메뉴 건너뛰기




Volumn 85, Issue 23, 2011, Pages 12492-12504

Autographa californica multiple nucleopolyhedrovirus GP64 protein: Roles of histidine residues in triggering membrane fusion and fusion pore expansion

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; GLYCOPROTEIN GP 64; HISTIDINE; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN;

EID: 81255123299     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05153-11     Document Type: Article
Times cited : (31)

References (50)
  • 1
    • 78049513712 scopus 로고    scopus 로고
    • Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB
    • Atanasiu, D., W. T. Saw, G. H. Cohen, and R. J. Eisenberg. 2010. Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB. J. Virol. 84:12292-12299.
    • (2010) J. Virol. , vol.84 , pp. 12292-12299
    • Atanasiu, D.1    Saw, W.T.2    Cohen, G.H.3    Eisenberg, R.J.4
  • 2
    • 36749035394 scopus 로고    scopus 로고
    • Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion
    • Atanasiu, D., et al. 2007. Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion. Proc. Natl. Acad. Sci. U. S. A. 104:18718-18723.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 18718-18723
    • Atanasiu, D.1
  • 3
    • 77950513683 scopus 로고    scopus 로고
    • Bimolecular complementation defines functional regions of herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion
    • Atanasiu, D., et al. 2010. Bimolecular complementation defines functional regions of herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion. J. Virol. 84:3825-3834.
    • (2010) J. Virol. , vol.84 , pp. 3825-3834
    • Atanasiu, D.1
  • 5
    • 0025982953 scopus 로고
    • Baculovirus gp64 gene expression: analysis of sequences modulating early transcription and transactivation by IE1
    • Blissard, G. W., and G. F. Rohrmann. 1991. Baculovirus gp64 gene expression: analysis of sequences modulating early transcription and transactivation by IE1. J. Virol. 65:5820-5827.
    • (1991) J. Virol. , vol.65 , pp. 5820-5827
    • Blissard, G.W.1    Rohrmann, G.F.2
  • 6
    • 0026757345 scopus 로고
    • Baculovirus GP64 envelope glycoprotein is sufficient to mediate pH dependent membrane fusion
    • Blissard, G. W., and J. R. Wenz. 1992. Baculovirus GP64 envelope glycoprotein is sufficient to mediate pH dependent membrane fusion. J. Virol. 66:6829-6835.
    • (1992) J. Virol. , vol.66 , pp. 6829-6835
    • Blissard, G.W.1    Wenz, J.R.2
  • 7
    • 0037853207 scopus 로고    scopus 로고
    • Membrane fusion induced by vesicular stomatitis virus depends on histidine protonation
    • Carneiro, F. A., et al. 2003. Membrane fusion induced by vesicular stomatitis virus depends on histidine protonation. J. Biol. Chem. 278:13789-13794.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13789-13794
    • Carneiro, F.A.1
  • 8
    • 10044283361 scopus 로고    scopus 로고
    • A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion
    • Chanel-Vos, C., and M. Kielian. 2004. A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion. J. Virol. 78:13543-13552.
    • (2004) J. Virol. , vol.78 , pp. 13543-13552
    • Chanel-Vos, C.1    Kielian, M.2
  • 9
    • 0021910031 scopus 로고
    • Fusion mutants of the influenza virus hemagglutinin glycoprotein
    • Daniels, R. S., et al. 1985. Fusion mutants of the influenza virus hemagglutinin glycoprotein. Cell 40:431-439.
    • (1985) Cell , vol.40 , pp. 431-439
    • Daniels, R.S.1
  • 10
    • 67849129179 scopus 로고    scopus 로고
    • Viral inactivation based on inhibition of membrane fusion: understanding the role of histidine protonation to develop new viral vaccines
    • Da Poian, A. T., F. A. Carneiro, and F. Stauffer. 2009. Viral inactivation based on inhibition of membrane fusion: understanding the role of histidine protonation to develop new viral vaccines. Protein Pept. Lett. 16:779-785.
    • (2009) Protein Pept. Lett. , vol.16 , pp. 779-785
    • Da Poian, A.T.1    Carneiro, F.A.2    Stauffer, F.3
  • 11
    • 77549086793 scopus 로고    scopus 로고
    • Low pH-induced conformational change in herpes simplex virus glycoprotein B
    • Dollery, S. J., M. G. Delboy, and A. V. Nicola. 2010. Low pH-induced conformational change in herpes simplex virus glycoprotein B. J. Virol. 3759-3766.
    • (2010) J. Virol. , pp. 3759-3766
    • Dollery, S.J.1    Delboy, M.G.2    Nicola, A.V.3
  • 12
    • 55949108725 scopus 로고    scopus 로고
    • Identification of specific histidines as pH sensors in flavivirus membrane fusion
    • Fritz, R., K. Stiasny, and F. X. Heinz. 2008. Identification of specific histidines as pH sensors in flavivirus membrane fusion. J. Cell Biol. 183:353-361.
    • (2008) J. Cell Biol. , vol.183 , pp. 353-361
    • Fritz, R.1    Stiasny, K.2    Heinz, F.X.3
  • 13
    • 67449093075 scopus 로고    scopus 로고
    • Glycoprotein B of herpes simplex virus associates with target membranes via its fusion loops
    • Hannah, B. P., et al. 2009. Glycoprotein B of herpes simplex virus associates with target membranes via its fusion loops. J. Virol. 83:6825-6836.
    • (2009) J. Virol. , vol.83 , pp. 6825-6836
    • Hannah, B.P.1
  • 14
    • 55949125587 scopus 로고    scopus 로고
    • The pH sensor for flavivirus membrane fusion
    • Harrison, S. C. 2008. The pH sensor for flavivirus membrane fusion. J. Cell Biol. 183:177-179.
    • (2008) J. Cell Biol. , vol.183 , pp. 177-179
    • Harrison, S.C.1
  • 16
    • 0033526508 scopus 로고    scopus 로고
    • Host cell receptor binding by baculovirus GP64 and kinetics of virion entry
    • Hefferon, K., A. Oomens, S. Monsma, C. Finnerty, and G. W. Blissard. 1999. Host cell receptor binding by baculovirus GP64 and kinetics of virion entry. Virology 258:455-468.
    • (1999) Virology , vol.258 , pp. 455-468
    • Hefferon, K.1    Oomens, A.2    Monsma, S.3    Finnerty, C.4    Blissard, G.W.5
  • 17
    • 0000485094 scopus 로고
    • Established insect cell line from the cabbage looper, Trichoplusia ni
    • Hink, W. F. 1970. Established insect cell line from the cabbage looper, Trichoplusia ni. Nature 226:466-467.
    • (1970) Nature , vol.226 , pp. 466-467
    • Hink, W.F.1
  • 18
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • Kadlec, J., S. Loureiro, N. G. Abrescia, D. I. Stuart, and I. M. Jones. 2008. The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nat. Struct. Mol. Biol. 15:1024-1030.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1024-1030
    • Kadlec, J.1    Loureiro, S.2    Abrescia, N.G.3    Stuart, D.I.4    Jones, I.M.5
  • 19
    • 33749266195 scopus 로고    scopus 로고
    • The role of histidine residues in low-pH-mediated viral membrane fusion
    • Kampmann, T., D. S. Mueller, A. E. Mark, P. R. Young, and B. Kobe. 2006. The role of histidine residues in low-pH-mediated viral membrane fusion. Structure 14:1481-1487.
    • (2006) Structure , vol.14 , pp. 1481-1487
    • Kampmann, T.1    Mueller, D.S.2    Mark, A.E.3    Young, P.R.4    Kobe, B.5
  • 20
    • 59649124119 scopus 로고    scopus 로고
    • A histidine switch in hemagglutinin-neuraminidase triggers paramyxovirus-cell membrane fusion
    • Krishnan, A., et al. 2009. A histidine switch in hemagglutinin-neuraminidase triggers paramyxovirus-cell membrane fusion. J. Virol. 83:1727-1741.
    • (2009) J. Virol. , vol.83 , pp. 1727-1741
    • Krishnan, A.1
  • 21
    • 66149118534 scopus 로고    scopus 로고
    • The Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) GP64 protein: analysis of transmembrane (TM) domain length and sequence requirements
    • Li, Z., and G. W. Blissard. 2009. The Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) GP64 protein: analysis of transmembrane (TM) domain length and sequence requirements. J. Virol. 83:4447-4461.
    • (2009) J. Virol. , vol.83 , pp. 4447-4461
    • Li, Z.1    Blissard, G.W.2
  • 22
    • 77956636143 scopus 로고    scopus 로고
    • Baculovirus GP64 disulfide bonds: the intermolecular disulfide bond of AcMNPV GP64 is not essential for membrane fusion and virion budding
    • Li, Z., and G. W. Blissard. 2010. Baculovirus GP64 disulfide bonds: the intermolecular disulfide bond of AcMNPV GP64 is not essential for membrane fusion and virion budding. J. Virol. 84:8584-8589.
    • (2010) J. Virol. , vol.84 , pp. 8584-8589
    • Li, Z.1    Blissard, G.W.2
  • 23
    • 41149157914 scopus 로고    scopus 로고
    • Functional analysis of the transmembrane (TM) domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: substitution of heterologous TM domains
    • Li, Z., and G. W. Blissard. 2008. Functional analysis of the transmembrane (TM) domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: substitution of heterologous TM domains. J. Virol. 82: 3329-3341.
    • (2008) J. Virol. , vol.82 , pp. 3329-3341
    • Li, Z.1    Blissard, G.W.2
  • 24
    • 70350319200 scopus 로고    scopus 로고
    • The pre-transmembrane domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein is critical for membrane fusion and virus infectivity
    • Li, Z., and G. W. Blissard. 2009. The pre-transmembrane domain of the Autographa californica multicapsid nucleopolyhedrovirus GP64 protein is critical for membrane fusion and virus infectivity. J. Virol. 83:10993-11004.
    • (2009) J. Virol. , vol.83 , pp. 10993-11004
    • Li, Z.1    Blissard, G.W.2
  • 25
    • 33748674858 scopus 로고    scopus 로고
    • Functional entry of baculovirus into insect and mammalian cells is dependent on clathrin-mediated endocytosis
    • Long, G., X. Pan, R. Kormelink, and J. M. Vlak. 2006. Functional entry of baculovirus into insect and mammalian cells is dependent on clathrin-mediated endocytosis. J. Virol. 80:8830-8833.
    • (2006) J. Virol. , vol.80 , pp. 8830-8833
    • Long, G.1    Pan, X.2    Kormelink, R.3    Vlak, J.M.4
  • 26
    • 0027209690 scopus 로고
    • Efficient generation of infectious recombinant baculoviruses by site-specific transposon-mediated insertion of foreign genes into a baculovirus genome propagated in Escherichia coli
    • Luckow, V. A., S. C. Lee, G. F. Barry, and P. O. Olins. 1993. Efficient generation of infectious recombinant baculoviruses by site-specific transposon-mediated insertion of foreign genes into a baculovirus genome propagated in Escherichia coli. J. Virol. 67:4566-4579.
    • (1993) J. Virol. , vol.67 , pp. 4566-4579
    • Luckow, V.A.1    Lee, S.C.2    Barry, G.F.3    Olins, P.O.4
  • 27
    • 0032583172 scopus 로고    scopus 로고
    • Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 trimers into multiprotein aggregates
    • Markovic, I., H. Pulyaeva, A. Sokoloff, and L. V. Chernomordik. 1998. Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 trimers into multiprotein aggregates. J. Cell Biol. 143:1155-1166.
    • (1998) J. Cell Biol. , vol.143 , pp. 1155-1166
    • Markovic, I.1    Pulyaeva, H.2    Sokoloff, A.3    Chernomordik, L.V.4
  • 28
    • 0029898597 scopus 로고    scopus 로고
    • The GP64 envelope fusion protein is an essential baculovirus protein required for cell to cell transmission of infection
    • Monsma, S. A., A. G. P. Oomens, and G. W. Blissard. 1996. The GP64 envelope fusion protein is an essential baculovirus protein required for cell to cell transmission of infection. J. Virol. 70:4607-4616.
    • (1996) J. Virol. , vol.70 , pp. 4607-4616
    • Monsma, S.A.1    Oomens, A.G.P.2    Blissard, G.W.3
  • 29
    • 39449133035 scopus 로고    scopus 로고
    • Histidine protonation and the activation of viral fusion proteins
    • Mueller, D. S., et al. 2008. Histidine protonation and the activation of viral fusion proteins. Biochem. Soc. Trans. 36:43-45.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 43-45
    • Mueller, D.S.1
  • 30
    • 70450162409 scopus 로고    scopus 로고
    • Protonation of individual histidine residues is not required for the pH-dependent entry of West Nile virus: evaluation of the "histidine switch" hypothesis
    • Nelson, S., S. Poddar, T. Y. Lin, and T. C. Pierson. 2009. Protonation of individual histidine residues is not required for the pH-dependent entry of West Nile virus: evaluation of the "histidine switch" hypothesis. J. Virol. 83:12631-12635.
    • (2009) J. Virol. , vol.83 , pp. 12631-12635
    • Nelson, S.1    Poddar, S.2    Lin, T.Y.3    Pierson, T.C.4
  • 31
    • 0033557048 scopus 로고    scopus 로고
    • Requirement for GP64 to drive efficient budding of Autographa californica multicapsid nucleopolyhedrovirus
    • Oomens, A. G. P., and G. W. Blissard. 1999. Requirement for GP64 to drive efficient budding of Autographa californica multicapsid nucleopolyhedrovirus. Virology 254:297-314.
    • (1999) Virology , vol.254 , pp. 297-314
    • Oomens, A.G.P.1    Blissard, G.W.2
  • 32
    • 0029001890 scopus 로고
    • The baculovirus GP64 envelope fusion protein: synthesis, oligomerization, and processing
    • Oomens, A. G. P., S. A. Monsma, and G. W. Blissard. 1995. The baculovirus GP64 envelope fusion protein: synthesis, oligomerization, and processing. Virology 209:592-603.
    • (1995) Virology , vol.209 , pp. 592-603
    • Oomens, A.G.P.1    Monsma, S.A.2    Blissard, G.W.3
  • 33
    • 0033524323 scopus 로고    scopus 로고
    • An analysis of the role of the target membrane on the gp64-induced fusion pore
    • Plonsky, I., M. S. Cho, A. G. P. Oomens, G. W. Blissard, and J. Zimmerberg. 1999. An analysis of the role of the target membrane on the gp64-induced fusion pore. Virology 253:65-76.
    • (1999) Virology , vol.253 , pp. 65-76
    • Plonsky, I.1    Cho, M.S.2    Oomens, A.G.P.3    Blissard, G.W.4    Zimmerberg, J.5
  • 34
    • 42949085300 scopus 로고    scopus 로고
    • Initial size and dynamics of viral fusion pores are a function of the fusion protein mediating membrane fusion
    • Plonsky, I., D. H. Kingsley, A. Rashtian, P. S. Blank, and J. Zimmerberg. 2008. Initial size and dynamics of viral fusion pores are a function of the fusion protein mediating membrane fusion. Biol. Cell 100:377-386.
    • (2008) Biol. Cell , vol.100 , pp. 377-386
    • Plonsky, I.1    Kingsley, D.H.2    Rashtian, A.3    Blank, P.S.4    Zimmerberg, J.5
  • 35
    • 0030472394 scopus 로고    scopus 로고
    • The initial fusion pore induced by baculovirus GP64 is large and forms quickly
    • Plonsky, I., and J. Zimmerberg. 1996. The initial fusion pore induced by baculovirus GP64 is large and forms quickly. J. Cell Biol. 135:1831-1839.
    • (1996) J. Cell Biol. , vol.135 , pp. 1831-1839
    • Plonsky, I.1    Zimmerberg, J.2
  • 36
    • 66149140928 scopus 로고    scopus 로고
    • Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein
    • Qin, Z. L., Y. Zheng, and M. Kielian. 2009. Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein. J. Virol. 83:4670-4677.
    • (2009) J. Virol. , vol.83 , pp. 4670-4677
    • Qin, Z.L.1    Zheng, Y.2    Kielian, M.3
  • 37
    • 33947661927 scopus 로고    scopus 로고
    • The relevance of salt bridges for the stability of the influenza virus hemagglutinin
    • Rachakonda, P. S., et al. 2007. The relevance of salt bridges for the stability of the influenza virus hemagglutinin. FASEB J. 21:995-1002.
    • (2007) FASEB J , vol.21 , pp. 995-1002
    • Rachakonda, P.S.1
  • 38
    • 64049092310 scopus 로고    scopus 로고
    • Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein
    • Reed, M. L., et al. 2009. Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein. J. Virol. 83:3568-3580.
    • (2009) J. Virol. , vol.83 , pp. 3568-3580
    • Reed, M.L.1
  • 39
    • 0036309399 scopus 로고    scopus 로고
    • Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers
    • Roche, S., and Y. Gaudin. 2002. Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers. Virology 297: 128-135.
    • (2002) Virology , vol.297 , pp. 128-135
    • Roche, S.1    Gaudin, Y.2
  • 40
    • 10044243988 scopus 로고    scopus 로고
    • Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state
    • Russell, C. J., T. S. Jardetzky, and R. A. Lamb. 2004. Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state. J. Virol. 78:13727-13742.
    • (2004) J. Virol. , vol.78 , pp. 13727-13742
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 41
    • 59749100734 scopus 로고    scopus 로고
    • Low-pH triggering of human metapneumovirus fusion: essential residues and importance in entry
    • Schowalter, R. M., A. Chang, J. G. Robach, U. J. Buchholz, and R. E. Dutch. 2009. Low-pH triggering of human metapneumovirus fusion: essential residues and importance in entry. J. Virol. 83:1511-1522.
    • (2009) J. Virol. , vol.83 , pp. 1511-1522
    • Schowalter, R.M.1    Chang, A.2    Robach, J.G.3    Buchholz, U.J.4    Dutch, R.E.5
  • 42
    • 78649413011 scopus 로고    scopus 로고
    • Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1
    • Stampfer, S. D., H. Lou, G. H. Cohen, R. J. Eisenberg, and E. E. Heldwein. 2010. Structural basis of local, pH-dependent conformational changes in glycoprotein B from herpes simplex virus type 1. J. Virol. 84:12924-12933.
    • (2010) J. Virol. , vol.84 , pp. 12924-12933
    • Stampfer, S.D.1    Lou, H.2    Cohen, G.H.3    Eisenberg, R.J.4    Heldwein, E.E.5
  • 43
    • 33846136390 scopus 로고    scopus 로고
    • Inactivation of vesicular stomatitis virus through inhibition of membrane fusion by chemical modification of the viral glycoprotein
    • Stauffer, F., et al. 2007. Inactivation of vesicular stomatitis virus through inhibition of membrane fusion by chemical modification of the viral glycoprotein. Antiviral Res. 73:31-39.
    • (2007) Antiviral Res. , vol.73 , pp. 31-39
    • Stauffer, F.1
  • 44
    • 84855225539 scopus 로고    scopus 로고
    • Molecular mechanisms of flavivirus membrane fusion
    • doi:10.1007/s00726-009-0370-4
    • Stiasny, K., R. Fritz, K. Pangerl, and F. Heinz. 2009. Molecular mechanisms of flavivirus membrane fusion. Amino Acids doi:10.1007/s00726-009-0370-4.
    • (2009) Amino Acids
    • Stiasny, K.1    Fritz, R.2    Pangerl, K.3    Heinz, F.4
  • 45
    • 32844457667 scopus 로고    scopus 로고
    • Baculoviridae
    • H. V. Van Regenmortel, D. H. L. Bishop, M. H. Van Regenmortel, and C. M. Fauquet (ed.), Elsevier Academic Press, New York, NY
    • Theilmann, D. A., et al. 2005. Baculoviridae, p. 177-185. In H. V. Van Regenmortel, D. H. L. Bishop, M. H. Van Regenmortel, and C. M. Fauquet (ed.), Virus taxonomy: eighth report of the International Committee on Taxonomy of Viruses. Elsevier Academic Press, New York, NY.
    • (2005) Virus taxonomy: eighth report of the International Committee on Taxonomy of Viruses , pp. 177-185
    • Theilmann, D.A.1
  • 46
    • 36749003222 scopus 로고    scopus 로고
    • Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion
    • Thoennes, S., et al. 2008. Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology 370:403-414.
    • (2008) Virology , vol.370 , pp. 403-414
    • Thoennes, S.1
  • 47
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme
    • White, J. M., S. E. Delos, M. Brecher, and K. Schornberg. 2008. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43:189-219.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 48
    • 79955373167 scopus 로고    scopus 로고
    • Structural characterization of an early fusion intermediate of influenza virus hemagglutinin
    • Xu, R., and I. A. Wilson. 2011. Structural characterization of an early fusion intermediate of influenza virus hemagglutinin. J. Virol. 85:5172-5182.
    • (2011) J. Virol. , vol.85 , pp. 5172-5182
    • Xu, R.1    Wilson, I.A.2
  • 49
    • 42449100377 scopus 로고    scopus 로고
    • Identification of a GP64 subdomain involved in receptor binding by budded virions of the baculovirus AcMNPV
    • Zhou, J., and G. W. Blissard. 2008. Identification of a GP64 subdomain involved in receptor binding by budded virions of the baculovirus AcMNPV. J. Virol. 82:4449-4460.
    • (2008) J. Virol. , vol.82 , pp. 4449-4460
    • Zhou, J.1    Blissard, G.W.2
  • 50
    • 33747065188 scopus 로고    scopus 로고
    • Mapping the conformational epitope of a neutralizing antibody (AcV1) directed against the AcMNPV GP64 protein
    • Zhou, J., and G. W. Blissard. 2006. Mapping the conformational epitope of a neutralizing antibody (AcV1) directed against the AcMNPV GP64 protein. Virology 352:427-437.
    • (2006) Virology , vol.352 , pp. 427-437
    • Zhou, J.1    Blissard, G.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.