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Volumn 169, Issue 1, 2012, Pages 301-305

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

Author keywords

Collectins; Glycosylation; Influenza viruses; SP D

Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ; SURFACTANT PROTEIN D;

EID: 84867216481     PISSN: 01681702     EISSN: 18727492     Source Type: Journal    
DOI: 10.1016/j.virusres.2012.08.003     Document Type: Article
Times cited : (18)

References (32)
  • 1
    • 0028344851 scopus 로고
    • Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin
    • Anders E.M., Hartley C.A., Reading P.C., Ezekowitz R.A. Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin. Journal of General Virology 1994, 75(Pt 3):615-622.
    • (1994) Journal of General Virology , vol.75 , Issue.PART 3 , pp. 615-622
    • Anders, E.M.1    Hartley, C.A.2    Reading, P.C.3    Ezekowitz, R.A.4
  • 3
    • 79251480393 scopus 로고    scopus 로고
    • Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain
    • Das S.R., Puigbo P., Hensley S.E., Hurt D.E., Bennink J.R., Yewdell J.W. Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain. PLoS Pathogens 2010, 6(11):e1001211.
    • (2010) PLoS Pathogens , vol.6 , Issue.11
    • Das, S.R.1    Puigbo, P.2    Hensley, S.E.3    Hurt, D.E.4    Bennink, J.R.5    Yewdell, J.W.6
  • 12
    • 44649136618 scopus 로고    scopus 로고
    • Genetically destined potentials for N-linked glycosylation of influenza virus hemagglutinin
    • Igarashi M., Ito K., Kida H., Takada A. Genetically destined potentials for N-linked glycosylation of influenza virus hemagglutinin. Virology 2008, 376(2):323-329.
    • (2008) Virology , vol.376 , Issue.2 , pp. 323-329
    • Igarashi, M.1    Ito, K.2    Kida, H.3    Takada, A.4
  • 13
    • 77958149678 scopus 로고    scopus 로고
    • Pandemic H1N1 influenza a viruses are resistant to the antiviral activities of innate immune proteins of the collectin and pentraxin superfamilies
    • Job E.R., Deng Y.M., Tate M.D., Bottazzi B., Crouch E.C., Dean M.M., Mantovani A., Brooks A.G., Reading P.C. Pandemic H1N1 influenza a viruses are resistant to the antiviral activities of innate immune proteins of the collectin and pentraxin superfamilies. Journal of Immunology 2010, 185:4284-4291.
    • (2010) Journal of Immunology , vol.185 , pp. 4284-4291
    • Job, E.R.1    Deng, Y.M.2    Tate, M.D.3    Bottazzi, B.4    Crouch, E.C.5    Dean, M.M.6    Mantovani, A.7    Brooks, A.G.8    Reading, P.C.9
  • 15
    • 67649297821 scopus 로고    scopus 로고
    • Emergence and pandemic potential of swine-origin H1N1 influenza virus
    • Neumann G., Noda T., Kawaoka Y. Emergence and pandemic potential of swine-origin H1N1 influenza virus. Nature 2009, 459(7249):931-939.
    • (2009) Nature , vol.459 , Issue.7249 , pp. 931-939
    • Neumann, G.1    Noda, T.2    Kawaoka, Y.3
  • 17
    • 79952621304 scopus 로고    scopus 로고
    • The ability of pandemic influenza virus hemagglutinins to induce lower respiratory pathology is associated with decreased surfactant protein D binding
    • Qi L., Kash J.C., Dugan V.G., Jagger B.W., Lau Y.F., Sheng Z.M., Crouch E.C., Hartshorn K.L., Taubenberger J.K. The ability of pandemic influenza virus hemagglutinins to induce lower respiratory pathology is associated with decreased surfactant protein D binding. Virology 2011, 412(2):426-434.
    • (2011) Virology , vol.412 , Issue.2 , pp. 426-434
    • Qi, L.1    Kash, J.C.2    Dugan, V.G.3    Jagger, B.W.4    Lau, Y.F.5    Sheng, Z.M.6    Crouch, E.C.7    Hartshorn, K.L.8    Taubenberger, J.K.9
  • 18
    • 0030879806 scopus 로고    scopus 로고
    • Collectin-mediated antiviral host defense of the lung: evidence from influenza virus infection of mice
    • Reading P.C., Morey L.S., Crouch E.C., Anders E.M. Collectin-mediated antiviral host defense of the lung: evidence from influenza virus infection of mice. Journal of Virology 1997, 71(11):8204-8212.
    • (1997) Journal of Virology , vol.71 , Issue.11 , pp. 8204-8212
    • Reading, P.C.1    Morey, L.S.2    Crouch, E.C.3    Anders, E.M.4
  • 19
    • 73949084221 scopus 로고    scopus 로고
    • Loss of a single N-linked glycan from the hemagglutinin of influenza virus is associated with resistance to collectins and increased virulence in mice
    • Reading P.C., Pickett D.L., Tate M.D., Whitney P.G., Job E.R., Brooks A.G. Loss of a single N-linked glycan from the hemagglutinin of influenza virus is associated with resistance to collectins and increased virulence in mice. Respiratory Research 2009, 10:117.
    • (2009) Respiratory Research , vol.10 , pp. 117
    • Reading, P.C.1    Pickett, D.L.2    Tate, M.D.3    Whitney, P.G.4    Job, E.R.5    Brooks, A.G.6
  • 21
    • 0031866073 scopus 로고    scopus 로고
    • Comparison of RNA hybridization, hemagglutination assay, titration of infectious virus and immunofluorescence as methods for monitoring influenza virus replication in vitro
    • Rimmelzwaan G.F., Baars M., Claas E.C., Osterhaus A.D. Comparison of RNA hybridization, hemagglutination assay, titration of infectious virus and immunofluorescence as methods for monitoring influenza virus replication in vitro. Journal of Virological Methods 1998, 74(1):57-66.
    • (1998) Journal of Virological Methods , vol.74 , Issue.1 , pp. 57-66
    • Rimmelzwaan, G.F.1    Baars, M.2    Claas, E.C.3    Osterhaus, A.D.4
  • 23
    • 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 M.D., Brooks A.G., Reading P.C. 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. Journal of Immunology 2011, 187(4):1884-1894.
    • (2011) Journal of Immunology , vol.187 , Issue.4 , pp. 1884-1894
    • Tate, M.D.1    Brooks, A.G.2    Reading, P.C.3
  • 24
    • 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
    • Tate M.D., Job E.R., Brooks A.G., Reading P.C. Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 influenza viruses to innate proteins in airway secretions and virulence in mice. Virology 2011, 413(1):84-92.
    • (2011) Virology , vol.413 , Issue.1 , pp. 84-92
    • Tate, M.D.1    Job, E.R.2    Brooks, A.G.3    Reading, P.C.4
  • 26
    • 0042346137 scopus 로고    scopus 로고
    • Porcine pulmonary collectins show distinct interactions with influenza A viruses: role of the N-linked oligosaccharides in the carbohydrate recognition domain
    • van Eijk M., White M.R., Crouch E.C., Batenburg J.J., Vaandrager A.B., Van Golde L.M., Haagsman H.P., Hartshorn K.L. Porcine pulmonary collectins show distinct interactions with influenza A viruses: role of the N-linked oligosaccharides in the carbohydrate recognition domain. Journal of Immunology 2003, 171(3):1431-1440.
    • (2003) Journal of Immunology , vol.171 , Issue.3 , pp. 1431-1440
    • van Eijk, M.1    White, M.R.2    Crouch, E.C.3    Batenburg, J.J.4    Vaandrager, A.B.5    Van Golde, L.M.6    Haagsman, H.P.7    Hartshorn, K.L.8
  • 28
    • 80053613561 scopus 로고    scopus 로고
    • The carbohydrate recognition domain of collectins
    • Veldhuizen E.J., van Eijk M., Haagsman H.P. The carbohydrate recognition domain of collectins. FEBS Journal 2011, 278(20):3930-3941.
    • (2011) FEBS Journal , vol.278 , Issue.20 , pp. 3930-3941
    • Veldhuizen, E.J.1    van Eijk, M.2    Haagsman, H.P.3
  • 30
    • 84867209685 scopus 로고    scopus 로고
    • WHO
    • Pandemic (H1N1) 2009-update 112
    • WHO, 2009. Pandemic (H1N1) 2009-update 112.
    • (2009)
  • 32
    • 9744280420 scopus 로고    scopus 로고
    • Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin
    • Zhang M., Gaschen B., Blay W., Foley B., Haigwood N., Kuiken C., Korber B. Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin. Glycobiology 2004, 14(12):1229-1246.
    • (2004) Glycobiology , vol.14 , Issue.12 , pp. 1229-1246
    • Zhang, M.1    Gaschen, B.2    Blay, W.3    Foley, B.4    Haigwood, N.5    Kuiken, C.6    Korber, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.