.1    Zhang, W.2    Gabler, S.3    Chipman, P.R.4    Strauss, E.G.5
  • 73
    • 0025225365 scopus 로고
    • Synthetic peptides of Venezuelan equine encephalomyelitis virus E2 glycoprotein. I. Immunogenic analysis and identification of a protective peptide
    • Hunt AR, Johnson AJ, Roehrig JT (1990) Synthetic peptides of Venezuelan equine encephalomyelitis virus E2 glycoprotein. I. Immunogenic analysis and identification of a protective peptide. Virology 179: 701-711.
    • (1990) Virology , vol.179 , pp. 701-711
    • Hunt, A.R.1    Johnson, A.J.2    Roehrig, J.T.3
  • 74
    • 0026015347 scopus 로고
    • Synthetic peptides of the E2 glycoprotein of Venezuelan equine encephalomyelitis virus. II. Antibody to the amino terminus protects animals by limiting viral replication
    • Hunt AR, Short WA, Johnson AJ, Bolin RA, Roehrig JT (1991) Synthetic peptides of the E2 glycoprotein of Venezuelan equine encephalomyelitis virus. II. Antibody to the amino terminus protects animals by limiting viral replication. Virology 185: 281-290.
    • (1991) Virology , vol.185 , pp. 281-290
    • Hunt, A.R.1    Short, W.A.2    Johnson, A.J.3    Bolin, R.A.4    Roehrig, J.T.5
  • 75
    • 0026345264 scopus 로고
    • Synthetic peptides of Venezuelan equine encephalomyelitis virus E2 glycoprotein. III. Identification of a protective peptide derived from the carboxy-terminal extramembranal one-third of the protein
    • Johnson AJ, Hunt AR, Roehrig JT (1991) Synthetic peptides of Venezuelan equine encephalomyelitis virus E2 glycoprotein. III. Identification of a protective peptide derived from the carboxy-terminal extramembranal one-third of the protein. Virology 185: 840-842.
    • (1991) Virology , vol.185 , pp. 840-842
    • Johnson, A.J.1    Hunt, A.R.2    Roehrig, J.T.3
  • 76
    • 0028958221 scopus 로고
    • Localization of a protective epitope on a Venezuelan equine encephalomyelitis (VEE) virus peptide that protects mice from both epizootic and enzootic VEE virus challenge and is immunogenic in horses
    • Hunt AR, Roehrig JT (1995) Localization of a protective epitope on a Venezuelan equine encephalomyelitis (VEE) virus peptide that protects mice from both epizootic and enzootic VEE virus challenge and is immunogenic in horses. Vaccine 13: 281-288.
    • (1995) Vaccine , vol.13 , pp. 281-288
    • Hunt, A.R.1    Roehrig, J.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.