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Volumn 5, Issue 187, 2013, Pages

Glycosylations in the globular head of the hemagglutinin protein modulate the virulence and antigenic properties of the H1N1 influenza viruses

Author keywords

[No Author keywords available]

Indexed keywords

HEMAGGLUTININ; POLYCLONAL ANTIBODY;

EID: 84880558705     PISSN: 19466234     EISSN: 19466242     Source Type: Journal    
DOI: 10.1126/scitranslmed.3005996     Document Type: Article
Times cited : (107)

References (32)
  • 2
    • 79960384534 scopus 로고    scopus 로고
    • Influenza A viruses: New research developments
    • R. A. Medina, A. García-Sastre, Influenza A viruses: New research developments. Nat. Rev. Microbiol. 9, 590-603 (2011).
    • (2011) Nat. Rev. Microbiol , vol.9 , pp. 590-603
    • Medina, R.A.1    García-Sastre, A.2
  • 8
    • 77951165843 scopus 로고    scopus 로고
    • Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus
    • R. Xu, D. C. Ekiert, J. C. Krause, R. Hai, J. E. Crowe Jr., I. A. Wilson, 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    Ekiert, D.C.2    Krause, J.C.3    Hai, R.4    Crowe Jr., J.E.5    Wilson, I.A.6
  • 9
    • 79251480393 scopus 로고    scopus 로고
    • Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain
    • S. R. Das, P. Puigbò, S. E. Hensley, D. E. Hurt, J. R. Bennink, J. W. Yewdell, Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain. PLoS Pathog. 6, e1001211 (2010).
    • (2010) PLoS Pathog , vol.6
    • Das, S.R.1    Puigbò, P.2    Hensley, S.E.3    Hurt, D.E.4    Bennink, J.R.5    Yewdell, J.W.6
  • 10
    • 79960872741 scopus 로고    scopus 로고
    • Glycosylation site alteration in the evolution of influenza A (H1N1) viruses
    • S. Sun, Q. Wang, F. Zhao, W. Chen, Z. Li, Glycosylation site alteration in the evolution of influenza A (H1N1) viruses. PLoS One 6, e22844 (2011).
    • (2011) PLoS One , vol.6
    • Sun, S.1    Wang, Q.2    Zhao, F.3    Chen, W.4    Li, Z.5
  • 11
    • 44649136618 scopus 로고    scopus 로고
    • Genetically destined potentials for N-linked glycosylation of influenza virus hemagglutinin
    • M. Igarashi, K. Ito, H. Kida, A. Takada, Genetically destined potentials for N-linked glycosylation of influenza virus hemagglutinin. Virology 376, 323-329 (2008).
    • (2008) Virology , vol.376 , pp. 323-329
    • Igarashi, M.1    Ito, K.2    Kida, H.3    Takada, A.4
  • 13
    • 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
    • M. D. Tate, A. G. Brooks, P. C. Reading, 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 (2011).
    • (2011) J. Immunol , vol.187 , pp. 1884-1894
    • Tate, M.D.1    Brooks, A.G.2    Reading, P.C.3
  • 14
    • 79953117247 scopus 로고    scopus 로고
    • Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 influenza viruses to innate proteins in airway secretions and virulence in mice
    • M. D. Tate, E. R. Job, A. G. Brooks, P. C. Reading, Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 influenza viruses to innate proteins in airway secretions and virulence in mice. Virology 413, 84-92 (2011).
    • (2011) Virology , vol.413 , pp. 84-92
    • Tate, M.D.1    Job, E.R.2    Brooks, A.G.3    Reading, P.C.4
  • 16
    • 77149123171 scopus 로고    scopus 로고
    • Does glycosylation as a modifier of original antigenic sin explain the case age distribution and unusual toxicity in pandemic novel H1N1 influenza?
    • T. Reichert, G. Chowell, H. Nishiura, R. A. Christensen, J. A. McCullers, Does glycosylation as a modifier of original antigenic sin explain the case age distribution and unusual toxicity in pandemic novel H1N1 influenza? BMC Infect. Dis. 10, 5 (2010).
    • (2010) BMC Infect. Dis , vol.10 , pp. 5
    • Reichert, T.1    Chowell, G.2    Nishiura, H.3    Christensen, R.A.4    McCullers, J.A.5
  • 17
    • 77649176948 scopus 로고    scopus 로고
    • Predicting the antigenic structure of the pandemic (H1N1) 2009 influenza virus hemagglutinin
    • M. Igarashi, K. Ito, R. Yoshida, D. Tomabechi, H. Kida, A. Takada, Predicting the antigenic structure of the pandemic (H1N1) 2009 influenza virus hemagglutinin. PLoS One 5, e8553 (2010).
    • (2010) PLoS One , vol.5
    • Igarashi, M.1    Ito, K.2    Yoshida, R.3    Tomabechi, D.4    Kida, H.5    Takada, A.6
  • 22
    • 84867216481 scopus 로고    scopus 로고
    • The number and position of N-linked glycosylation sites in the hemagglutinin determine differential recognition of seasonal and 2009 pandemic H1N1 influenza virus by porcine surfactant protein D
    • M. L. Hillaire, M. van Eijk, N. J. Nieuwkoop, S. E. Vogelzang-van Trierum, R. A. Fouchier, A. D. Osterhaus, H. P. Haagsman, G. F. Rimmelzwaan, The number and position of N-linked glycosylation sites in the hemagglutinin determine differential recognition of seasonal and 2009 pandemic H1N1 influenza virus by porcine surfactant protein D. Virus Res. 169, 301-305 (2012).
    • (2012) Virus Res , vol.169 , pp. 301-305
    • Hillaire, M.L.1    Van Eijk, M.2    Nieuwkoop, N.J.3    Vogelzang-Van Trierum, S.E.4    Fouchier, R.A.5    Osterhaus, A.D.6    Haagsman, H.P.7    Rimmelzwaan, G.F.8
  • 23
    • 84874270957 scopus 로고    scopus 로고
    • Addition of glycosylation to influenza A virus hemagglutinin modulates antibodymediated recognition of H1N1 2009 pandemic viruses
    • E. R. Job, Y. M. Deng, K. K. Barfod, M. D. Tate, N. Caldwell, S. Reddiex, S. Maurer-Stroh, A. G. Brooks, P. C. Reading, Addition of glycosylation to influenza A virus hemagglutinin modulates antibodymediated recognition of H1N1 2009 pandemic viruses. J. Immunol. 190, 2169-2177 (2013).
    • (2013) J. Immunol , vol.190 , pp. 2169-2177
    • Job, E.R.1    Deng, Y.M.2    Barfod, K.K.3    Tate, M.D.4    Caldwell, N.5    Reddiex, S.6    Maurer-Stroh, S.7    Brooks, A.G.8    Reading, P.C.9
  • 24
    • 79952162488 scopus 로고    scopus 로고
    • Animal models for influenza virus pathogenesis and transmission
    • N. M. Bouvier, A. C. Lowen, Animal models for influenza virus pathogenesis and transmission. Viruses 2, 1530-1563 (2010).
    • (2010) Viruses , vol.2 , pp. 1530-1563
    • Bouvier, N.M.1    Lowen, A.C.2
  • 25
    • 81255179897 scopus 로고    scopus 로고
    • The DBA.2 mouse is susceptible to disease following infection with a broad, but limited, range of influenza A and B viruses
    • N. Pica, A. Iyer, I. Ramos, N. M. Bouvier, A. Fernandez-Sesma, A. Garcia-Sastre, A. C. Lowen, P. Palese, J. Steel, The DBA.2 mouse is susceptible to disease following infection with a broad, but limited, range of influenza A and B viruses. J. Virol. 85, 12825-12829 (2011).
    • (2011) J. Virol , vol.85 , pp. 12825-12829
    • Pica, N.1    Iyer, A.2    Ramos, I.3    Bouvier, N.M.4    Fernandez-Sesma, A.5    Garcia-Sastre, A.6    Lowen, A.C.7    Palese, P.8    Steel, J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.