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Volumn 88, Issue 1, 2014, Pages 699-704

Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyperglycosylation of the globular head domain

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOLOGICAL ADJUVANT; INFLUENZA VACCINE; POLYINOSINIC POLYCYTIDYLIC ACID; VIRUS HEMAGGLUTININ;

EID: 84890874733     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02608-13     Document Type: Article
Times cited : (147)

References (38)
  • 4
    • 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
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
    • 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. http://dx.doi .org/10.1038/289373a0.
    • (1981) Nature , vol.289 , pp. 373-378
    • Wiley, D.C.1    Wilson, I.A.2    Skehel, J.J.3
  • 11
    • 84863597077 scopus 로고    scopus 로고
    • A pan-H1 anti-hemagglutinin monoclonal antibody with potent broad-spectrum efficacy in vivo
    • Tan GS, Krammer F, Eggink D, Kongchanagul A, Moran TM, Palese P. 2012. A pan-H1 anti-hemagglutinin monoclonal antibody with potent broad-spectrum efficacy in vivo. J. Virol. 86:6179-6188. http://dx.doi.org /10.1128/JVI.00469-12.
    • (2012) J. Virol. , vol.86 , pp. 6179-6188
    • Tan, G.S.1    Krammer, F.2    Eggink, D.3    Kongchanagul, A.4    Moran, T.M.5    Palese, P.6
  • 13
    • 77649242815 scopus 로고    scopus 로고
    • Broadly protective monoclonal antibodies against H3 influenza viruses following sequential immunization with different hemagglutinins
    • Wang TT, Tan GS, Hai R, Pica N, Petersen E, Moran TM, Palese P. 2010. Broadly protective monoclonal antibodies against H3 influenza viruses following sequential immunization with different hemagglutinins. PLoS Pathog. 6:e1000796. http://dx.doi.org/10.1371/journal.ppat.1000796.
    • (2010) PLoS Pathog. , vol.6
    • Wang, T.T.1    Tan, G.S.2    Hai, R.3    Pica, N.4    Petersen, E.5    Moran, T.M.6    Palese, P.7
  • 14
    • 78649989474 scopus 로고    scopus 로고
    • Induction of unnatural immunity: prospects for a broadly protective universal influenza vaccine
    • Nabel GJ, Fauci AS. 2010. Induction of unnatural immunity: prospects for a broadly protective universal influenza vaccine. Nat.Med.16:1389-1391. http: //dx.doi.org/10.1038/nm1210-1389.
    • (2010) Nat.Med. , vol.16 , pp. 1389-1391
    • Nabel, G.J.1    Fauci, A.S.2
  • 15
    • 80455168614 scopus 로고    scopus 로고
    • Why do influenza virus subtypes die out? A hypothesis
    • Palese P, Wang TT. 2011. Why do influenza virus subtypes die out? A hypothesis. mBio 2(5):e00150-11. http://dx.doi.org/10.1128/mBio.00150-11.
    • (2011) mBio 2 , vol.5
    • Palese, P.1    Wang, T.T.2
  • 16
    • 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
  • 17
    • 84861302846 scopus 로고    scopus 로고
    • Evidence for N-glycan shielding of antigenic sites during evolution of human influenza A virus hemagglutinin
    • Kobayashi Y, Suzuki Y. 2012. Evidence for N-glycan shielding of antigenic sites during evolution of human influenza A virus hemagglutinin. J. Virol. 86:3446-3451. http://dx.doi.org/10.1128/JVI.06147-11.
    • (2012) J. Virol. , vol.86 , pp. 3446-3451
    • Kobayashi, Y.1    Suzuki, Y.2
  • 19
    • 0003746861 scopus 로고
    • A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody
    • Skehel JJ, Stevens DJ, Daniels RS, Douglas AR, Knossow M, Wilson IA, Wiley DC. 1984. A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody. Proc. Natl. Acad. Sci. U. S. A. 81:1779-1783. http://dx.doi.org/10.1073 /pnas.81.6.1779.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 1779-1783
    • Skehel, J.J.1    Stevens, D.J.2    Daniels, R.S.3    Douglas, A.R.4    Knossow, M.5    Wilson, I.A.6    Wiley, D.C.7
  • 21
    • 84857606264 scopus 로고    scopus 로고
    • Positive selection for gains of N-linked glycosylation sites in hemagglutinin during evolution of H3N2 human influenza A virus
    • Suzuki Y. 2011. Positive selection for gains of N-linked glycosylation sites in hemagglutinin during evolution of H3N2 human influenza A virus. Genes Genet. Syst. 86:287-294. http://dx.doi.org/10.1266/ggs.86.287.
    • (2011) Genes Genet. Syst. , vol.86 , pp. 287-294
    • Suzuki, Y.1
  • 23
    • 0025884056 scopus 로고
    • Efficient selection for highexpression transfectants with a novel eukaryotic vector
    • Niwa H, Yamamura K, Miyazaki J. 1991. Efficient selection for highexpression transfectants with a novel eukaryotic vector. Gene 108:193- 199. http://dx.doi.org/10.1016/0378-1119(91)90434-D.
    • (1991) Gene , vol.108
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 24
    • 33646867165 scopus 로고    scopus 로고
    • The production of cleaved, trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein vaccine antigens and infectious pseudoviruses using linear polyethylenimine as a transfection reagent
    • Kirschner M, Monrose V, Paluch M, Techodamrongsin N, Rethwilm A, Moore JP. 2006. The production of cleaved, trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein vaccine antigens and infectious pseudoviruses using linear polyethylenimine as a transfection reagent. Protein Expr. Purif. 48:61-68. http://dx.doi.org/10.1016/j.pep .2006.02.017.
    • (2006) Protein Expr. Purif. , vol.48 , pp. 61-68
    • Kirschner, M.1    Monrose, V.2    Paluch, M.3    Techodamrongsin, N.4    Rethwilm, A.5    Moore, J.P.6
  • 28
    • 84880617786 scopus 로고    scopus 로고
    • In vivo bioluminescent imaging of influenza a virus infection and characterization of novel cross-protective monoclonal antibodies
    • Heaton NS, Leyva-Grado VH, Tan GS, Eggink D, Hai R, Palese P. 2013. In vivo bioluminescent imaging of influenza a virus infection and characterization of novel cross-protective monoclonal antibodies. J. Virol. 87: 8272-8281. http://dx.doi.org/10.1128/JVI.00969-13.
    • (2013) J. Virol. , vol.87 , pp. 8272-8281
    • Heaton, N.S.1    Leyva-Grado, V.H.2    Tan, G.S.3    Eggink, D.4    Hai, R.5    Palese, P.6
  • 30
    • 84865289490 scopus 로고    scopus 로고
    • A carboxy-terminal trimerization domain stabilizes conformational epitopes on the stalk domain of soluble recombinant hemagglutinin substrates
    • Krammer F, Margine I, Tan GS, Pica N, Krause JC, Palese P. 2012. A carboxy-terminal trimerization domain stabilizes conformational epitopes on the stalk domain of soluble recombinant hemagglutinin substrates. PLoS One 7:e43603. http://dx.doi.org/10.1371/journal.pone .0043603.
    • (2012) PLoS One , vol.7
    • Krammer, F.1    Margine, I.2    Tan, G.S.3    Pica, N.4    Krause, J.C.5    Palese, P.6
  • 31
    • 84880284754 scopus 로고    scopus 로고
    • Induction of cross-reactive antibodies to novel H7N9 influenza virus by recombinant Newcastle disease virus expressing a North American lineage H7 subtype hemagglutinin
    • Goff PH, Krammer F, Hai R, Seibert CW, Margine I, Garcia-Sastre A, Palese P. 2013. Induction of cross-reactive antibodies to novel H7N9 influenza virus by recombinant Newcastle disease virus expressing a North American lineage H7 subtype hemagglutinin. J. Virol. 87:8235- 8240. http://dx.doi.org/10.1128/JVI.01085-13.
    • (2013) J. Virol. , vol.87
    • Goff, P.H.1    Krammer, F.2    Hai, R.3    Seibert, C.W.4    Margine, I.5    Garcia-Sastre, A.6    Palese, P.7
  • 32
    • 84861325359 scopus 로고    scopus 로고
    • Influenza viruses expressing chimeric hemagglutinins: globular head and stalk domains derived from different subtypes
    • Hai R, Krammer F, Tan GS, Pica N, Eggink D, Maamary J, Margine I, Albrecht RA, Palese P. 2012. Influenza viruses expressing chimeric hemagglutinins: globular head and stalk domains derived from different subtypes. J. Virol. 86:5774-5781. http://dx.doi.org/10.1128/JVI.00137-12.
    • (2012) J. Virol. , vol.86 , pp. 5774-5781
    • Hai, R.1    Krammer, F.2    Tan, G.S.3    Pica, N.4    Eggink, D.5    Maamary, J.6    Margine, I.7    Albrecht, R.A.8    Palese, P.9
  • 34
    • 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
  • 36
    • 84862908804 scopus 로고    scopus 로고
    • Complement-dependent lysis of influenza a virusinfected cells by broadly cross-reactive human monoclonal antibodies
    • Terajima M, Cruz J, Co MD, Lee JH, Kaur K, Wrammert J, Wilson PC, Ennis FA. 2011. Complement-dependent lysis of influenza a virusinfected cells by broadly cross-reactive human monoclonal antibodies. J. Virol. 85:13463-13467. http://dx.doi.org/10.1128/JVI.05193-11.
    • (2011) J. Virol. , vol.85 , pp. 13463-13467
    • Terajima, M.1    Cruz, J.2    Co, M.D.3    Lee, J.H.4    Kaur, K.5    Wrammert, J.6    Wilson, P.C.7    Ennis, F.A.8
  • 37
    • 23144441143 scopus 로고    scopus 로고
    • GlyProt: in silico glycosylation of proteins
    • Bohne-Lang A, von der Lieth CW. 2005. GlyProt: in silico glycosylation of proteins. Nucleic Acids Res. 33:W214-W219. http://dx.doi.org/10 .1093/nar/gki385.
    • (2005) Nucleic Acids Res. , vol.33
    • Bohne-Lang, A.1    von der Lieth, C.W.2
  • 38
    • 0027513851 scopus 로고
    • Induction of antihemagglutinin antibodies by polyclonal antiidiotype antibodies
    • Dinca L, Neuwirth S, Schulman J, Bona C. 1993. Induction of antihemagglutinin antibodies by polyclonal antiidiotype antibodies. Viral Immunol. 6:75-84. http://dx.doi.org/10.1089/vim.1993.6.75.
    • (1993) Viral Immunol. , vol.6 , pp. 75-84
    • Dinca, L.1    Neuwirth, S.2    Schulman, J.3    Bona, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.