메뉴 건너뛰기




Volumn 7, Issue , 2016, Pages

A broadly neutralizing anti-influenza antibody reveals ongoing capacity of haemagglutinin-specific memory B cells to evolve

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; FC RECEPTOR; IGHV3 30 PROTEIN; IMMUNOGLOBULIN G1; INFLUENZA VIRUS HEMAGGLUTININ; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 3114; NEUTRALIZING ANTIBODY; PROTEIN; TRYPSIN; UNCLASSIFIED DRUG; VIRUS ANTIBODY; VLD94N PROTEIN; INFLUENZA VACCINE; PROTEIN BINDING;

EID: 84987781434     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms12780     Document Type: Article
Times cited : (72)

References (55)
  • 1
    • 84987831110 scopus 로고    scopus 로고
    • WHO revised, March, 2003 (updated 19 October 2011) Available at
    • WHO. WHO Influenza Fact Sheet No. 211, revised March 2003 (updated 19 October 2011). Available at http://www. who. int/mediacentre/factsheets/2003/fs211/en/(2011).
    • (2011) WHO Influenza Fact Sheet , vol.211
  • 3
    • 0033574008 scopus 로고    scopus 로고
    • 1918 Spanish influenza: The secrets remain elusive
    • Webster, R. G. 1918 Spanish influenza: the secrets remain elusive. Proc. Natl Acad. Sci. USA 96, 1164-1166 (1999).
    • (1999) Proc. Natl Acad. Sci.s USA , vol.96 , pp. 1164-1166
    • Webster, R.G.1
  • 4
    • 51449086295 scopus 로고    scopus 로고
    • The biology of influenza viruses
    • Bouvier, N. M., Palese, P. The biology of influenza viruses. Vaccine 26 (Suppl 4): D49-D53 (2008).
    • (2008) Vaccine , vol.26 , pp. D49-D53
    • Bouvier, N.M.1    Palese, P.2
  • 5
    • 33847044691 scopus 로고    scopus 로고
    • The evolution of epidemic influenza
    • Nelson, M. I., Holmes, E. C. The evolution of epidemic influenza. Nat. Rev. Genet. 8, 196-205 (2007).
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 196-205
    • Nelson, M.I.1    Holmes, E.C.2
  • 6
    • 84887290174 scopus 로고    scopus 로고
    • New world bats harbor diverse influenza A viruses
    • Tong, S. et al. New world bats harbor diverse influenza A viruses. PLoS Pathog. 9, e1003657 (2013).
    • (2013) PLoS Pathog , vol.9 , pp. 1003657
    • Tong, S.1
  • 8
    • 77956499048 scopus 로고    scopus 로고
    • Influenza virus evolution, host adaptation, and pandemic formation
    • Taubenberger, J. K., Kash, J. C. Influenza virus evolution, host adaptation, and pandemic formation. Cell Host Microbe 7, 440-451 (2010).
    • (2010) Cell Host Microbe , vol.7 , pp. 440-451
    • Taubenberger, J.K.1    Kash, J.C.2
  • 9
    • 0022477122 scopus 로고
    • Measurement of the mutation rates of animal viruses: Influenza A virus and poliovirus type 1
    • Parvin, J. D., Moscona, A., Pan, W. T., Leider, J. M., Palese, P. Measurement of the mutation rates of animal viruses: influenza A virus and poliovirus type 1. J. Virol. 59, 377-383 (1986).
    • (1986) J. Virol. , vol.59 , pp. 377-383
    • Parvin, J.D.1    Moscona, A.2    Pan, W.T.3    Leider, J.M.4    Palese, P.5
  • 10
    • 70350595871 scopus 로고    scopus 로고
    • Hemagglutinin receptor binding avidity drives influenza A virus antigenic drift
    • Hensley, S. E. et al. Hemagglutinin receptor binding avidity drives influenza A virus antigenic drift. Science 326, 734-736 (2009).
    • (2009) Science , vol.326 , pp. 734-736
    • Hensley, S.E.1
  • 12
    • 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
  • 13
    • 77949365750 scopus 로고    scopus 로고
    • New class of monoclonal antibodies against severe influenza: Prophylactic and therapeutic efficacy in ferrets
    • Friesen, R. H. et al. New class of monoclonal antibodies against severe influenza: prophylactic and therapeutic efficacy in ferrets. PLoS ONE 5, e9106 (2010).
    • (2010) PLoS ONE , vol.5 , pp. 9106
    • Friesen, R.H.1
  • 14
    • 80051635697 scopus 로고    scopus 로고
    • A highly conserved neutralizing epitope on group 2 influenza A viruses
    • Ekiert, D. C. et al. A highly conserved neutralizing epitope on group 2 influenza A viruses. Science 333, 843-850 (2011).
    • (2011) Science , vol.333 , pp. 843-850
    • Ekiert, D.C.1
  • 15
    • 80051670323 scopus 로고    scopus 로고
    • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins
    • Corti, D. et al. A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins. Science 333, 850-856 (2011).
    • (2011) Science , vol.333 , pp. 850-856
    • Corti, D.1
  • 16
    • 84866122029 scopus 로고    scopus 로고
    • Highly conserved protective epitopes on influenza B viruses
    • Dreyfus, C. et al. Highly conserved protective epitopes on influenza B viruses. Science 337, 1343-1348 (2012).
    • (2012) Science , vol.337 , pp. 1343-1348
    • Dreyfus, C.1
  • 17
    • 84880427552 scopus 로고    scopus 로고
    • An in vivo human-plasmablast enrichment technique allows rapid identification of therapeutic influenza A antibodies
    • Nakamura, G. et al. An in vivo human-plasmablast enrichment technique allows rapid identification of therapeutic influenza A antibodies. Cell Host Microbe 14, 93-103 (2013).
    • (2013) Cell Host Microbe , vol.14 , pp. 93-103
    • Nakamura, G.1
  • 18
    • 84901304592 scopus 로고    scopus 로고
    • Alternative recognition of the conserved stem epitope in influenza A virus hemagglutinin by a VH3-30-encoded heterosubtypic antibody
    • Wyrzucki, A. et al. Alternative recognition of the conserved stem epitope in influenza A virus hemagglutinin by a VH3-30-encoded heterosubtypic antibody. J. Virol. 88, 7083-7092 (2014).
    • (2014) J. Virol. , vol.88 , pp. 7083-7092
    • Wyrzucki, A.1
  • 19
    • 84923172342 scopus 로고    scopus 로고
    • Heterosubtypic antibodies to influenza A virus have limited activity against cell-bound virus but are not impaired by strain-specific serum antibodies
    • Wyrzucki, A., Bianchi, M., Kohler, I., Steck, M., Hangartner, L. Heterosubtypic antibodies to influenza A virus have limited activity against cell-bound virus but are not impaired by strain-specific serum antibodies. J. Virol. 89, 3136-3144 (2015).
    • (2015) J. Virol. , vol.89 , pp. 3136-3144
    • Wyrzucki, A.1    Bianchi, M.2    Kohler, I.3    Steck, M.4    Hangartner, L.5
  • 20
    • 84937684824 scopus 로고    scopus 로고
    • A potent broad-spectrum protective human monoclonal antibody crosslinking two haemagglutinin monomers of influenza A virus
    • Wu, Y. et al. A potent broad-spectrum protective human monoclonal antibody crosslinking two haemagglutinin monomers of influenza A virus. Nat. Commun. 6, 7708 (2015).
    • (2015) Nat. Commun. , vol.6 , pp. 7708
    • Wu, Y.1
  • 21
    • 84924034216 scopus 로고    scopus 로고
    • Preexisting human antibodies neutralize recently emerged H7N9 influenza strains
    • Henry Dunand, C. J. et al. Preexisting human antibodies neutralize recently emerged H7N9 influenza strains. J. Clin. Invest. 125, 1255-1268 (2015).
    • (2015) J. Clin. Invest. , vol.125 , pp. 1255-1268
    • Henry Dunand, C.J.1
  • 22
    • 69949151874 scopus 로고    scopus 로고
    • A rapid and efficient single-cell manipulation method for screening antigen-specific antibody-secreting cells from human peripheral blood
    • Jin, A. et al. A rapid and efficient single-cell manipulation method for screening antigen-specific antibody-secreting cells from human peripheral blood. Nat. Med. 15, 1088-1092 (2009).
    • (2009) Nat. Med. , vol.15 , pp. 1088-1092
    • Jin, A.1
  • 23
    • 63849240274 scopus 로고    scopus 로고
    • Rapid generation of fully human monoclonal antibodies specific to a vaccinating antigen
    • Smith, K. et al. Rapid generation of fully human monoclonal antibodies specific to a vaccinating antigen. Nat. Protoc. 4, 372-384 (2009).
    • (2009) Nat. Protoc. , vol.4 , pp. 372-384
    • Smith, K.1
  • 25
    • 0032033127 scopus 로고    scopus 로고
    • Humoral immunity due to long-lived plasma cells
    • Slifka, M. K., Antia, R., Whitmire, J. K., Ahmed, R. Humoral immunity due to long-lived plasma cells. Immunity 8, 363-372 (1998).
    • (1998) Immunity , vol.8 , pp. 363-372
    • Slifka, M.K.1    Antia, R.2    Whitmire, J.K.3    Ahmed, R.4
  • 26
    • 84855512128 scopus 로고    scopus 로고
    • Memory B cells, but not long-lived plasma cells, possess antigen specificities for viral escape mutants
    • Purtha, W. E., Tedder, T. F., Johnson, S., Bhattacharya, D., Diamond, M. S. Memory B cells, but not long-lived plasma cells, possess antigen specificities for viral escape mutants. J. Exp. Med. 208, 2599-2606 (2011).
    • (2011) J. Exp. Med. , vol.208 , pp. 2599-2606
    • Purtha, W.E.1    Tedder, T.F.2    Johnson, S.3    Bhattacharya, D.4    Diamond, M.S.5
  • 27
    • 84888799995 scopus 로고    scopus 로고
    • Both mutated and unmutated memory B cells accumulate mutations in the course of the secondary response and develop a new antibody repertoire optimally adapted to the secondary stimulus
    • Kaji, T. et al. Both mutated and unmutated memory B cells accumulate mutations in the course of the secondary response and develop a new antibody repertoire optimally adapted to the secondary stimulus. Int. Immunol. 25, 683-695 (2013).
    • (2013) Int. Immunol. , vol.25 , pp. 683-695
    • Kaji, T.1
  • 28
    • 84874092680 scopus 로고    scopus 로고
    • Lineage structure of the human antibody repertoire in response to influenza vaccination
    • Jiang, N. et al. Lineage structure of the human antibody repertoire in response to influenza vaccination. Sci. Trans. Med. 5, 171-119 (2013).
    • (2013) Sci. Trans. Med. , vol.5 , pp. 119-171
    • Jiang, N.1
  • 29
    • 84922225958 scopus 로고    scopus 로고
    • Rapid development of broadly influenza neutralizing antibodies through redundant mutations
    • Pappas, L. et al. Rapid development of broadly influenza neutralizing antibodies through redundant mutations. Nature. 516, 418-22 (2014).
    • (2014) Nature , vol.516 , pp. 418-422
    • Pappas, L.1
  • 30
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J., Wiley, D. C. 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.C.2
  • 31
    • 0028123337 scopus 로고
    • Host cell proteases controlling virus pathogenicity
    • Klenk, H. D., Garten, W. Host cell proteases controlling virus pathogenicity. Trends Microbiol. 2, 39-43 (1994).
    • (1994) Trends Microbiol. , vol.2 , pp. 39-43
    • Klenk, H.D.1    Garten, W.2
  • 32
    • 0015862870 scopus 로고
    • Proteolytic cleavage by plasmin of the HA polypeptide of influenza virus: Host cell activation of serum plasminogen
    • Lazarowitz, S. G., Goldberg, A. R., Choppin, P. W. Proteolytic cleavage by plasmin of the HA polypeptide of influenza virus: host cell activation of serum plasminogen. Virology 56, 172-180 (1973).
    • (1973) Virology , vol.56 , pp. 172-180
    • Lazarowitz, S.G.1    Goldberg, A.R.2    Choppin, P.W.3
  • 33
    • 84893797938 scopus 로고    scopus 로고
    • Broadly neutralizing hemagglutinin stalk-specific antibodies require FcgammaR interactions for protection against influenza virus in vivo
    • DiLillo, D. J., Tan, G. S., Palese, P., Ravetch, J. V. Broadly neutralizing hemagglutinin stalk-specific antibodies require FcgammaR interactions for protection against influenza virus in vivo. Nat. Med. 20, 143-151 (2014).
    • (2014) Nat. Med. , vol.20 , pp. 143-151
    • DiLillo, D.J.1    Tan, G.S.2    Palese, P.3    Ravetch, J.V.4
  • 34
    • 84904460487 scopus 로고    scopus 로고
    • Antibody structure determination using a combination of homology modeling, energy-based refinement, and loop prediction
    • Zhu, K. et al. Antibody structure determination using a combination of homology modeling, energy-based refinement, and loop prediction. Proteins 82, 1646-1655 (2014).
    • (2014) Proteins , vol.82 , pp. 1646-1655
    • Zhu, K.1
  • 35
    • 48449105393 scopus 로고    scopus 로고
    • The RosettaDock server for local protein-protein docking
    • Lyskov, S., Gray, J. J. The RosettaDock server for local protein-protein docking. Nucleic Acids Res. 36, W233-W238 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. W233-W238
    • Lyskov, S.1    Gray, J.J.2
  • 36
    • 34547572513 scopus 로고    scopus 로고
    • FastContact: A free energy scoring tool for protein-protein complex structures
    • Champ, P. C., Camacho, C. J. FastContact: a free energy scoring tool for protein-protein complex structures. Nucleic Acids Res. 35, W556-W560 (2007).
    • (2007) Nucleic Acids Res. , vol.35 , pp. W556-W560
    • Champ, P.C.1    Camacho, C.J.2
  • 37
    • 84861872090 scopus 로고    scopus 로고
    • Pandemic H1N1 influenza vaccine induces a recall response in humans that favors broadly cross-reactive memory B cells
    • Li, G. M. et al. Pandemic H1N1 influenza vaccine induces a recall response in humans that favors broadly cross-reactive memory B cells. Proc. Natl Acad. Sci. USA 109, 9047-9052 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 9047-9052
    • Li, G.M.1
  • 38
    • 77951876927 scopus 로고    scopus 로고
    • Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine
    • Corti, D. et al. Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine. J. Clin. Invest. 120, 1663-1673 (2010).
    • (2010) J. Clin. Invest. , vol.120 , pp. 1663-1673
    • Corti, D.1
  • 39
    • 84901687604 scopus 로고    scopus 로고
    • Molecular signatures of hemagglutinin stem-directed heterosubtypic human neutralizing antibodies against influenza A viruses
    • Avnir, Y. et al. Molecular signatures of hemagglutinin stem-directed heterosubtypic human neutralizing antibodies against influenza A viruses. PLoS Pathog. 10, e1004103 (2014).
    • (2014) PLoS Pathog , vol.10 , pp. 1004103
    • Avnir, Y.1
  • 40
    • 84866949036 scopus 로고    scopus 로고
    • Structural and genetic basis for development of broadly neutralizing influenza antibodies
    • Lingwood, D. et al. Structural and genetic basis for development of broadly neutralizing influenza antibodies. Nature 489, 566-570 (2012).
    • (2012) Nature , vol.489 , pp. 566-570
    • Lingwood, D.1
  • 41
    • 33746574474 scopus 로고    scopus 로고
    • Targeting of somatic hypermutation
    • Odegard, V. H., Schatz, D. G. Targeting of somatic hypermutation. Nat. Rev. Immunol. 6, 573-583 (2006).
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 573-583
    • Odegard, V.H.1    Schatz, D.G.2
  • 42
    • 0023161403 scopus 로고
    • Timing, genetic requirements and functional consequences of somatic hypermutation during B-cell development
    • Allen, D. et al. Timing, genetic requirements and functional consequences of somatic hypermutation during B-cell development. Immunol. Rev. 96, 5-22 (1987).
    • (1987) Immunol. Rev. , vol.96 , pp. 5-22
    • Allen, D.1
  • 43
    • 84908389429 scopus 로고    scopus 로고
    • Induction of broadly reactive anti-hemagglutinin stalk antibodies by an H5N1 vaccine in humans
    • Nachbagauer, R. et al. Induction of broadly reactive anti-hemagglutinin stalk antibodies by an H5N1 vaccine in humans. J. Virol. 88, 13260-13268 (2014).
    • (2014) J. Virol. , vol.88 , pp. 13260-13268
    • Nachbagauer, R.1
  • 44
    • 84878611784 scopus 로고    scopus 로고
    • Chimeric hemagglutinin influenza virus vaccine constructs elicit broadly protective stalk-specific antibodies
    • Krammer, F., Pica, N., Hai, R., Margine, I., Palese, P. Chimeric hemagglutinin influenza virus vaccine constructs elicit broadly protective stalk-specific antibodies. J. Virol. 87, 6542-6550 (2013).
    • (2013) J. Virol. , vol.87 , pp. 6542-6550
    • Krammer, F.1    Pica, N.2    Hai, R.3    Margine, I.4    Palese, P.5
  • 45
    • 84941023600 scopus 로고    scopus 로고
    • Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection
    • Yassine, H. M. et al. Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection. Nat. Med. 21, 1065-1070 (2015).
    • (2015) Nat. Med. , vol.21 , pp. 1065-1070
    • Yassine, H.M.1
  • 46
    • 84941873935 scopus 로고    scopus 로고
    • A stable trimeric influenza hemagglutinin stem as a broadly protective immunogen
    • Impagliazzo, A. et al. A stable trimeric influenza hemagglutinin stem as a broadly protective immunogen. Science 349, 1301-1306 (2015).
    • (2015) Science , vol.349 , pp. 1301-1306
    • Impagliazzo, A.1
  • 47
    • 84872924387 scopus 로고    scopus 로고
    • 1976 and 2009 H1N1 influenza virus vaccines boost anti-hemagglutinin stalk antibodies in humans
    • Miller, M. S. et al. 1976 and 2009 H1N1 influenza virus vaccines boost anti-hemagglutinin stalk antibodies in humans. J. Infect. Dis. 207, 98-105 (2013).
    • (2013) J. Infect. Dis. , vol.207 , pp. 98-105
    • Miller, M.S.1
  • 48
    • 84901400888 scopus 로고    scopus 로고
    • Influence of pre-existing hemagglutination inhibition titers against historical influenza strains on antibody response to inactivated trivalent influenza vaccine in adults 50-80 years of age
    • Ross, T. M. et al. Influence of pre-existing hemagglutination inhibition titers against historical influenza strains on antibody response to inactivated trivalent influenza vaccine in adults 50-80 years of age. Hum. Vaccin. Immunother. 10, 1195-1203 (2014).
    • (2014) Hum. Vaccin. Immunother. , vol.10 , pp. 1195-1203
    • Ross, T.M.1
  • 49
    • 84887976550 scopus 로고    scopus 로고
    • The kinase mTOR modulates the antibody response to provide cross-protective immunity to lethal infection with influenza virus
    • Keating, R. et al. The kinase mTOR modulates the antibody response to provide cross-protective immunity to lethal infection with influenza virus. Nat. Immunol. 14, 1266-1276 (2013).
    • (2013) Nat. Immunol. , vol.14 , pp. 1266-1276
    • Keating, R.1
  • 50
    • 84919756169 scopus 로고    scopus 로고
    • MTOR inhibition improves immune function in the elderly
    • Mannick, J. B. et al. mTOR inhibition improves immune function in the elderly. Sci. Transl. Med. 6, 268ra179 (2014).
    • (2014) Sci. Transl. Med. , vol.6 , pp. 179-268
    • Mannick, J.B.1
  • 51
    • 84958292295 scopus 로고    scopus 로고
    • IGHV1-69 polymorphism modulates anti-influenza antibody repertoires, correlates with IGHV utilization shifts and varies by ethnicity
    • Avnir, Y. et al. IGHV1-69 polymorphism modulates anti-influenza antibody repertoires, correlates with IGHV utilization shifts and varies by ethnicity. Sci. Rep. 6, 20842 (2016).
    • (2016) Sci. Rep. , vol.6 , pp. 20842
    • Avnir, Y.1
  • 52
    • 84949936325 scopus 로고    scopus 로고
    • An Anti-influenza virus antibody inhibits viral infection by reducing nucleus entry of influenza nucleoprotein
    • Yoon, A. et al. An Anti-influenza virus antibody inhibits viral infection by reducing nucleus entry of influenza nucleoprotein. PLoS ONE 10, e0141312 (2015).
    • (2015) PLoS ONE , vol.10 , pp. 0141312
    • Yoon, A.1
  • 53
    • 36849031722 scopus 로고    scopus 로고
    • Efficient generation of monoclonal antibodies from single human B cells by single cell RT-PCR and expression vector cloning
    • Tiller, T. et al. Efficient generation of monoclonal antibodies from single human B cells by single cell RT-PCR and expression vector cloning. J. Immunol. Methods 329, 112-124 (2008).
    • (2008) J. Immunol. Methods , vol.329 , pp. 112-124
    • Tiller, T.1
  • 54
    • 0028057250 scopus 로고
    • Depletion of B cells in vivo by a chimeric mouse human monoclonal antibody to CD20
    • Reff, M. E. et al. Depletion of B cells in vivo by a chimeric mouse hsuman monoclonal antibody to CD20. Blood 83, 435-445 (1994).
    • (1994) Blood , vol.83 , pp. 435-445
    • Reff, M.E.1
  • 55
    • 84914152611 scopus 로고    scopus 로고
    • Development of a robust reporter-based ADCC assay with frozen, thaw-and-use cells to measure Fc effector function of therapeutic antibodies
    • Cheng, Z. J. et al. Development of a robust reporter-based ADCC assay with frozen, thaw-and-use cells to measure Fc effector function of therapeutic antibodies. J. Immunol. Methods 414, 69-81 (2014).
    • (2014) J. Immunol. Methods , vol.414 , pp. 69-81
    • Cheng, Z.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.