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Volumn 7, Issue 5, 2012, Pages

The epitope and neutralization mechanism of AVFLuIgG01, a broad-reactive human monoclonal antibody against H5N1 influenza virus

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; INFLUENZA VIRUS HEMAGGLUTININ; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY AVFLULGG01; UNCLASSIFIED DRUG;

EID: 84861475076     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0038126     Document Type: Article
Times cited : (23)

References (39)
  • 1
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
    • Wiley DC, Wilson IA, Skehel JJ, (1981) Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature 289: 373-378.
    • (1981) Nature , vol.289 , pp. 373-378
    • Wiley, D.C.1    Wilson, I.A.2    Skehel, J.J.3
  • 2
    • 0020416123 scopus 로고
    • The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype)
    • Caton AJ, Brownlee GG, Yewdell JW, Gerhard W, (1982) The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype). Cell 31: 417-427.
    • (1982) Cell , vol.31 , pp. 417-427
    • Caton, A.J.1    Brownlee, G.G.2    Yewdell, J.W.3    Gerhard, W.4
  • 3
    • 0034795117 scopus 로고    scopus 로고
    • Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus
    • Tsuchiya E, Sugawara K, Hongo S, Matsuzaki Y, Muraki Y, et al. (2001) Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus. J Gen Virol 82: 2475-2484.
    • (2001) J Gen Virol , vol.82 , pp. 2475-2484
    • Tsuchiya, E.1    Sugawara, K.2    Hongo, S.3    Matsuzaki, Y.4    Muraki, Y.5
  • 4
    • 0025369455 scopus 로고
    • Hemagglutinin mutations related to attenuation and altered cell tropism of a virulent avian influenza A virus
    • Philpott M, Hioe C, Sheerar M, Hinshaw VS, (1990) Hemagglutinin mutations related to attenuation and altered cell tropism of a virulent avian influenza A virus. J Virol 64: 2941-2947.
    • (1990) J Virol , vol.64 , pp. 2941-2947
    • Philpott, M.1    Hioe, C.2    Sheerar, M.3    Hinshaw, V.S.4
  • 5
    • 0035949581 scopus 로고    scopus 로고
    • X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs
    • Ha Y, Stevens DJ, Skehel JJ, Wiley DC, (2001) X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proc Natl Acad Sci U S A 98: 11181-11186.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11181-11186
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 6
    • 0036500549 scopus 로고    scopus 로고
    • H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes
    • Ha Y, Stevens DJ, Skehel JJ, Wiley DC, (2002) H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes. EMBO J 21: 865-875.
    • (2002) EMBO J , vol.21 , pp. 865-875
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 7
    • 0036771639 scopus 로고    scopus 로고
    • Structure of antigenic sites on the haemagglutinin molecule of H5 avian influenza virus and phenotypic variation of escape mutants
    • Kaverin NV, Rudneva IA, Ilyushina NA, Varich NL, Lipatov AS, et al. (2002) Structure of antigenic sites on the haemagglutinin molecule of H5 avian influenza virus and phenotypic variation of escape mutants. J Gen Virol 83: 2497-2505.
    • (2002) J Gen Virol , vol.83 , pp. 2497-2505
    • Kaverin, N.V.1    Rudneva, I.A.2    Ilyushina, N.A.3    Varich, N.L.4    Lipatov, A.S.5
  • 8
    • 36349018925 scopus 로고    scopus 로고
    • Epitope mapping of the hemagglutinin molecule of a highly pathogenic H5N1 influenza virus by using monoclonal antibodies
    • Kaverin NV, Rudneva IA, Govorkova EA, Timofeeva TA, Shilov AA, et al. (2007) Epitope mapping of the hemagglutinin molecule of a highly pathogenic H5N1 influenza virus by using monoclonal antibodies. J Virol 81: 12911-12917.
    • (2007) J Virol , vol.81 , pp. 12911-12917
    • Kaverin, N.V.1    Rudneva, I.A.2    Govorkova, E.A.3    Timofeeva, T.A.4    Shilov, A.A.5
  • 10
    • 33750721332 scopus 로고    scopus 로고
    • Meta-analysis: convalescent blood products for Spanish influenza pneumonia: a future H5N1 treatment?
    • Luke TC, Kilbane EM, Jackson JL, Hoffman SL, (2006) Meta-analysis: convalescent blood products for Spanish influenza pneumonia: a future H5N1 treatment? Ann Intern Med 145: 599-609.
    • (2006) Ann Intern Med , vol.145 , pp. 599-609
    • Luke, T.C.1    Kilbane, E.M.2    Jackson, J.L.3    Hoffman, S.L.4
  • 11
    • 34948813121 scopus 로고    scopus 로고
    • Treatment with convalescent plasma for influenza A (H5N1) infection
    • Zhou B, Zhong N, Guan Y, (2007) Treatment with convalescent plasma for influenza A (H5N1) infection. N Engl J Med 357: 1450-1451.
    • (2007) N Engl J Med , vol.357 , pp. 1450-1451
    • Zhou, B.1    Zhong, N.2    Guan, Y.3
  • 12
    • 65549170411 scopus 로고    scopus 로고
    • Generation, characterization and epitope mapping of two neutralizing and protective human recombinant antibodies against influenza A H5N1 viruses
    • Sun L, Lu X, Li C, Wang M, Liu Q, et al. (2009) Generation, characterization and epitope mapping of two neutralizing and protective human recombinant antibodies against influenza A H5N1 viruses. PLoS One 4: e5476.
    • (2009) PLoS One , vol.4
    • Sun, L.1    Lu, X.2    Li, C.3    Wang, M.4    Liu, Q.5
  • 13
    • 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
  • 14
    • 74449089618 scopus 로고    scopus 로고
    • Exploring peptide mimics for the production of antibodies against discontinuous protein epitopes
    • Irving MB, Craig L, Menendez A, Gangadhar BP, Montero M, et al. (2010) Exploring peptide mimics for the production of antibodies against discontinuous protein epitopes. Mol Immunol 47: 1137-1148.
    • (2010) Mol Immunol , vol.47 , pp. 1137-1148
    • Irving, M.B.1    Craig, L.2    Menendez, A.3    Gangadhar, B.P.4    Montero, M.5
  • 15
    • 34249886331 scopus 로고    scopus 로고
    • Stepwise prediction of conformational discontinuous B-cell epitopes using the Mapitope algorithm
    • Bublil EM, Freund NT, Mayrose I, Penn O, Roitburd-Berman A, et al. (2007) Stepwise prediction of conformational discontinuous B-cell epitopes using the Mapitope algorithm. Proteins 68: 294-304.
    • (2007) Proteins , vol.68 , pp. 294-304
    • Bublil, E.M.1    Freund, N.T.2    Mayrose, I.3    Penn, O.4    Roitburd-Berman, A.5
  • 16
    • 60649084396 scopus 로고    scopus 로고
    • Pep-3D-Search: a method for B-cell epitope prediction based on mimotope analysis
    • Huang YX, Bao YL, Guo SY, Wang Y, Zhou CG, et al. (2008) Pep-3D-Search: a method for B-cell epitope prediction based on mimotope analysis. BMC Bioinformatics 9: 538.
    • (2008) BMC Bioinformatics , vol.9 , pp. 538
    • Huang, Y.X.1    Bao, Y.L.2    Guo, S.Y.3    Wang, Y.4    Zhou, C.G.5
  • 17
    • 84863229743 scopus 로고    scopus 로고
    • A Human Antibody Recognizing a Conserved Epitope of H5 Hemagglutinin Broadly Neutralizes Highly Pathogenic Avian Influenza H5N1 Viruses
    • Hu H, Voss J, Zhang G, Buchy P, Zuo T, et al. (2012) A Human Antibody Recognizing a Conserved Epitope of H5 Hemagglutinin Broadly Neutralizes Highly Pathogenic Avian Influenza H5N1 Viruses. J Virol 86: 2978-2989.
    • (2012) J Virol , vol.86 , pp. 2978-2989
    • Hu, H.1    Voss, J.2    Zhang, G.3    Buchy, P.4    Zuo, T.5
  • 18
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin
    • Skehel JJ, Wiley DC, (2000) Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69: 531-569.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 20
    • 21644473491 scopus 로고    scopus 로고
    • Epitope mapping
    • Morris GE, (2005) Epitope mapping. Methods Mol Biol 295: 255-268.
    • (2005) Methods Mol Biol , vol.295 , pp. 255-268
    • Morris, G.E.1
  • 21
    • 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
  • 22
    • 33744941072 scopus 로고    scopus 로고
    • Antigenic and immunogenic characterization of recombinant baculovirus-expressed severe acute respiratory syndrome coronavirus spike protein: implication for vaccine design
    • He Y, Li J, Heck S, Lustigman S, Jiang S, (2006) Antigenic and immunogenic characterization of recombinant baculovirus-expressed severe acute respiratory syndrome coronavirus spike protein: implication for vaccine design. J Virol 80: 5757-5767.
    • (2006) J Virol , vol.80 , pp. 5757-5767
    • He, Y.1    Li, J.2    Heck, S.3    Lustigman, S.4    Jiang, S.5
  • 23
    • 70349383960 scopus 로고    scopus 로고
    • Recombinant receptor-binding domain of SARS-CoV spike protein expressed in mammalian, insect and E. coli cells elicits potent neutralizing antibody and protective immunity
    • Du L, Zhao G, Chan CC, Sun S, Chen M, et al. (2009) Recombinant receptor-binding domain of SARS-CoV spike protein expressed in mammalian, insect and E. coli cells elicits potent neutralizing antibody and protective immunity. Virology 393: 144-150.
    • (2009) Virology , vol.393 , pp. 144-150
    • Du, L.1    Zhao, G.2    Chan, C.C.3    Sun, S.4    Chen, M.5
  • 24
    • 80053596320 scopus 로고    scopus 로고
    • Influenza vaccines: what do we want and how can we get it?
    • Geeraedts F, Huckriede A, (2011) Influenza vaccines: what do we want and how can we get it? Adv Exp Med Biol 780: 161-174.
    • (2011) Adv Exp Med Biol , vol.780 , pp. 161-174
    • Geeraedts, F.1    Huckriede, A.2
  • 25
    • 70350459697 scopus 로고    scopus 로고
    • One step closer to universal influenza epitopes
    • Li OT, Poon LL, (2009) One step closer to universal influenza epitopes. Expert Rev Anti Infect Ther 7: 687-690.
    • (2009) Expert Rev Anti Infect Ther , vol.7 , pp. 687-690
    • Li, O.T.1    Poon, L.L.2
  • 26
    • 66149085695 scopus 로고    scopus 로고
    • Mapping antibody epitopes of the avian H5N1 influenza virus
    • Yen HL, Peiris JS, (2009) Mapping antibody epitopes of the avian H5N1 influenza virus. PLoS Med 6: e1000064.
    • (2009) PLoS Med , vol.6
    • Yen, H.L.1    Peiris, J.S.2
  • 27
    • 34249669303 scopus 로고    scopus 로고
    • Prophylactic and therapeutic efficacy of human monoclonal antibodies against H5N1 influenza
    • Simmons CP, Bernasconi NL, Suguitan AL, Mills K, Ward JM, et al. (2007) Prophylactic and therapeutic efficacy of human monoclonal antibodies against H5N1 influenza. PLoS Med 4: e178.
    • (2007) PLoS Med , vol.4
    • Simmons, C.P.1    Bernasconi, N.L.2    Suguitan, A.L.3    Mills, K.4    Ward, J.M.5
  • 28
    • 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
  • 29
    • 43149109969 scopus 로고    scopus 로고
    • Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies
    • Kashyap AK, Steel J, Oner AF, Dillon MA, Swale RE, et al. (2008) Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies. Proc Natl Acad Sci U S A 105: 5986-5991.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5986-5991
    • Kashyap, A.K.1    Steel, J.2    Oner, A.F.3    Dillon, M.A.4    Swale, R.E.5
  • 30
    • 56049097199 scopus 로고    scopus 로고
    • Neutralizing human monoclonal antibody against H5N1 influenza HA selected from a Fab-phage display library
    • Lim AP, Chan CE, Wong SK, Chan AH, Ooi EE, et al. (2008) Neutralizing human monoclonal antibody against H5N1 influenza HA selected from a Fab-phage display library. Virol J 5: 130.
    • (2008) Virol J , vol.5 , pp. 130
    • Lim, A.P.1    Chan, C.E.2    Wong, S.K.3    Chan, A.H.4    Ooi, E.E.5
  • 31
    • 58049198443 scopus 로고    scopus 로고
    • Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells
    • Throsby M, van den Brink E, Jongeneelen M, Poon LL, Alard P, et al. (2008) Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells. PLoS One 3: e3942.
    • (2008) PLoS One , vol.3
    • Throsby, M.1    van den Brink, E.2    Jongeneelen, M.3    Poon, L.L.4    Alard, P.5
  • 32
    • 0034535166 scopus 로고    scopus 로고
    • Two influenza A virus-specific Fabs neutralize by inhibiting virus attachment to target cells, while neutralization by their IgGs is complex and occurs simultaneously through fusion inhibition and attachment inhibition
    • Edwards MJ, Dimmock NJ, (2000) Two influenza A virus-specific Fabs neutralize by inhibiting virus attachment to target cells, while neutralization by their IgGs is complex and occurs simultaneously through fusion inhibition and attachment inhibition. Virology 278: 423-435.
    • (2000) Virology , vol.278 , pp. 423-435
    • Edwards, M.J.1    Dimmock, N.J.2
  • 33
    • 0034785732 scopus 로고    scopus 로고
    • Hemagglutinin 1-specific immunoglobulin G and Fab molecules mediate postattachment neutralization of influenza A virus by inhibition of an early fusion event
    • Edwards MJ, Dimmock NJ, (2001) Hemagglutinin 1-specific immunoglobulin G and Fab molecules mediate postattachment neutralization of influenza A virus by inhibition of an early fusion event. J Virol 75: 10208-10218.
    • (2001) J Virol , vol.75 , pp. 10208-10218
    • Edwards, M.J.1    Dimmock, N.J.2
  • 34
    • 0034983229 scopus 로고    scopus 로고
    • A haemagglutinin (HA1)-specific FAb neutralizes influenza A virus by inhibiting fusion activity
    • Edwards MJ, Dimmock NJ, (2001) A haemagglutinin (HA1)-specific FAb neutralizes influenza A virus by inhibiting fusion activity. J Gen Virol 82: 1387-1395.
    • (2001) J Gen Virol , vol.82 , pp. 1387-1395
    • Edwards, M.J.1    Dimmock, N.J.2
  • 35
    • 62749124125 scopus 로고    scopus 로고
    • Monoclonal antibodies against the fusion peptide of hemagglutinin protect mice from lethal influenza A virus H5N1 infection
    • Prabhu N, Prabakaran M, Ho HT, Velumani S, Qiang J, et al. (2009) Monoclonal antibodies against the fusion peptide of hemagglutinin protect mice from lethal influenza A virus H5N1 infection. J Virol 83: 2553-2562.
    • (2009) J Virol , vol.83 , pp. 2553-2562
    • Prabhu, N.1    Prabakaran, M.2    Ho, H.T.3    Velumani, S.4    Qiang, J.5
  • 36
    • 33847623088 scopus 로고    scopus 로고
    • Antibodies specific to the HA2 glycopolypeptide of influenza A virus haemagglutinin with fusion-inhibition activity contribute to the protection of mice against lethal infection
    • Gocnik M, Fislova T, Sladkova T, Mucha V, Kostolansky F, et al. (2007) Antibodies specific to the HA2 glycopolypeptide of influenza A virus haemagglutinin with fusion-inhibition activity contribute to the protection of mice against lethal infection. J Gen Virol 88: 951-955.
    • (2007) J Gen Virol , vol.88 , pp. 951-955
    • Gocnik, M.1    Fislova, T.2    Sladkova, T.3    Mucha, V.4    Kostolansky, F.5
  • 37
    • 77955011794 scopus 로고    scopus 로고
    • An antibody against a novel and conserved epitope in the hemagglutinin 1 subunit neutralizes numerous H5N1 influenza viruses
    • Oh HL, Akerstrom S, Shen S, Bereczky S, Karlberg H, et al. (2010) An antibody against a novel and conserved epitope in the hemagglutinin 1 subunit neutralizes numerous H5N1 influenza viruses. J Virol 84: 8275-8286.
    • (2010) J Virol , vol.84 , pp. 8275-8286
    • Oh, H.L.1    Akerstrom, S.2    Shen, S.3    Bereczky, S.4    Karlberg, H.5
  • 38
    • 84862908396 scopus 로고    scopus 로고
    • Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like protease
    • Bertram S, Glowacka I, Muller MA, Lavender H, Gnirss K, et al. (2011) Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like protease. J Virol 85: 13363-13372.
    • (2011) J Virol , vol.85 , pp. 13363-13372
    • Bertram, S.1    Glowacka, I.2    Muller, M.A.3    Lavender, H.4    Gnirss, K.5
  • 39
    • 79954628266 scopus 로고    scopus 로고
    • Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response
    • Glowacka I, Bertram S, Muller MA, Allen P, Soilleux E, et al. (2011) Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response. J Virol 85: 4122-4134.
    • (2011) J Virol , vol.85 , pp. 4122-4134
    • Glowacka, I.1    Bertram, S.2    Muller, M.A.3    Allen, P.4    Soilleux, E.5


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