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Volumn 90, Issue 19, 2016, Pages 8496-8508

Unmasking stemspecific neutralizing epitopes by abolishing N-linked glycosylation sites of influenza virus hemagglutinin proteins for vaccine design

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; INFLUENZA VIRUS HEMAGGLUTININ; INFLUENZA VACCINE; NEUTRALIZING ANTIBODY; RECOMBINANT PROTEIN; RECOMBINANT VACCINE; VIRUS ANTIBODY;

EID: 84990225283     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00880-16     Document Type: Article
Times cited : (39)

References (39)
  • 1
    • 84903131264 scopus 로고    scopus 로고
    • In the shadow of hemagglutinin: a growing interest in influenza viral neuraminidase and its role as a vaccine antigen
    • Wohlbold TJ, Krammer F. 2014. In the shadow of hemagglutinin: a growing interest in influenza viral neuraminidase and its role as a vaccine antigen. Viruses 6:2465-2494. http://dx.doi.org/10.3390/v6062465
    • (2014) Viruses , vol.6 , pp. 2465-2494
    • Wohlbold, T.J.1    Krammer, F.2
  • 3
    • 77956556232 scopus 로고    scopus 로고
    • Influenza hemagglutinin and neuraminidase membrane glycoproteins
    • Gamblin SJ, Skehel JJ. 2010. Influenza hemagglutinin and neuraminidase membrane glycoproteins. J Biol Chem 285:28403-28409. http://dx.doi.org/10.1074/jbc. R110.129809
    • (2010) J Biol Chem , vol.285 , pp. 28403-28409
    • Gamblin, S.J.1    Skehel, J.J.2
  • 4
    • 84937468596 scopus 로고    scopus 로고
    • Development of framework for assessing influenza virus pandemic risk
    • Trock SC, Burke SA, Cox NJ. 2015. Development of framework for assessing influenza virus pandemic risk. Emerg Infect Dis 21:1372-1378. http://dx.doi.org/10.3201/eid2108.141086
    • (2015) Emerg Infect Dis , vol.21 , pp. 1372-1378
    • Trock, S.C.1    Burke, S.A.2    Cox, N.J.3
  • 5
    • 84924060844 scopus 로고    scopus 로고
    • Advances in the development of influenza virus vaccines
    • Krammer F, Palese P. 2015. Advances in the development of influenza virus vaccines. Nat Rev Drug Discov 14:167-182. http://dx.doi.org/10.1038/nrd4529
    • (2015) Nat Rev Drug Discov , vol.14 , pp. 167-182
    • Krammer, F.1    Palese, P.2
  • 6
    • 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. http://dx.doi.org/10.1146/annurev.biochem.69.1.531
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 7
    • 79251480393 scopus 로고    scopus 로고
    • Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain
    • Das SR, Puigbo P, Hensley SE, Hurt DE, Bennink JR, Yewdell JW. 2010. Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain. PLoS Pathog 6:e1001211. http://dx.doi.org/10.1371/journal.ppat.1001211
    • (2010) PLoS Pathog , vol.6
    • Das, S.R.1    Puigbo, P.2    Hensley, S.E.3    Hurt, D.E.4    Bennink, J.R.5    Yewdell, J.W.6
  • 9
    • 84885953445 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin stalk-based antibodies and vaccines
    • Krammer F, Palese P. 2013. Influenza virus hemagglutinin stalk-based antibodies and vaccines. Curr Opin Virol 3:521-530. http://dx.doi.org/10.1016/j.coviro.2013.07.007
    • (2013) Curr Opin Virol , vol.3 , pp. 521-530
    • Krammer, F.1    Palese, P.2
  • 11
    • 0036184705 scopus 로고    scopus 로고
    • N-glycans attached to the stem domain of haemagglutinin efficiently regulate influenza A virus replication
    • Wagner R, Heuer D, WolffT, Herwig A, Klenk HD. 2002. N-glycans attached to the stem domain of haemagglutinin efficiently regulate influenza A virus replication. J Gen Virol 83:601-609. http://dx.doi.org/10.1099/0022-1317-83-3-601
    • (2002) J Gen Virol , vol.83 , pp. 601-609
    • Wagner, R.1    Heuer, D.2    Wolff, T.3    Herwig, A.4    Klenk, H.D.5
  • 12
    • 84930473564 scopus 로고    scopus 로고
    • Role of stem glycans attached to haemagglutinin in the biological characteristics of H5N1 avian influenza virus
    • Zhang X, Chen S, Yang D, Wang X, Zhu J, Peng D, Liu X. 2015. Role of stem glycans attached to haemagglutinin in the biological characteristics of H5N1 avian influenza virus. J Gen Virol 96:1248-1257. http://dx.doi.org/10.1099/vir.0.000082
    • (2015) J Gen Virol , vol.96 , pp. 1248-1257
    • Zhang, X.1    Chen, S.2    Yang, D.3    Wang, X.4    Zhu, J.5    Peng, D.6    Liu, X.7
  • 13
    • 84902166999 scopus 로고    scopus 로고
    • Protective immunity based on the conserved hemagglutinin stalk domain and its prospects for universal influenza vaccine development
    • Khanna, M, Sharma, S, Kumar, B, Rajput, R. 2014. Protective immunity based on the conserved hemagglutinin stalk domain and its prospects for universal influenza vaccine development. Biomed Res Int 2014:546274. http://dx.doi.org/10.1155/2014/546274
    • (2014) Biomed Res Int , vol.2014
    • Khanna, M.1    Sharma, S.2    Kumar, B.3    Rajput, R.4
  • 14
    • 84877620734 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies against influenza viruses
    • Laursen NS, Wilson IA. 2013. Broadly neutralizing antibodies against influenza viruses. Antiviral Res 98:476-483. http://dx.doi.org/10.1016/j.antiviral.2013.03.021
    • (2013) Antiviral Res , vol.98 , pp. 476-483
    • Laursen, N.S.1    Wilson, I.A.2
  • 16
    • 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. 2013. Chimeric hemagglutinin influenza virus vaccine constructs elicit broadly protective stalk-specific antibodies. J Virol 87:6542-6550. http://dx.doi.org/10.1128/JVI.00641-13
    • (2013) J Virol , vol.87 , pp. 6542-6550
    • Krammer, F.1    Pica, N.2    Hai, R.3    Margine, I.4    Palese, P.5
  • 19
    • 84862220814 scopus 로고    scopus 로고
    • Broader neutralizing antibodies against H5N1 viruses using prime-boost immunization of hyperglycosylated hemagglutinin DNA and virus-like particles
    • Lin SC, Lin YF, Chong P, Wu SC. 2012. Broader neutralizing antibodies against H5N1 viruses using prime-boost immunization of hyperglycosylated hemagglutinin DNA and virus-like particles. PLoS One 7:e39075. http://dx.doi.org/10.1371/journal.pone.0039075
    • (2012) PLoS One , vol.7
    • Lin, S.C.1    Lin, Y.F.2    Chong, P.3    Wu, S.C.4
  • 20
    • 84899892665 scopus 로고    scopus 로고
    • Glycan masking of hemagglutinin for adenovirus vector and recombinant protein immunizations elicits broadly neutralizing antibodies against H5N1 avian influenza viruses
    • Lin SC, Liu WC, Jan JT, Wu SC. 2014. Glycan masking of hemagglutinin for adenovirus vector and recombinant protein immunizations elicits broadly neutralizing antibodies against H5N1 avian influenza viruses. PLoS One 9:e92822. http://dx.doi.org/10.1371/journal.pone.0092822
    • (2014) PLoS One , vol.9
    • Lin, S.C.1    Liu, W.C.2    Jan, J.T.3    Wu, S.C.4
  • 21
    • 84890874733 scopus 로고    scopus 로고
    • Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyperglycosylation of the globular head domain
    • Eggink D, GoffPH, Palese P. 2014. Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyperglycosylation of the globular head domain. J Virol 88:699-704. http://dx.doi.org/10.1128/JVI.02608-13
    • (2014) J Virol , vol.88 , pp. 699-704
    • Eggink, D.1    Goff, P.H.2    Palese, P.3
  • 26
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43. http://dx.doi.org/10.1038/371037a0
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 29
    • 84943751764 scopus 로고    scopus 로고
    • Discovering neutralizing antibodies targeting the stem epitope of H1N1 influenza hemagglutinin with synthetic phage-displayed antibody libraries
    • Tung CP, Chen IC, Yu CM, Peng HP, Jian JW, Ma SH, Lee YC, Jan JT, Yang AS. 2015. Discovering neutralizing antibodies targeting the stem epitope of H1N1 influenza hemagglutinin with synthetic phage-displayed antibody libraries. Sci Rep 5:15053. http://dx.doi.org/10.1038/srep15053
    • (2015) Sci Rep , vol.5 , pp. 15053
    • Tung, C.P.1    Chen, I.C.2    Yu, C.M.3    Peng, H.P.4    Jian, J.W.5    Ma, S.H.6    Lee, Y.C.7    Jan, J.T.8    Yang, A.S.9
  • 30
    • 78049492732 scopus 로고    scopus 로고
    • Dendritic cell activation by recombinant hemagglutinin proteins of H1N1 and H5N1 influenza A viruses
    • Liu WC, Lin SC, Yu YL, Chu CL, Wu SC. 2010. Dendritic cell activation by recombinant hemagglutinin proteins of H1N1 and H5N1 influenza A viruses. J Virol 84:12011-12017. http://dx.doi.org/10.1128/JVI.01316-10
    • (2010) J Virol , vol.84 , pp. 12011-12017
    • Liu, W.C.1    Lin, S.C.2    Yu, Y.L.3    Chu, C.L.4    Wu, S.C.5
  • 32
    • 36649037147 scopus 로고    scopus 로고
    • A dual reporter gene based system to quantitate the cell fusion of avian influenza virus H5N1
    • Su Y, Yang H, Zhang B, Qi X, Tien P. 2008. A dual reporter gene based system to quantitate the cell fusion of avian influenza virus H5N1. Biotechnol Lett 30:73-79
    • (2008) Biotechnol Lett , vol.30 , pp. 73-79
    • Su, Y.1    Yang, H.2    Zhang, B.3    Qi, X.4    Tien, P.5
  • 35
    • 84925486400 scopus 로고    scopus 로고
    • The N-linked glycosylation site at position 158 on the head of hemagglutinin and the virulence of H5N1 avian influenza virus in mice
    • Suptawiwat O, Boonarkart C, Chakritbudsabong W, Uiprasertkul M, Puthavathana P, Wiriyarat W, Auewarakul P. 2015. The N-linked glycosylation site at position 158 on the head of hemagglutinin and the virulence of H5N1 avian influenza virus in mice. Arch Virol 160:409-415. http://dx.doi.org/10.1007/s00705-014-2306-x
    • (2015) Arch Virol , vol.160 , pp. 409-415
    • Suptawiwat, O.1    Boonarkart, C.2    Chakritbudsabong, W.3    Uiprasertkul, M.4    Puthavathana, P.5    Wiriyarat, W.6    Auewarakul, P.7
  • 36
    • 80051921486 scopus 로고    scopus 로고
    • Specific sites of N-linked glycosylation on the hemagglutinin of H1N1 subtype influenza A virus determine sensitivity to inhibitors of the innate immune system and virulence in mice
    • Tate MD, Brooks AG, Reading PC. 2011. Specific sites of N-linked glycosylation on the hemagglutinin of H1N1 subtype influenza A virus determine sensitivity to inhibitors of the innate immune system and virulence in mice. J Immunol 187:1884-1894. http://dx.doi.org/10.4049/jimmunol.1100295
    • (2011) J Immunol , vol.187 , pp. 1884-1894
    • Tate, M.D.1    Brooks, A.G.2    Reading, P.C.3
  • 37
    • 77953297916 scopus 로고    scopus 로고
    • Glycosylation at 158N of the hemagglutinin protein and receptor binding specificity synergistically affect the antigenicity and immunogenicity of a live attenuated H5N1 A/Vietnam/1203/2004 vaccine virus in ferrets
    • Wang W, Lu B, Zhou H, Suguitan AL, Jr, Cheng X, Subbarao K, Kemble G, Jin H. 2010. Glycosylation at 158N of the hemagglutinin protein and receptor binding specificity synergistically affect the antigenicity and immunogenicity of a live attenuated H5N1 A/Vietnam/1203/2004 vaccine virus in ferrets. J Virol 84:6570-6577. http://dx.doi.org/10.1128/JVI.00221-10
    • (2010) J Virol , vol.84 , pp. 6570-6577
    • Wang, W.1    Lu, B.2    Zhou, H.3    Suguitan, A.L.4    Cheng, X.5    Subbarao, K.6    Kemble, G.7    Jin, H.8
  • 38
    • 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
  • 39
    • 84956934982 scopus 로고    scopus 로고
    • Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection
    • DiLillo DJ, Palese P, Wilson PC, Ravetch JV. 2016. Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection. J Clin Invest 126:605-610. http://dx.doi.org/10.1172/JCI84428
    • (2016) J Clin Invest , vol.126 , pp. 605-610
    • DiLillo, D.J.1    Palese, P.2    Wilson, P.C.3    Ravetch, J.V.4


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