메뉴 건너뛰기




Volumn 88, Issue 12, 2014, Pages 7083-7092

Alternative recognition of the conserved stem epitope in influenza a virus hemagglutinin by a VH3-30-encoded heterosubtypic antibody

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; INFLUENZA VIRUS HEMAGGLUTININ; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 3.1; UNCLASSIFIED DRUG; VIRUS ANTIBODY;

EID: 84901304592     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00178-14     Document Type: Article
Times cited : (60)

References (49)
  • 3
    • 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. http://dx.doi.org/10.1016/0092-8674(82)90135-0.
    • (1982) Cell , vol.31 , pp. 417-427
    • Caton, A.J.1    Brownlee, G.G.2    Yewdell, J.W.3    Gerhard, W.4
  • 5
    • 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, Li ZN, Nakamura K. 2001. Antigenic structure of the haemagglutinin of human influenza A/H2N2 virus. J. Gen. Virol. 82:2475-2484. http://vir.sgmjournals.org/content/82/10/2475.long.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2475-2484
    • Tsuchiya, E.1    Sugawara, K.2    Hongo, S.3    Matsuzaki, Y.4    Muraki, Y.5    Li, Z.N.6    Nakamura, K.7
  • 6
    • 75449093578 scopus 로고    scopus 로고
    • Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic
    • Xu R, McBride R, Paulson JC, Basler CF, Wilson IA. 2010. Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic. J. Virol. 84:1715-1721. http://dx.doi.org/10.1128/JVI.02162-09.
    • (2010) J. Virol. , vol.84 , pp. 1715-1721
    • Xu, R.1    McBride, R.2    Paulson, J.C.3    Basler, C.F.4    Wilson, I.A.5
  • 9
    • 84867427047 scopus 로고    scopus 로고
    • Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA
    • Julien JP, Lee PS, Wilson IA. 2012. Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA. Immunol. Rev. 250:180-198. http://dx.doi.org/10.1111/imr.12005.
    • (2012) Immunol. Rev. , vol.250 , pp. 180-198
    • Julien, J.P.1    Lee, P.S.2    Wilson, I.A.3
  • 10
    • 84867641531 scopus 로고    scopus 로고
    • Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity
    • Lee PS, Yoshida R, Ekiert DC, Sakai N, Suzuki Y, Takada A, Wilson IA. 2012. Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity. Proc. Natl. Acad. Sci. U. S. A. 109:17040-17045. http://dx.doi.org/10.1073/pnas.1212371109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 17040-17045
    • Lee, P.S.1    Yoshida, R.2    Ekiert, D.C.3    Sakai, N.4    Suzuki, Y.5    Takada, A.6    Wilson, I.A.7
  • 11
    • 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, Iba Y, Kubota-Koketsu R, Asano Y, Okuno Y, Kurosawa Y. 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. http://dx.doi.org/10.1128/JVI.05397-11.
    • (2011) J. Virol. , vol.85 , pp. 11048-11057
    • Ohshima, N.1    Iba, Y.2    Kubota-Koketsu, R.3    Asano, Y.4    Okuno, Y.5    Kurosawa, Y.6
  • 14
    • 84875186505 scopus 로고    scopus 로고
    • A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin
    • Xu R, Krause JC, McBride R, Paulson JC, Crowe JE, Jr, Wilson IA. 2013. A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin. Nat. Struct. Mol. Biol. 20:363-370. http://dx.doi.org/10.1038/nsmb.2500.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 363-370
    • Xu, R.1    Krause, J.C.2    McBride, R.3    Paulson, J.C.4    Crowe Jr., J.E.5    Wilson, I.A.6
  • 16
    • 33947590474 scopus 로고    scopus 로고
    • Scientific barriers to developing vaccines against avian influenza viruses
    • Subbarao K, Joseph T. 2007. Scientific barriers to developing vaccines against avian influenza viruses. Nat. Rev. Immunol. 7:267-278. http://dx.doi.org/10.1038/nri2054.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 267-278
    • Subbarao, K.1    Joseph, T.2
  • 18
    • 84862777115 scopus 로고    scopus 로고
    • Seroevidence for H5N1 influenza infections in humans: meta-analysis
    • Wang TT, Parides MK, Palese P. 2012. Seroevidence for H5N1 influenza infections in humans: meta-analysis. Science 335:1463. http://dx.doi.org/10.1126/science.1218888.
    • (2012) Science , vol.335 , pp. 1463
    • Wang, T.T.1    Parides, M.K.2    Palese, P.3
  • 20
    • 84889243391 scopus 로고    scopus 로고
    • Preferential recognition of avian-like receptors in human influenza A H7N9 viruses
    • Xu R, de Vries RP, Zhu X, Nycholat CM, McBride R, Yu W, Paulson JC, Wilson IA. 2013. Preferential recognition of avian-like receptors in human influenza A H7N9 viruses. Science 342:1230-1235. http://dx.doi.org/10.1126/science.1243761.
    • (2013) Science , vol.342 , pp. 1230-1235
    • Xu, R.1    de Vries, R.P.2    Zhu, X.3    Nycholat, C.M.4    McBride, R.5    Yu, W.6    Paulson, J.C.7    Wilson, I.A.8
  • 21
    • 84877920759 scopus 로고    scopus 로고
    • Structure of a classical broadly neutralizing stem antibody in complex with a pandemic H2 influenza virus hemagglutinin
    • Dreyfus C, Ekiert DC, Wilson IA. 2013. Structure of a classical broadly neutralizing stem antibody in complex with a pandemic H2 influenza virus hemagglutinin. J. Virol. 87:7149-7154. http://dx.doi.org/10.1128/JVI.02975-12.
    • (2013) J. Virol. , vol.87 , pp. 7149-7154
    • Dreyfus, C.1    Ekiert, D.C.2    Wilson, I.A.3
  • 22
    • 0027471177 scopus 로고
    • A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains
    • Okuno Y, Isegawa Y, Sasao F, Ueda S. 1993. A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. J. Virol. 67:2552-2558.
    • (1993) J. Virol. , vol.67 , pp. 2552-2558
    • Okuno, Y.1    Isegawa, Y.2    Sasao, F.3    Ueda, S.4
  • 34
    • 0035559445 scopus 로고    scopus 로고
    • Universal primer set for the full-length amplification of all influenza A viruses
    • Hoffmann E, Stech J, Guan Y, Webster RG, Perez DR. 2001. Universal primer set for the full-length amplification of all influenza A viruses. Arch. Virol. 146:2275-2289. http://dx.doi.org/10.1007/s007050170002.
    • (2001) Arch. Virol. , vol.146 , pp. 2275-2289
    • Hoffmann, E.1    Stech, J.2    Guan, Y.3    Webster, R.G.4    Perez, D.R.5
  • 35
    • 0034705225 scopus 로고    scopus 로고
    • A DNA transfection system for generation of influenza A virus from eight plasmids
    • Hoffmann E, Neumann G, Kawaoka Y, Hobom G, Webster RG. 2000. A DNA transfection system for generation of influenza A virus from eight plasmids. Proc. Natl. Acad. Sci. U. S. A. 97:6108-6113. http://dx.doi.org/10.1073/pnas.100133697.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6108-6113
    • Hoffmann, E.1    Neumann, G.2    Kawaoka, Y.3    Hobom, G.4    Webster, R.G.5
  • 37
    • 1642352884 scopus 로고    scopus 로고
    • Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus
    • Stevens J, Corper AL, Basler CF, Taubenberger JK, Palese P, Wilson IA. 2004. Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus. Science 303:1866-1870. http://dx.doi.org/10.1126/science.1093373.
    • (2004) Science , vol.303 , pp. 1866-1870
    • Stevens, J.1    Corper, A.L.2    Basler, C.F.3    Taubenberger, J.K.4    Palese, P.5    Wilson, I.A.6
  • 38
    • 63849240274 scopus 로고    scopus 로고
    • Rapid generation of fully human monoclonal antibodies specific to a vaccinating antigen
    • Smith K, Garman L, Wrammert J, Zheng NY, Capra JD, Ahmed R, Wilson PC. 2009. Rapid generation of fully human monoclonal antibodies specific to a vaccinating antigen. Nat. Protoc. 4:372-384. http://dx.doi.org/10.1038/nprot.2009.3.
    • (2009) Nat. Protoc. , vol.4 , pp. 372-384
    • Smith, K.1    Garman, L.2    Wrammert, J.3    Zheng, N.Y.4    Capra, J.D.5    Ahmed, R.6    Wilson, P.C.7
  • 39
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ. 2007. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr. 63:32-41. http://dx.doi.org/10.1107/S0907444906045975.
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 40
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr
    • Murshudov GN, Vagin AA, Dodson EJ. 1997. Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. DBiol. Crystallogr. 53:240-255. http://dx.doi.org/10.1107/S0907444996012255.
    • (1997) DBiol. Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 42
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald IK, Thornton JM. 1994. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238:777-793. http://dx.doi.org/10.1006/jmbi.1994.1334.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 43
    • 0023660979 scopus 로고
    • Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution
    • SheriffS, Hendrickson WA, Smith JL. 1987. Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution. J. Mol. Biol. 197:273-296. http://dx.doi.org/10.1016/0022-2836(87)90124-0.
    • (1987) J. Mol. Biol. , vol.197 , pp. 273-296
    • Sheriff, S.1    Hendrickson, W.A.2    Smith, J.L.3
  • 44
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly ML. 1983. Solvent-accessible surfaces of proteins and nucleic acids. Science 221:709-713. http://dx.doi.org/10.1126/science.6879170.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 45
    • 48049124972 scopus 로고    scopus 로고
    • Analysis and improvements to Kabat and structurally correct numbering of antibody variable domains
    • Abhinandan KR, Martin AC. 2008. Analysis and improvements to Kabat and structurally correct numbering of antibody variable domains. Mol. Immunol. 45:3832-3839. http://dx.doi.org/10.1016/j.molimm.2008.05.022.
    • (2008) Mol. Immunol. , vol.45 , pp. 3832-3839
    • Abhinandan, K.R.1    Martin, A.C.2
  • 49
    • 84893797938 scopus 로고    scopus 로고
    • Broadly neutralizing hemagglutinin stalk-specific antibodies require FcgammaR interactions for protection against influenza virus in vivo
    • Dilillo DJ, Tan GS, Palese P, Ravetch JV. 2014. Broadly neutralizing hemagglutinin stalk-specific antibodies require FcgammaR interactions for protection against influenza virus in vivo. Nat. Med. 20:143-151. http://dx.doi.org/10.1038/nm.3443.
    • (2014) Nat. Med. , vol.20 , pp. 143-151
    • Dilillo, D.J.1    Tan, G.S.2    Palese, P.3    Ravetch, J.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.