메뉴 건너뛰기




Volumn 8, Issue 1, 2013, Pages

A Critical HA1 Neutralizing Domain of H5N1 Influenza in an Optimal Conformation Induces Strong Cross-Protection

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN G; INFLUENZA VIRUS HEMAGGLUTININ; INFLUENZA VIRUS HEMAGGLUTININ 1; MONOMER; NEUTRALIZING ANTIBODY; RECOMBINANT HEMAGGLUTININ 13 263; RECOMBINANT HEMAGGLUTININ 13 263 FC FUSION PROTEIN; RECOMBINANT HEMAGGLUTININ 13 263 FD FUSION PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VACCINE;

EID: 84872190107     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0053568     Document Type: Article
Times cited : (29)

References (48)
  • 1
    • 84861394598 scopus 로고    scopus 로고
    • Experimental adaptation of an influenza H5 HA confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets
    • Imai M, Watanabe T, Hatta M, Das SC, Ozawa M, et al. (2012) Experimental adaptation of an influenza H5 HA confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets. Nature 486: 420-428.
    • (2012) Nature , vol.486 , pp. 420-428
    • Imai, M.1    Watanabe, T.2    Hatta, M.3    Das, S.C.4    Ozawa, M.5
  • 3
    • 79953192523 scopus 로고    scopus 로고
    • Roles of the hemagglutinin of influenza A virus in viral entry and development of antiviral therapeutics and vaccines
    • Jiang S, Li R, Du L, Liu S, (2010) Roles of the hemagglutinin of influenza A virus in viral entry and development of antiviral therapeutics and vaccines. Protein Cell 1: 342-354.
    • (2010) Protein Cell , vol.1 , pp. 342-354
    • Jiang, S.1    Li, R.2    Du, L.3    Liu, S.4
  • 4
    • 79957901666 scopus 로고    scopus 로고
    • Fine epitope mapping of monoclonal antibodies against hemagglutinin of a highly pathogenic H5N1 influenza virus using yeast surface display
    • Han T, Sui J, Bennett AS, Liddington RC, Donis RO, et al. (2011) Fine epitope mapping of monoclonal antibodies against hemagglutinin of a highly pathogenic H5N1 influenza virus using yeast surface display. Biochem Biophys Res Commun 409: 253-259.
    • (2011) Biochem Biophys Res Commun , vol.409 , pp. 253-259
    • Han, T.1    Sui, J.2    Bennett, A.S.3    Liddington, R.C.4    Donis, R.O.5
  • 6
    • 71049124869 scopus 로고    scopus 로고
    • Heterosubtype neutralizing responses to influenza A (H5N1) viruses are mediated by antibodies to virus haemagglutinin
    • Garcia JM, Pepin S, Lagarde N, Ma ES, Vogel FR, et al. (2009) Heterosubtype neutralizing responses to influenza A (H5N1) viruses are mediated by antibodies to virus haemagglutinin. PLoS One 4: e7918.
    • (2009) PLoS One , vol.4
    • Garcia, J.M.1    Pepin, S.2    Lagarde, N.3    Ma, E.S.4    Vogel, F.R.5
  • 7
    • 67349094613 scopus 로고    scopus 로고
    • Evaluation of conserved and variable influenza antigens for immunization against different isolates of H5N1 viruses
    • Patel A, Tran K, Gray M, Li Y, Ao Z, et al. (2009) Evaluation of conserved and variable influenza antigens for immunization against different isolates of H5N1 viruses. Vaccine 27: 3083-3089.
    • (2009) Vaccine , vol.27 , pp. 3083-3089
    • Patel, A.1    Tran, K.2    Gray, M.3    Li, Y.4    Ao, Z.5
  • 8
    • 84863994618 scopus 로고    scopus 로고
    • A triclade DNA vaccine designed on the basis of a comprehensive serologic study elicits neutralizing antibody responses against all clades and subclades of highly pathogenic avian influenza H5N1 viruses
    • Zhou F, Wang G, Buchy P, Cai Z, Chen H, et al. (2012) A triclade DNA vaccine designed on the basis of a comprehensive serologic study elicits neutralizing antibody responses against all clades and subclades of highly pathogenic avian influenza H5N1 viruses. J Virol 86: 6970-6978.
    • (2012) J Virol , vol.86 , pp. 6970-6978
    • Zhou, F.1    Wang, G.2    Buchy, P.3    Cai, Z.4    Chen, H.5
  • 9
    • 33645981586 scopus 로고    scopus 로고
    • Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus
    • Stevens J, Blixt O, Tumpey TM, Taubenberger JK, Paulson JC, et al. (2006) Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science 312: 404-410.
    • (2006) Science , vol.312 , pp. 404-410
    • Stevens, J.1    Blixt, O.2    Tumpey, T.M.3    Taubenberger, J.K.4    Paulson, J.C.5
  • 10
    • 66149149791 scopus 로고    scopus 로고
    • Antigenic fingerprinting of H5N1 avian influenza using convalescent sera and monoclonal antibodies reveals potential vaccine and diagnostic targets
    • Khurana S, Suguitan AL Jr, Rivera Y, Simmons CP, Lanzavecchia A, et al. (2009) Antigenic fingerprinting of H5N1 avian influenza using convalescent sera and monoclonal antibodies reveals potential vaccine and diagnostic targets. PLoS Med 6: e1000049.
    • (2009) PLoS Med , vol.6
    • Khurana, S.1    Suguitan Jr., A.L.2    Rivera, Y.3    Simmons, C.P.4    Lanzavecchia, A.5
  • 11
    • 79953101262 scopus 로고    scopus 로고
    • Effect of receptor binding domain mutations on receptor binding and transmissibility of avian influenza H5N1 viruses
    • Maines TR, Chen LM, Van HN, Tumpey TM, Blixt O, et al. (2011) Effect of receptor binding domain mutations on receptor binding and transmissibility of avian influenza H5N1 viruses. Virology 413: 139-147.
    • (2011) Virology , vol.413 , pp. 139-147
    • Maines, T.R.1    Chen, L.M.2    van, H.N.3    Tumpey, T.M.4    Blixt, O.5
  • 12
    • 58549110104 scopus 로고    scopus 로고
    • Changes in H5N1 influenza virus hemagglutinin receptor binding domain affect systemic spread
    • Yen HL, Aldridge JR, Boon AC, Ilyushina NA, Salomon R, et al. (2009) Changes in H5N1 influenza virus hemagglutinin receptor binding domain affect systemic spread. Proc Natl Acad Sci U S A 106: 286-291.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 286-291
    • Yen, H.L.1    Aldridge, J.R.2    Boon, A.C.3    Ilyushina, N.A.4    Salomon, R.5
  • 13
    • 80055113889 scopus 로고    scopus 로고
    • H5N1 virus-like particle vaccine elicits cross-reactive neutralizing antibodies that preferentially bind to the oligomeric form of influenza virus hemagglutinin in humans
    • Khurana S, Wu J, Verma N, Verma S, Raghunandan R, et al. (2011) H5N1 virus-like particle vaccine elicits cross-reactive neutralizing antibodies that preferentially bind to the oligomeric form of influenza virus hemagglutinin in humans. J Virol 85: 10945-10954.
    • (2011) J Virol , vol.85 , pp. 10945-10954
    • Khurana, S.1    Wu, J.2    Verma, N.3    Verma, S.4    Raghunandan, R.5
  • 15
    • 79551557170 scopus 로고    scopus 로고
    • A recombinant vaccine of H5N1 HA1 fused with foldon and human IgG Fc induced complete cross-clade protection against divergent H5N1 viruses
    • Du L, Leung VH, Zhang X, Zhou J, Chen M, et al. (2011) A recombinant vaccine of H5N1 HA1 fused with foldon and human IgG Fc induced complete cross-clade protection against divergent H5N1 viruses. PLoS One 6: e16555.
    • (2011) PLoS One , vol.6
    • Du, L.1    Leung, V.H.2    Zhang, X.3    Zhou, J.4    Chen, M.5
  • 16
    • 17044375920 scopus 로고    scopus 로고
    • Receptor-binding domain of severe acute respiratory syndrome coronavirus spike protein contains multiple conformation-dependent epitopes that induce highly potent neutralizing antibodies
    • He Y, Lu H, Siddiqui P, Zhou Y, Jiang S, (2005) Receptor-binding domain of severe acute respiratory syndrome coronavirus spike protein contains multiple conformation-dependent epitopes that induce highly potent neutralizing antibodies. J Immunol 174: 4908-4915.
    • (2005) J Immunol , vol.174 , pp. 4908-4915
    • He, Y.1    Lu, H.2    Siddiqui, P.3    Zhou, Y.4    Jiang, S.5
  • 17
    • 33947189535 scopus 로고    scopus 로고
    • Receptor-binding domain of SARS-CoV spike protein induces long-term protective immunity in an animal model
    • Du L, Zhao G, He Y, Guo Y, Zheng BJ, et al. (2007) Receptor-binding domain of SARS-CoV spike protein induces long-term protective immunity in an animal model. Vaccine 25: 2832-2838.
    • (2007) Vaccine , vol.25 , pp. 2832-2838
    • Du, L.1    Zhao, G.2    He, Y.3    Guo, Y.4    Zheng, B.J.5
  • 18
    • 5144234050 scopus 로고    scopus 로고
    • Receptor-binding domain of SARS-CoV spike protein induces highly potent neutralizing antibodies: implication for developing subunit vaccine
    • He Y, Zhou Y, Liu S, Kou Z, Li W, et al. (2004) Receptor-binding domain of SARS-CoV spike protein induces highly potent neutralizing antibodies: implication for developing subunit vaccine. Biochem Biophys Res Commun 324: 773-781.
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 773-781
    • He, Y.1    Zhou, Y.2    Liu, S.3    Kou, Z.4    Li, W.5
  • 19
    • 40449085104 scopus 로고    scopus 로고
    • Intranasal vaccination of recombinant adeno-associated virus encoding receptor-binding domain of severe acute respiratory syndrome coronavirus (SARS-CoV) spike protein induces strong mucosal immune responses and provides long-term protection against SARS-CoV infection
    • Du L, Zhao G, Lin Y, Sui H, Chan C, et al. (2008) Intranasal vaccination of recombinant adeno-associated virus encoding receptor-binding domain of severe acute respiratory syndrome coronavirus (SARS-CoV) spike protein induces strong mucosal immune responses and provides long-term protection against SARS-CoV infection. J Immunol 180: 948-956.
    • (2008) J Immunol , vol.180 , pp. 948-956
    • Du, L.1    Zhao, G.2    Lin, Y.3    Sui, H.4    Chan, C.5
  • 20
    • 62049083943 scopus 로고    scopus 로고
    • Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses
    • Sui J, Hwang WC, Perez S, Wei G, Aird D, et al. (2009) Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nat Struct Mol Biol 16: 265-273.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 265-273
    • Sui, J.1    Hwang, W.C.2    Perez, S.3    Wei, G.4    Aird, D.5
  • 21
    • 0025304137 scopus 로고
    • Refinement of the influenza virus hemagglutinin by simulated annealing
    • Weis WI, Brunger AT, Skehel JJ, Wiley DC, (1990) Refinement of the influenza virus hemagglutinin by simulated annealing. J Mol Biol 212: 737-761.
    • (1990) J Mol Biol , vol.212 , pp. 737-761
    • Weis, W.I.1    Brunger, A.T.2    Skehel, J.J.3    Wiley, D.C.4
  • 22
    • 84857371887 scopus 로고    scopus 로고
    • Public health and biosecurity.The obligation to prevent the next dual-use controversy
    • Faden RR, Karron RA, (2012) Public health and biosecurity.The obligation to prevent the next dual-use controversy. Science 335: 802-804.
    • (2012) Science , vol.335 , pp. 802-804
    • Faden, R.R.1    Karron, R.A.2
  • 23
    • 84857355131 scopus 로고    scopus 로고
    • Public health and biosecurity.Life sciences at a crossroads: respiratory transmissible H5N1
    • Osterholm MT, Henderson DA, (2012) Public health and biosecurity. Life sciences at a crossroads: respiratory transmissible H5N1. Science 335: 801-802.
    • (2012) Science , vol.335 , pp. 801-802
    • Osterholm, M.T.1    Henderson, D.A.2
  • 24
    • 84862777094 scopus 로고    scopus 로고
    • Public health and biosecurity.Adaptations of avian flu virus are a cause for concern
    • Berns KI, Casadevall A, Cohen ML, Ehrlich SA, Enquist LW, et al. (2012) Public health and biosecurity. Adaptations of avian flu virus are a cause for concern. Science 335: 660-661.
    • (2012) Science , vol.335 , pp. 660-661
    • Berns, K.I.1    Casadevall, A.2    Cohen, M.L.3    Ehrlich, S.A.4    Enquist, L.W.5
  • 26
    • 84859182929 scopus 로고    scopus 로고
    • Genetically engineered transmissible influenza A/H5N1: A call for laboratory safety and security
    • Le Duc JW, Franz DR, (2012) Genetically engineered transmissible influenza A/H5N1: A call for laboratory safety and security. Biosecur Bioterror 10: 153-154.
    • (2012) Biosecur Bioterror , vol.10 , pp. 153-154
    • Le Duc, J.W.1    Franz, D.R.2
  • 28
    • 80053645706 scopus 로고    scopus 로고
    • Evaluation of a virosomal H5N1 vaccine formulated with Matrix M adjuvant in a phase I clinical trial
    • Cox RJ, Pedersen G, Madhun AS, Svindland S, Saevik M, et al. (2011) Evaluation of a virosomal H5N1 vaccine formulated with Matrix M adjuvant in a phase I clinical trial. Vaccine 29: 8049-8059.
    • (2011) Vaccine , vol.29 , pp. 8049-8059
    • Cox, R.J.1    Pedersen, G.2    Madhun, A.S.3    Svindland, S.4    Saevik, M.5
  • 29
    • 79957453401 scopus 로고    scopus 로고
    • Dose-sparing H5N1 A/Indonesia/05/2005 pre-pandemic influenza vaccine in adults and elderly adults: a phase III, placebo-controlled, randomized study
    • Langley JM, Risi G, Caldwell M, Gilderman L, Berwald B, et al. (2011) Dose-sparing H5N1 A/Indonesia/05/2005 pre-pandemic influenza vaccine in adults and elderly adults: a phase III, placebo-controlled, randomized study. J Infect Dis 203: 1729-1738.
    • (2011) J Infect Dis , vol.203 , pp. 1729-1738
    • Langley, J.M.1    Risi, G.2    Caldwell, M.3    Gilderman, L.4    Berwald, B.5
  • 30
    • 77954982419 scopus 로고    scopus 로고
    • A single immunization with CoVaccine HT-adjuvanted H5N1 influenza virus vaccine induces protective cellular and humoral immune responses in ferrets
    • Bodewes R, Kreijtz JH, van AG, Geelhoed-Mieras MM, Verburgh RJ, et al. (2010) A single immunization with CoVaccine HT-adjuvanted H5N1 influenza virus vaccine induces protective cellular and humoral immune responses in ferrets. J Virol 84: 7943-7952.
    • (2010) J Virol , vol.84 , pp. 7943-7952
    • Bodewes, R.1    Kreijtz, J.H.2    van, A.G.3    Geelhoed-Mieras, M.M.4    Verburgh, R.J.5
  • 31
    • 82455188114 scopus 로고    scopus 로고
    • Vaccination with drifted variants of avian H5 hemagglutinin protein elicits a broadened antibody response that is protective against challenge with homologous or drifted live H5 influenza virus
    • Santiago FW, Fitzgerald T, Treanor JJ, Topham DJ, (2011) Vaccination with drifted variants of avian H5 hemagglutinin protein elicits a broadened antibody response that is protective against challenge with homologous or drifted live H5 influenza virus. Vaccine 29: 8888-8897.
    • (2011) Vaccine , vol.29 , pp. 8888-8897
    • Santiago, F.W.1    Fitzgerald, T.2    Treanor, J.J.3    Topham, D.J.4
  • 32
    • 51649100250 scopus 로고    scopus 로고
    • A consensus-hemagglutinin-based DNA vaccine that protects mice against divergent H5N1 influenza viruses
    • Chen MW, Cheng TJ, Huang Y, Jan JT, Ma SH, et al. (2008) A consensus-hemagglutinin-based DNA vaccine that protects mice against divergent H5N1 influenza viruses. Proc Natl Acad Sci U S A 105: 13538-13543.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 13538-13543
    • Chen, M.W.1    Cheng, T.J.2    Huang, Y.3    Jan, J.T.4    Ma, S.H.5
  • 33
    • 79551569177 scopus 로고    scopus 로고
    • Vectors based on modified vaccinia Ankara expressing influenza H5N1 hemagglutinin induce substantial cross-clade protective immunity
    • Hessel A, Schwendinger M, Holzer GW, Orlinger KK, Coulibaly S, et al. (2011) Vectors based on modified vaccinia Ankara expressing influenza H5N1 hemagglutinin induce substantial cross-clade protective immunity. PLoS One 6: e16247.
    • (2011) PLoS One , vol.6
    • Hessel, A.1    Schwendinger, M.2    Holzer, G.W.3    Orlinger, K.K.4    Coulibaly, S.5
  • 34
    • 84355166474 scopus 로고    scopus 로고
    • Safety and immunogenicity of two different doses of a Vero cell-derived, whole virus clade 2 H5N1 (A/Indonesia/05/2005) influenza vaccine
    • Tambyah PA, Wilder-Smith A, Pavlova BG, Barrett PN, Oh HM, et al. (2012) Safety and immunogenicity of two different doses of a Vero cell-derived, whole virus clade 2 H5N1 (A/Indonesia/05/2005) influenza vaccine. Vaccine 30: 329-335.
    • (2012) Vaccine , vol.30 , pp. 329-335
    • Tambyah, P.A.1    Wilder-Smith, A.2    Pavlova, B.G.3    Barrett, P.N.4    Oh, H.M.5
  • 35
    • 79957796724 scopus 로고    scopus 로고
    • Recombinant trimeric HA protein immunogenicity of H5N1 avian influenza viruses and their combined use with inactivated or adenovirus vaccines
    • Lin SC, Huang MH, Tsou PC, Huang LM, Chong P, et al. (2011) Recombinant trimeric HA protein immunogenicity of H5N1 avian influenza viruses and their combined use with inactivated or adenovirus vaccines. PLoS One 6: e20052.
    • (2011) PLoS One , vol.6
    • Lin, S.C.1    Huang, M.H.2    Tsou, P.C.3    Huang, L.M.4    Chong, P.5
  • 36
    • 84859997825 scopus 로고    scopus 로고
    • Immunization with SARS coronavirus vaccines leads to pulmonary immunopathology on challenge with the SARS virus
    • Tseng CT, Sbrana E, Iwata-Yoshikawa N, Newman PC, Garron T, et al. (2012) Immunization with SARS coronavirus vaccines leads to pulmonary immunopathology on challenge with the SARS virus. PLoS One 7: e35421.
    • (2012) PLoS One , vol.7
    • Tseng, C.T.1    Sbrana, E.2    Iwata-Yoshikawa, N.3    Newman, P.C.4    Garron, T.5
  • 37
    • 79952418476 scopus 로고    scopus 로고
    • Adjuvant-free immunization with hemagglutinin-Fc fusion proteins as an approach to influenza vaccines
    • Loureiro S, Ren J, Phapugrangkul P, Colaco CA, Bailey CR, et al. (2011) Adjuvant-free immunization with hemagglutinin-Fc fusion proteins as an approach to influenza vaccines. J Virol 85: 3010-3014.
    • (2011) J Virol , vol.85 , pp. 3010-3014
    • Loureiro, S.1    Ren, J.2    Phapugrangkul, P.3    Colaco, C.A.4    Bailey, C.R.5
  • 38
    • 8544254692 scopus 로고    scopus 로고
    • Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable beta-hairpin: atomic details of trimer dissociation and local beta-hairpin stability from residual dipolar couplings
    • Meier S, Guthe S, Kiefhaber T, Grzesiek S, (2004) Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable beta-hairpin: atomic details of trimer dissociation and local beta-hairpin stability from residual dipolar couplings. J Mol Biol 344: 1051-1069.
    • (2004) J Mol Biol , vol.344 , pp. 1051-1069
    • Meier, S.1    Guthe, S.2    Kiefhaber, T.3    Grzesiek, S.4
  • 39
    • 77955275844 scopus 로고    scopus 로고
    • Novel recombinant engineered gp41 N-terminal heptad repeat trimers and their potential as anti-HIV-1 therapeutics or microbicides
    • Chen X, Lu L, Qi Z, Lu H, Wang J, et al. (2010) Novel recombinant engineered gp41 N-terminal heptad repeat trimers and their potential as anti-HIV-1 therapeutics or microbicides. J Biol Chem 285: 25506-25515.
    • (2010) J Biol Chem , vol.285 , pp. 25506-25515
    • Chen, X.1    Lu, L.2    Qi, Z.3    Lu, H.4    Wang, J.5
  • 40
    • 45749084541 scopus 로고    scopus 로고
    • Comparative efficacy of neutralizing antibodies elicited by recombinant hemagglutinin proteins from avian H5N1 influenza virus
    • Wei CJ, Xu L, Kong WP, Shi W, Canis K, et al. (2008) Comparative efficacy of neutralizing antibodies elicited by recombinant hemagglutinin proteins from avian H5N1 influenza virus. J Virol 82: 6200-6208.
    • (2008) J Virol , vol.82 , pp. 6200-6208
    • Wei, C.J.1    Xu, L.2    Kong, W.P.3    Shi, W.4    Canis, K.5
  • 41
    • 58249100316 scopus 로고    scopus 로고
    • Cross-reactive HIV-1-neutralizing activity of serum IgG from a rabbit immunized with gp41 fused to IgG1 Fc: possible role of the prolonged half-life of the immunogen
    • Zhang MY, Wang Y, Mankowski MK, Ptak RG, Dimitrov DS, (2009) Cross-reactive HIV-1-neutralizing activity of serum IgG from a rabbit immunized with gp41 fused to IgG1 Fc: possible role of the prolonged half-life of the immunogen. Vaccine 27: 857-863.
    • (2009) Vaccine , vol.27 , pp. 857-863
    • Zhang, M.Y.1    Wang, Y.2    Mankowski, M.K.3    Ptak, R.G.4    Dimitrov, D.S.5
  • 42
    • 67649552030 scopus 로고    scopus 로고
    • Fc-receptors and immunity to malaria: from models to vaccines
    • Pleass RJ, (2009) Fc-receptors and immunity to malaria: from models to vaccines. Parasite Immunol 31: 529-538.
    • (2009) Parasite Immunol , vol.31 , pp. 529-538
    • Pleass, R.J.1
  • 43
    • 67651204591 scopus 로고    scopus 로고
    • Surface display of IgG Fc on baculovirus vectors enhances binding to antigen-presenting cells and cell lines expressing Fc receptors
    • Martyn JC, Cardin AJ, Wines BD, Cendron A, Li S, et al. (2009) Surface display of IgG Fc on baculovirus vectors enhances binding to antigen-presenting cells and cell lines expressing Fc receptors. Arch Virol 154: 1129-1138.
    • (2009) Arch Virol , vol.154 , pp. 1129-1138
    • Martyn, J.C.1    Cardin, A.J.2    Wines, B.D.3    Cendron, A.4    Li, S.5
  • 44
    • 79960563634 scopus 로고    scopus 로고
    • Recombinant HA1 produced in E.coli forms functional oligomers and generates strain-specific SRID potency antibodies for pandemic influenza vaccines
    • Khurana S, Larkin C, Verma S, Joshi MB, Fontana J, et al. (2011) Recombinant HA1 produced in E. coli forms functional oligomers and generates strain-specific SRID potency antibodies for pandemic influenza vaccines. Vaccine 29: 5657-5665.
    • (2011) Vaccine , vol.29 , pp. 5657-5665
    • Khurana, S.1    Larkin, C.2    Verma, S.3    Joshi, M.B.4    Fontana, J.5
  • 45
    • 77955280069 scopus 로고    scopus 로고
    • A recombinant mimetics of the HIV-1 gp41 prehairpin fusion intermediate fused with human IgG Fc fragment elicits neutralizing antibody response in the vaccinated mice
    • Qi Z, Pan C, Lu H, Shui Y, Li L, et al. (2010) A recombinant mimetics of the HIV-1 gp41 prehairpin fusion intermediate fused with human IgG Fc fragment elicits neutralizing antibody response in the vaccinated mice. Biochem Biophys Res Commun 398: 506-512.
    • (2010) Biochem Biophys Res Commun , vol.398 , pp. 506-512
    • Qi, Z.1    Pan, C.2    Lu, H.3    Shui, Y.4    Li, L.5
  • 46
    • 77954213672 scopus 로고    scopus 로고
    • Development of a safe and convenient neutralization assay for rapid screening of influenza HA-specific neutralizing monoclonal antibodies
    • Du L, Zhao G, Zhang X, Liu Z, Yu H, et al. (2010) Development of a safe and convenient neutralization assay for rapid screening of influenza HA-specific neutralizing monoclonal antibodies. Biochem Biophys Res Commun 397: 580-585.
    • (2010) Biochem Biophys Res Commun , vol.397 , pp. 580-585
    • Du, L.1    Zhao, G.2    Zhang, X.3    Liu, Z.4    Yu, H.5
  • 47
    • 33748794547 scopus 로고    scopus 로고
    • Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies
    • Chou TC, (2006) Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies. Pharmacol Rev 58: 621-681.
    • (2006) Pharmacol Rev , vol.58 , pp. 621-681
    • Chou, T.C.1
  • 48
    • 77957821697 scopus 로고    scopus 로고
    • Induction of protection against divergent H5N1 influenza viruses using a recombinant fusion protein linking influenza M2e to Onchocerca volvulus activation associated protein-1 (ASP-1) adjuvant
    • Zhao G, Du L, Xiao W, Sun S, Lin Y, et al. (2010) Induction of protection against divergent H5N1 influenza viruses using a recombinant fusion protein linking influenza M2e to Onchocerca volvulus activation associated protein-1 (ASP-1) adjuvant. Vaccine 28: 7233-7240.
    • (2010) Vaccine , vol.28 , pp. 7233-7240
    • Zhao, G.1    Du, L.2    Xiao, W.3    Sun, S.4    Lin, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.