메뉴 건너뛰기




Volumn 109, Issue 42, 2012, Pages 17040-17045

Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity

Author keywords

[No Author keywords available]

Indexed keywords

CROSS REACTING ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G; INFLUENZA VIRUS HEMAGGLUTININ; NEUTRALIZING ANTIBODY;

EID: 84867641531     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1212371109     Document Type: Article
Times cited : (150)

References (42)
  • 1
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson IA, Skehel JJ, Wiley DC (1981) Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 2
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis W, et al. (1988) Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333:426-431.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1
  • 3
    • 0019860749 scopus 로고
    • Sequence relationships among the hemagglutinin genes of 12 subtypes of influenza A virus
    • Air GM (1981) Sequence relationships among the hemagglutinin genes of 12 subtypes of influenza A virus. Proc Natl Acad Sci USA 78:7639-7643.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 7639-7643
    • Air, G.M.1
  • 4
    • 0026175939 scopus 로고
    • Comparison of complete amino acid sequences and re-ceptor- Binding properties among 13 serotypes of hemagglutinins of influenza A viruses
    • Nobusawa E, et al. (1991) Comparison of complete amino acid sequences and re-ceptor- binding properties among 13 serotypes of hemagglutinins of influenza A viruses. Virology 182:475- 485.
    • (1991) Virology , vol.182 , pp. 475-485
    • Nobusawa, E.1
  • 5
    • 84863230485 scopus 로고    scopus 로고
    • A distinct lineage of influenza A virus from bats
    • Tong S, et al. (2012) A distinct lineage of influenza A virus from bats. Proc Natl Acad Sci USA 109:4269-4274.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 4269-4274
    • Tong, S.1
  • 6
    • 47049092748 scopus 로고    scopus 로고
    • The contents of the syringe
    • Salzberg S (2008) The contents of the syringe. Nature 454:160-161.
    • (2008) Nature , vol.454 , pp. 160-161
    • Salzberg, S.1
  • 7
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
    • DOI 10.1038/289373a0
    • 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. (Pubitemid 11135143)
    • (1981) Nature , vol.289 , Issue.5796 , pp. 373-378
    • Wiley, D.C.1    Wilson, I.A.2
  • 8
    • 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
  • 9
    • 84859510667 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies against influenza virus and prospects for universal therapies
    • Ekiert DC, Wilson IA (2012) Broadly neutralizing antibodies against influenza virus and prospects for universal therapies. Curr Opin Virol 2:134-141.
    • (2012) Curr Opin Virol , vol.2 , pp. 134-141
    • Ekiert, D.C.1    Wilson, I.A.2
  • 10
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley DC, Skehel JJ (1987) The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu Rev Biochem 56:365-394.
    • (1987) Annu Rev Biochem , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 12
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • DOI 10.1038/371037a0
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC (1994) Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43. (Pubitemid 24277462)
    • (1994) Nature , vol.371 , Issue.6492 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 13
    • 0029026358 scopus 로고
    • Structure of influenza virus haemagglutinin complexed with a neutralizing antibody
    • Bizebard T, et al. (1995) Structure of influenza virus haemagglutinin complexed with a neutralizing antibody. Nature 376:92-94.
    • (1995) Nature , vol.376 , pp. 92-94
    • Bizebard, T.1
  • 15
    • 77951165843 scopus 로고    scopus 로고
    • Structural basis of preexisting immunity to the 2009 H1N1 pandemic infl uenza virus
    • Xu R, et al. (2010) Structural basis of preexisting immunity to the 2009 H1N1 pandemic infl uenza virus. Science 328:357-360.
    • (2010) Science , vol.328 , pp. 357-360
    • Xu, R.1
  • 16
    • 80052184942 scopus 로고    scopus 로고
    • Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin
    • Whittle JR, et al. (2011) Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin. Proc Natl Acad Sci USA 108:14216-14221.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 14216-14221
    • Whittle, J.R.1
  • 17
    • 64849114224 scopus 로고    scopus 로고
    • Antibody recognition of a highly conserved influenza virus epitope
    • Ekiert DC, et al. (2009) Antibody recognition of a highly conserved influenza virus epitope. Science 324:246-251.
    • (2009) Science , vol.324 , pp. 246-251
    • Ekiert, D.C.1
  • 18
    • 80051635697 scopus 로고    scopus 로고
    • A highly conserved neutralizing epitope on group 2 influenza A viruses
    • Ekiert DC, et al. (2011) A highly conserved neutralizing epitope on group 2 influenza A viruses. Science 333:843-850.
    • (2011) Science , vol.333 , pp. 843-850
    • Ekiert, D.C.1
  • 19
    • 84866122029 scopus 로고    scopus 로고
    • Highly conserved protective epitopes on influenza B viruses
    • Dreyfus C, et al. (2012) Highly conserved protective epitopes on influenza B viruses. Science 337:1343-1348.
    • (2012) Science , vol.337 , pp. 1343-1348
    • Dreyfus, C.1
  • 20
    • 80051670323 scopus 로고    scopus 로고
    • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 infl uenza A hemagglutinins
    • Corti D, et al. (2011) A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 infl uenza A hemagglutinins. Science 333:850-856.
    • (2011) Science , vol.333 , pp. 850-856
    • Corti, D.1
  • 22
    • 58049198443 scopus 로고    scopus 로고
    • Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells
    • Throsby M, 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
  • 23
    • 62049083943 scopus 로고    scopus 로고
    • Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses
    • Sui J, 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
  • 24
    • 77957678820 scopus 로고    scopus 로고
    • Protection from the 2009 H1N1 pandemic infl uenza by an antibody from combinatorial survivor-based libraries
    • Kashyap AK, et al. (2010) Protection from the 2009 H1N1 pandemic infl uenza by an antibody from combinatorial survivor-based libraries. PLoS Pathog 6:e1000990.
    • (2010) PLoS Pathog , vol.6
    • Kashyap, A.K.1
  • 25
    • 77951876927 scopus 로고    scopus 로고
    • Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine
    • Corti D, et al. (2010) Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine. J Clin Invest 120:1663-1673.
    • (2010) J Clin Invest , vol.120 , pp. 1663-1673
    • Corti, D.1
  • 26
    • 78651488739 scopus 로고    scopus 로고
    • Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection
    • Wrammert J, et al. (2011) Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection. J Exp Med 208:181-193.
    • (2011) J Exp Med , vol.208 , pp. 181-193
    • Wrammert, J.1
  • 27
    • 77956119219 scopus 로고    scopus 로고
    • Induction of broadly neutralizing H1N1 influenza antibodies by vaccination
    • Wei CJ, et al. (2010) Induction of broadly neutralizing H1N1 influenza antibodies by vaccination. Science 329:1060-1064.
    • (2010) Science , vol.329 , pp. 1060-1064
    • Wei, C.J.1
  • 28
    • 33645399959 scopus 로고    scopus 로고
    • Safety and immunogenicity of an inactivated subvirion influenza A (H5N1) vaccine
    • Treanor JJ, Campbell JD, Zangwill KM, Rowe T,Wolff M(2006) Safety and immunogenicity of an inactivated subvirion influenza A (H5N1) vaccine. N Engl J Med 354:1343-1351.
    • (2006) N Engl J Med , vol.354 , pp. 1343-1351
    • Treanor, J.J.1    Campbell, J.D.2    Zangwill, K.M.3    Rowe, T.4    Wolff, M.5
  • 29
    • 63449125762 scopus 로고    scopus 로고
    • Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of infl uenza A viruses
    • Yoshida R, et al. (2009) Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of infl uenza A viruses. PLoS Pathog 5:e1000350.
    • (2009) PLoS Pathog , vol.5
    • Yoshida, R.1
  • 30
    • 80055111172 scopus 로고    scopus 로고
    • Naturally occurring antibodies in humans can neutralize a variety of influenza virus strains, including H3, H1, H2, and H5
    • Ohshima N, et al. (2011) Naturally occurring antibodies in humans can neutralize a variety of influenza virus strains, including H3, H1, H2, and H5. J Virol 85:11048-11057.
    • (2011) J Virol , vol.85 , pp. 11048-11057
    • Ohshima, N.1
  • 31
    • 80053474133 scopus 로고    scopus 로고
    • A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of the influenza H1N1 virus hemagglutinin
    • Krause JC, et al. (2011) A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of the influenza H1N1 virus hemagglutinin. J Virol 85:10905-10908.
    • (2011) J Virol , vol.85 , pp. 10905-10908
    • Krause, J.C.1
  • 32
    • 80053557269 scopus 로고    scopus 로고
    • Epitope-specific human influenza antibody repertoires diversify by B cell intraclonal sequence divergence and interclonal convergence
    • Krause JC, et al. (2011) Epitope-specific human influenza antibody repertoires diversify by B cell intraclonal sequence divergence and interclonal convergence. J Immunol 187:3704-3711.
    • (2011) J Immunol , vol.187 , pp. 3704-3711
    • Krause, J.C.1
  • 33
    • 84866953140 scopus 로고    scopus 로고
    • Cross-neutralization of influenza A viruses mediated by a single antibody loop
    • Ekiert DC, et al. (2012) Cross-neutralization of influenza A viruses mediated by a single antibody loop. Nature 489:526-532.
    • (2012) Nature , vol.489 , pp. 526-532
    • Ekiert, D.C.1
  • 34
    • 0038240827 scopus 로고    scopus 로고
    • X-ray structure of the hemagglutinin of a potential H3 avian progenitor of the 1968 Hong Kong pandemic influenza virus
    • DOI 10.1016/S0042-6822(03)00068-0
    • Ha Y, Stevens DJ, Skehel JJ, Wiley DC (2003) X-ray structure of the hemagglutinin of a potential H3 avian progenitor of the 1968 Hong Kong pandemic influenza virus. Virology 309:209-218. (Pubitemid 36579216)
    • (2003) Virology , vol.309 , Issue.2 , pp. 209-218
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 36
    • 0033053331 scopus 로고    scopus 로고
    • A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the virus receptor binding site
    • DOI 10.1038/9299
    • Fleury D, et al. (1999) A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the virus receptor binding site. Nat Struct Biol 6:530-534. (Pubitemid 29252830)
    • (1999) Nature Structural Biology , vol.6 , Issue.6 , pp. 530-534
    • Fleury, D.1    Barrere, B.2    Bizebard, T.3    Daniels, R.S.4    Skehel, J.J.5    Knossow, M.6
  • 37
    • 84863568230 scopus 로고    scopus 로고
    • Human monoclonal antibodies to pandemic 1957 H2N2 and pandemic 1968 H3N2 influenza viruses
    • Krause JC, et al. (2012) Human monoclonal antibodies to pandemic 1957 H2N2 and pandemic 1968 H3N2 influenza viruses. J Virol 86:6334-6340.
    • (2012) J Virol , vol.86 , pp. 6334-6340
    • Krause, J.C.1
  • 38
    • 79952394551 scopus 로고    scopus 로고
    • Vaccinate for the next H2N2 pandemic now
    • Nabel GJ, Wei CJ, Ledgerwood JE (2011) Vaccinate for the next H2N2 pandemic now. Nature 471:157-158.
    • (2011) Nature , vol.471 , pp. 157-158
    • Nabel, G.J.1    Wei, C.J.2    Ledgerwood, J.E.3
  • 40
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • Zhu P, et al. (2006) Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 441:847-852.
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1
  • 41
    • 66149132686 scopus 로고    scopus 로고
    • Examination of the contributions of size and avidity to the neutralization mechanisms of the anti-HIV antibodies b12 and 4E10
    • Klein JS, et al. (2009) Examination of the contributions of size and avidity to the neutralization mechanisms of the anti-HIV antibodies b12 and 4E10. Proc Natl Acad Sci USA 106:7385-7390.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7385-7390
    • Klein, J.S.1
  • 42
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66:12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.