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Volumn 20, Issue 3, 2013, Pages 363-370

A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin

Author keywords

[No Author keywords available]

Indexed keywords

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

EID: 84875186505     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2500     Document Type: Article
Times cited : (128)

References (45)
  • 1
    • 84882628111 scopus 로고    scopus 로고
    • Advances in the development of universal influenza vaccines
    • published online, doi:10.1111/irv.12013 (24 September)
    • Gilbert, S.C. Advances in the development of universal influenza vaccines. Influenza Other Respi. Viruses published online, doi:10.1111/irv.12013 (24 September 2012).
    • (2012) Influenza Other Respi. Viruses
    • Gilbert, S.C.1
  • 2
    • 84859510667 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies against influenza virus and prospects for universal therapies
    • Ekiert, D.C. & Wilson, I.A. Broadly neutralizing antibodies against influenza virus and prospects for universal therapies. Curr. Opin. Virol. 2, 134-141 (2012).
    • (2012) Curr. Opin. Virol , vol.2 , pp. 134-141
    • Ekiert, D.C.1    Wilson, I.A.2
  • 3
    • 84866740262 scopus 로고    scopus 로고
    • Recent progress in structure-based anti-influenza drug design
    • Du, J., Cross, T.A. & Zhou, H.X. Recent progress in structure-based anti-influenza drug design. Drug Discov. Today 17, 1111-1120 (2012).
    • (2012) Drug Discov. Today , vol.17 , pp. 1111-1120
    • Du, J.1    Cross, T.A.2    Zhou, H.X.3
  • 4
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J.J. & Wiley, D. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69, 531-569 (2000).
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.2
  • 5
    • 0000545033 scopus 로고
    • Interactions of animal viruses with cell surface receptors
    • (Academic Press,)
    • Paulson, J.C. Interactions of animal viruses with cell surface receptors. in The Receptors Vol. 2, 131-219 (Academic Press, 1985).
    • (1985) The Receptors , vol.2 , pp. 131-219
    • Paulson, J.C.1
  • 6
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis, W. et al. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333, 426-431 (1988).
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1
  • 7
    • 0037341410 scopus 로고    scopus 로고
    • Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding
    • Matrosovich, M. & Klenk, H.D. Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding. Rev. Med. Virol. 13, 85-97 (2003).
    • (2003) Rev. Med. Virol , vol.13 , pp. 85-97
    • Matrosovich, M.1    Klenk, H.D.2
  • 8
    • 0024466223 scopus 로고
    • Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: A 500-MHz proton nuclear magnetic resonance study
    • Sauter, N.K. et al. Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance study. Biochemistry 28, 8388-8396 (1989).
    • (1989) Biochemistry , vol.28 , pp. 8388-8396
    • Sauter, N.K.1
  • 9
    • 34247530859 scopus 로고    scopus 로고
    • Virus glycosylation: Role in virulence and immune interactions
    • Vigerust, D.J. & Shepherd, V.L. Virus glycosylation: role in virulence and immune interactions. Trends Microbiol. 15, 211-218 (2007).
    • (2007) Trends Microbiol , vol.15 , pp. 211-218
    • Vigerust, D.J.1    Shepherd, V.L.2
  • 10
    • 33748925430 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity
    • Sagar, M., Wu, X., Lee, S. & Overbaugh, J. Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity. J. Virol. 80, 9586-9598 (2006).
    • (2006) J. Virol , vol.80 , pp. 9586-9598
    • Sagar, M.1    Wu, X.2    Lee, S.3    Overbaugh, J.4
  • 11
    • 0025246369 scopus 로고
    • Structural basis of immune recognition of influenza virus hemagglutinin
    • Wilson, I.A. & Cox, N.J. Structural basis of immune recognition of influenza virus hemagglutinin. Annu. Rev. Immunol. 8, 737-771 (1990).
    • (1990) Annu. Rev. Immunol , vol.8 , pp. 737-771
    • Wilson, I.A.1    Cox, N.J.2
  • 12
    • 80052184942 scopus 로고    scopus 로고
    • Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin
    • Whittle, J.R. et al. Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin. Proc. Natl. Acad. Sci. USA 108, 14216-14221 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 14216-14221
    • Whittle, J.R.1
  • 13
    • 84866953140 scopus 로고    scopus 로고
    • Cross-neutralization of influenza A viruses mediated by a single antibody loop
    • Ekiert, D.C. et al. Cross-neutralization of influenza A viruses mediated by a single antibody loop. Nature 489, 526-532 (2012).
    • (2012) Nature , vol.489 , pp. 526-532
    • Ekiert, D.C.1
  • 14
    • 84867641531 scopus 로고    scopus 로고
    • Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity
    • Lee, P.S. et al. Heterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidity. Proc. Natl. Acad. Sci. USA 109, 17040-17045 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 17040-17045
    • Lee, P.S.1
  • 15
    • 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. 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).
    • (2011) J. Virol , vol.85 , pp. 11048-11057
    • Ohshima, N.1
  • 16
    • 84863568230 scopus 로고    scopus 로고
    • Human monoclonal antibodies to pandemic 1957 H2N2 and pandemic 1968 H3N2 influenza viruses
    • Krause, J.C. et al. Human monoclonal antibodies to pandemic 1957 H2N2 and pandemic 1968 H3N2 influenza viruses. J. Virol. 86, 6334-6340 (2012).
    • (2012) J. Virol , vol.86 , pp. 6334-6340
    • Krause, J.C.1
  • 17
    • 63449125762 scopus 로고    scopus 로고
    • Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses
    • Yoshida, R. et al. Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses. PLoS Pathog. 5, e1000350 (2009).
    • (2009) PLoS Pathog , vol.5
    • Yoshida, R.1
  • 18
    • 0014127288 scopus 로고
    • Excess pneumonia-influenza mortality by age and sex in three major influenza A2 epidemics, United States, 1957-58, 1960 and 1963
    • Serfling, R.E., Sherman, I.L. & Houseworth, W.J. Excess pneumonia-influenza mortality by age and sex in three major influenza A2 epidemics, United States, 1957-58, 1960 and 1963. Am. J. Epidemiol. 86, 433-441 (1967).
    • (1967) Am. J. Epidemiol , vol.86 , pp. 433-441
    • Serfling, R.E.1    Sherman, I.L.2    Houseworth, W.J.3
  • 19
    • 0016213790 scopus 로고
    • Excess mortality from epidemic influenza, 1957-1966
    • Housworth, J. & Langmuir, A.D. Excess mortality from epidemic influenza, 1957-1966. Am. J. Epidemiol. 100, 40-48 (1974).
    • (1974) Am. J. Epidemiol , vol.100 , pp. 40-48
    • Housworth, J.1    Langmuir, A.D.2
  • 20
    • 0031870067 scopus 로고    scopus 로고
    • Pandemic versus epidemic influenza mortality: A pattern of changing age distribution
    • Simonsen, L. et al. Pandemic versus epidemic influenza mortality: a pattern of changing age distribution. J. Infect. Dis. 178, 53-60 (1998).
    • (1998) J. Infect. Dis , vol.178 , pp. 53-60
    • Simonsen, L.1
  • 21
    • 79952394551 scopus 로고    scopus 로고
    • Vaccinate for the next H2N2 pandemic now
    • Nabel, G.J., Wei, C.J. & Ledgerwood, J.E. Vaccinate for the next H2N2 pandemic now. Nature 471, 157-158 (2011).
    • (2011) Nature , vol.471 , pp. 157-158
    • Nabel, G.J.1    Wei, C.J.2    Ledgerwood, J.E.3
  • 22
    • 0027198796 scopus 로고
    • Origin of the pandemic 1957 H2 influenza A virus and the persistence of its possible progenitors in the avian reservoir
    • Schäfer, J.R. et al. Origin of the pandemic 1957 H2 influenza A virus and the persistence of its possible progenitors in the avian reservoir. Virology 194, 781-788 (1993).
    • (1993) Virology , vol.194 , pp. 781-788
    • Schäfer, J.R.1
  • 23
    • 38049173100 scopus 로고    scopus 로고
    • Identification of H2N3 influenza A viruses from swine in the United States
    • Ma, W. et al. Identification of H2N3 influenza A viruses from swine in the United States. Proc. Natl. Acad. Sci. USA 104, 20949-20954 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20949-20954
    • Ma, W.1
  • 24
    • 0033937519 scopus 로고    scopus 로고
    • Cross-protection and reassortment studies with avian H2 influenza viruses
    • Kaverin, N.V. et al. Cross-protection and reassortment studies with avian H2 influenza viruses. Arch. Virol. 145, 1059-1066 (2000).
    • (2000) Arch. Virol , vol.145 , pp. 1059-1066
    • Kaverin, N.V.1
  • 25
    • 12144290520 scopus 로고    scopus 로고
    • Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120
    • Huang, C.C. et al. Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120. Proc. Natl. Acad. Sci. USA 101, 2706-2711 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2706-2711
    • Huang, C.C.1
  • 26
    • 0035865521 scopus 로고    scopus 로고
    • (H)1-69 gene is preferentially used by hepatitis C virus-associated B cell lymphomas and by normal B cells responding to the E2 viral antigen
    • Chan, C.H., Hadlock, K.G., Foung, S.K. & Levy, S.V. (H)1-69 gene is preferentially used by hepatitis C virus-associated B cell lymphomas and by normal B cells responding to the E2 viral antigen. Blood 97, 1023-1026 (2001).
    • (2001) Blood , vol.97 , pp. 1023-1026
    • Chan, C.H.1    Hadlock, K.G.2    Foung, S.K.3    Levy, S.V.4
  • 27
    • 0035403970 scopus 로고    scopus 로고
    • Immunoglobulin gene mutations and frequent use of VH1-69 and VH4-34 segments in hepatitis C virus-positive and hepatitis C virus-negative nodal marginal zone B-cell lymphoma
    • Marasca, R. et al. Immunoglobulin gene mutations and frequent use of VH1-69 and VH4-34 segments in hepatitis C virus-positive and hepatitis C virus-negative nodal marginal zone B-cell lymphoma. Am. J. Pathol. 159, 253-261 (2001).
    • (2001) Am. J. Pathol , vol.159 , pp. 253-261
    • Marasca, R.1
  • 28
    • 18744399909 scopus 로고    scopus 로고
    • Hepatitis C virus drives the unconstrained monoclonal expansion of VH1-69-expressing memory B cells in type II cryoglobulinemia: A model of infection-driven lymphomagenesis
    • Carbonari, M. et al. Hepatitis C virus drives the unconstrained monoclonal expansion of VH1-69-expressing memory B cells in type II cryoglobulinemia: a model of infection-driven lymphomagenesis. J. Immunol. 174, 6532-6539 (2005).
    • (2005) J. Immunol , vol.174 , pp. 6532-6539
    • Carbonari, M.1
  • 29
    • 33847101745 scopus 로고    scopus 로고
    • Structural definition of a conserved neutralization epitope on HIV-1 gp120
    • Zhou, T. et al. Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature 445, 732-737 (2007).
    • (2007) Nature , vol.445 , pp. 732-737
    • Zhou, T.1
  • 30
    • 33746810900 scopus 로고    scopus 로고
    • Structural basis for HIV-1 neutralization by a gp41 fusion intermediate-directed antibody
    • Luftig, M.A. et al. Structural basis for HIV-1 neutralization by a gp41 fusion intermediate-directed antibody. Nat. Struct. Mol. Biol. 13, 740-747 (2006).
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 740-747
    • Luftig, M.A.1
  • 31
    • 64849114224 scopus 로고    scopus 로고
    • Antibody recognition of a highly conserved influenza virus epitope
    • Ekiert, D.C. et al. Antibody recognition of a highly conserved influenza virus epitope. Science 324, 246-251 (2009).
    • (2009) Science , vol.324 , pp. 246-251
    • Ekiert, D.C.1
  • 32
    • 62049083943 scopus 로고    scopus 로고
    • Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses
    • Sui, J. et al. Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nat. Struct. Mol. Biol. 16, 265-273 (2009).
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 265-273
    • Sui, J.1
  • 33
    • 43149109969 scopus 로고    scopus 로고
    • Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies
    • Kashyap, A.K. et al. Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies. Proc. Natl. Acad. Sci. 105, 5986-5991 (2008).
    • (2008) Proc. Natl. Acad. Sci , vol.105 , pp. 5986-5991
    • Kashyap, A.K.1
  • 34
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (2007).
    • (2007) J. Mol. Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 35
    • 75449093578 scopus 로고    scopus 로고
    • Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic
    • Xu, R., McBride, R., Paulson, J.C., Basler, C.F. & Wilson, I.A. Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic. J. Virol. 84, 1715-1721 (2010).
    • (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
  • 36
    • 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. A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. J. Virol. 67, 2552-2558 (1993).
    • (1993) J. Virol , vol.67 , pp. 2552-2558
    • Okuno, Y.1    Isegawa, Y.2    Sasao, F.3    Ueda, S.4
  • 37
    • 0021675932 scopus 로고
    • Characterization of H2 influenza virus hemagglutinin with monoclonal antibodies: Influence of receptor specificity
    • Yamada, A., Brown, L.E. & Webster, R.G. Characterization of H2 influenza virus hemagglutinin with monoclonal antibodies: influence of receptor specificity. Virology 138, 276-286 (1984).
    • (1984) Virology , vol.138 , pp. 276-286
    • Yamada, A.1    Brown, L.E.2    Webster, R.G.3
  • 38
    • 80053557269 scopus 로고    scopus 로고
    • Epitope-specific human influenza antibody repertoires diversify by B cell intraclonal sequence divergence and interclonal convergence
    • Krause, J.C. et al. Epitope-specific human influenza antibody repertoires diversify by B cell intraclonal sequence divergence and interclonal convergence. J. Immunol. 187, 3704-3711 (2011).
    • (2011) J. Immunol , vol.187 , pp. 3704-3711
    • Krause, J.C.1
  • 39
    • 70350132189 scopus 로고    scopus 로고
    • Structures of receptor complexes formed by hemagglutinins from the Asian Influenza pandemic of 1957
    • Liu, J. et al. Structures of receptor complexes formed by hemagglutinins from the Asian Influenza pandemic of 1957. Proc. Natl. Acad. Sci. USA 106, 17175-17180 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 17175-17180
    • Liu, J.1
  • 40
    • 77951165843 scopus 로고    scopus 로고
    • Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus
    • Xu, R. et al. Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus. Science 328, 357-360 (2010).
    • (2010) Science , vol.328 , pp. 357-360
    • Xu, R.1
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams, P.D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D Biol. Crystallogr. 58, 1948-1954 (2002).
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 44
  • 45
    • 84856875534 scopus 로고    scopus 로고
    • Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic
    • Xu, R., McBride, R., Nycholat, C.M., Paulson, J.C. & Wilson, I.A. Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic. J. Virol. 86, 982-990 (2012).
    • (2012) J. Virol , vol.86 , pp. 982-990
    • Xu, R.1    McBride, R.2    Nycholat, C.M.3    Paulson, J.C.4    Wilson, I.A.5


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