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Volumn 4, Issue 7, 2013, Pages 502-511

Structure and receptor-binding properties of an airborne transmissible avian influenza A virus hemagglutinin H5 (VN1203mut)

Author keywords

airborne; avian influenza; H5; receptor binding; structure; transmission

Indexed keywords

HEMAGGLUTININ H5 PROTEIN; INFLUENZA VIRUS HEMAGGLUTININ; MUTANT PROTEIN; UNCLASSIFIED DRUG;

EID: 84880834962     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-013-3906-z     Document Type: Article
Times cited : (35)

References (32)
  • 1
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, N
    • Collaborative Computational Project, N. (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50, 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 2
    • 0030917883 scopus 로고    scopus 로고
    • Binding of the influenza A virus to cell-surface receptors: Structures of five hemagglutinin-sialyloligosaccharide complexes determined by x-ray crystallography
    • Eisen, M. B., Sabesan, S., Skehel, J. J., and Wiley, D. C. (1997). Binding of the influenza A virus to cell-surface receptors: Structures of five hemagglutinin-sialyloligosaccharide complexes determined by x-ray crystallography. Virology 232, 19-31.
    • (1997) Virology , vol.232 , pp. 19-31
    • Eisen, M.B.1    Sabesan, S.2    Skehel, J.J.3    Wiley, D.C.4
  • 3
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004). Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60, 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 5
    • 0035949581 scopus 로고    scopus 로고
    • X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs
    • Ha, Y., Stevens, D. J., Skehel, J. J., and Wiley, D. C. (2001). X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proc Natl Acad Sci U S A 98, 11181-11186.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11181-11186
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 6
    • 0035823083 scopus 로고    scopus 로고
    • Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses
    • Hatta, M., Gao, P., Halfmann, P., and Kawaoka, Y. (2001). Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses. Science 293, 1840-1842.
    • (2001) Science , vol.293 , pp. 1840-1842
    • Hatta, M.1    Gao, P.2    Halfmann, P.3    Kawaoka, Y.4
  • 8
    • 84861394598 scopus 로고    scopus 로고
    • Experimental adaptation of an influenza H5 HA confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets
    • Imai, M., Watanabe, T., Hatta, M., Das, S. C., Ozawa, M., Shinya, K., Zhong, G., Hanson, A., Katsura, H., Watanabe, S., et al. (2012). Experimental adaptation of an influenza H5 HA confers respiratory droplet transmission to a reassortant H5 HA/H1N1 virus in ferrets. Nature 486, 420-428.
    • (2012) Nature , vol.486 , pp. 420-428
    • Imai, M.1    Watanabe, T.2    Hatta, M.3    Das, S.C.4    Ozawa, M.5    Shinya, K.6    Zhong, G.7    Hanson, A.8    Katsura, H.9    Watanabe, S.10
  • 9
    • 84869210338 scopus 로고    scopus 로고
    • Insights into avian influenza virus pathogenicity: the hemagglutinin precursor HA0 of subtype H16 has an alpha-helix structure in Its cleavage site with inefficient HA1/HA2 cleavage
    • Lu, X., Shi, Y., Gao, F., Xiao, H., Wang, M., Qi, J., and Gao, G. F. (2012). Insights into avian influenza virus pathogenicity: the hemagglutinin precursor HA0 of subtype H16 has an alpha-helix structure in Its cleavage site with inefficient HA1/HA2 cleavage. J Virol 86, 12861-12870.
    • (2012) J Virol , vol.86 , pp. 12861-12870
    • Lu, X.1    Shi, Y.2    Gao, F.3    Xiao, H.4    Wang, M.5    Qi, J.6    Gao, G.F.7
  • 10
    • 79960384534 scopus 로고    scopus 로고
    • Influenza A viruses: new research developments
    • Medina, R. A., and Garcia-Sastre, A. (2011). Influenza A viruses: new research developments. Nat Rev Microbiol 9, 590-603.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 590-603
    • Medina, R.A.1    Garcia-Sastre, A.2
  • 12
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53, 240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 14
    • 67649297821 scopus 로고    scopus 로고
    • Emergence and pandemic potential of swine-origin H1N1 influenza virus
    • Neumann, G., Noda, T., and Kawaoka, Y. (2009). Emergence and pandemic potential of swine-origin H1N1 influenza virus. Nature 459, 931-939.
    • (2009) Nature , vol.459 , pp. 931-939
    • Neumann, G.1    Noda, T.2    Kawaoka, Y.3
  • 15
    • 34248170234 scopus 로고    scopus 로고
    • Avian influenza virus (H5N1): a threat to human health
    • Peiris, J. S., de Jong, M. D., and Guan, Y. (2007). Avian influenza virus (H5N1): a threat to human health. Clin Microbiol Rev 20, 243-267.
    • (2007) Clin Microbiol Rev , vol.20 , pp. 243-267
    • Peiris, J.S.1    de Jong, M.D.2    Guan, Y.3
  • 17
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R. J. (2001). Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr D Biol Crystallogr 57, 1373-1382.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 18
    • 0021040861 scopus 로고
    • Differential sensitivity of human, avian, and equine influenza A viruses to a glycoprotein inhibitor of infection: selection of receptor specific variants
    • Rogers, G. N., Pritchett, T. J., Lane, J. L., and Paulson, J. C. (1983). Differential sensitivity of human, avian, and equine influenza A viruses to a glycoprotein inhibitor of infection: selection of receptor specific variants. Virology 131, 394-408.
    • (1983) Virology , vol.131 , pp. 394-408
    • Rogers, G.N.1    Pritchett, T.J.2    Lane, J.L.3    Paulson, J.C.4
  • 19
    • 33645981586 scopus 로고    scopus 로고
    • Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus
    • Stevens, J., Blixt, O., Tumpey, T. M., Taubenberger, J. K., Paulson, J. C., and Wilson, I. A. (2006). Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science 312, 404-410.
    • (2006) Science , vol.312 , pp. 404-410
    • Stevens, J.1    Blixt, O.2    Tumpey, T.M.3    Taubenberger, J.K.4    Paulson, J.C.5    Wilson, I.A.6
  • 20
    • 1642352884 scopus 로고    scopus 로고
    • Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus
    • Stevens, J., Corper, A. L., Basler, C. F., Taubenberger, J. K., Palese, P., and Wilson, I. A. (2004). Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus. Science 303, 1866-1870.
    • (2004) Science , vol.303 , pp. 1866-1870
    • Stevens, J.1    Corper, A.L.2    Basler, C.F.3    Taubenberger, J.K.4    Palese, P.5    Wilson, I.A.6
  • 21
    • 84875807120 scopus 로고    scopus 로고
    • Bat-derived influenza hemagglutinin h17 does not bind canonical avian or human receptors and most likely uses a unique entry mechanism
    • Sun, X., Shi, Y., Lu, X., He, J., Gao, F., Yan, J., Qi, J., and Gao, G. F. (2013). Bat-derived influenza hemagglutinin h17 does not bind canonical avian or human receptors and most likely uses a unique entry mechanism. Cell Rep 3, 769-778.
    • (2013) Cell Rep , vol.3 , pp. 769-778
    • Sun, X.1    Shi, Y.2    Lu, X.3    He, J.4    Gao, F.5    Yan, J.6    Qi, J.7    Gao, G.F.8
  • 24
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J., and Wodak, S. J. (1999). SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr D Biol Crystallogr 55, 191-205.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 25
    • 2542461354 scopus 로고    scopus 로고
    • Functional and structural characteristics of NY-ESO-1-related HLA A2-restricted epitopes and the design of a novel immunogenic analogue
    • Webb, A. I., Dunstone, M. A., Chen, W., Aguilar, M. I., Chen, Q., Jackson, H., Chang, L., Kjer-Nielsen, L., Beddoe, T., McCluskey, J., et al. (2004). Functional and structural characteristics of NY-ESO-1-related HLA A2-restricted epitopes and the design of a novel immunogenic analogue. J Biol Chem 279, 23438-23446.
    • (2004) J Biol Chem , vol.279 , pp. 23438-23446
    • Webb, A.I.1    Dunstone, M.A.2    Chen, W.3    Aguilar, M.I.4    Chen, Q.5    Jackson, H.6    Chang, L.7    Kjer-Nielsen, L.8    Beddoe, T.9    McCluskey, J.10
  • 29
    • 80655143480 scopus 로고    scopus 로고
    • Crystal structure of swine major histo compatibility complex class I SLA-1 0401 and identification of 2009 pandemic swine-origin influenza A H1N1 virus cytotoxic T lymphocyte epitope peptides
    • Zhang, N., Qi, J., Feng, S., Gao, F., Liu, J., Pan, X., Chen, R., Li, Q., Chen, Z., Li, X., et al. (2011). Crystal structure of swine major histo compatibility complex class I SLA-1 0401 and identification of 2009 pandemic swine-origin influenza A H1N1 virus cytotoxic T lymphocyte epitope peptides. J Virol 85, 11709-11724.
    • (2011) J Virol , vol.85 , pp. 11709-11724
    • Zhang, N.1    Qi, J.2    Feng, S.3    Gao, F.4    Liu, J.5    Pan, X.6    Chen, R.7    Li, Q.8    Chen, Z.9    Li, X.10
  • 30
    • 77957816428 scopus 로고    scopus 로고
    • Crystal structure of the swineorigin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus
    • Zhang, W., Qi, J., Shi, Y., Li, Q., Gao, F., Sun, Y., Lu, X., Lu, Q., Vavricka, C. J., Liu, D., et al. (2010). Crystal structure of the swineorigin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus. Protein Cell 1, 459-467.
    • (2010) Protein Cell , vol.1 , pp. 459-467
    • Zhang, W.1    Qi, J.2    Shi, Y.3    Li, Q.4    Gao, F.5    Sun, Y.6    Lu, X.7    Lu, Q.8    Vavricka, C.J.9    Liu, D.10
  • 31
    • 84879263424 scopus 로고    scopus 로고
    • An Airborne Transmissible Avian Influenza H5 Hemagglutinin Seen at the Atomic Level
    • Zhang, W., Shi, Y., Lu, X., Shu, Y., Qi, J., and Gao, G. F. (2013). An Airborne Transmissible Avian Influenza H5 Hemagglutinin Seen at the Atomic Level. Science. (In Press).
    • (2013) Science
    • Zhang, W.1    Shi, Y.2    Lu, X.3    Shu, Y.4    Qi, J.5    Gao, G.F.6
  • 32
    • 84872831242 scopus 로고    scopus 로고
    • Hemagglutinin homologue from H17N10 bat influenza virus exhibits divergent receptor-binding and pH-dependent fusion activities
    • Zhu, X., Yu, W., McBride, R., Li, Y., Chen, L. M., Donis, R. O., Tong, S., Paulson, J. C., and Wilson, I. A. (2013). Hemagglutinin homologue from H17N10 bat influenza virus exhibits divergent receptor-binding and pH-dependent fusion activities. Proc Natl Acad Sci U S A 110, 1458-1463.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 1458-1463
    • Zhu, X.1    Yu, W.2    McBride, R.3    Li, Y.4    Chen, L.M.5    Donis, R.O.6    Tong, S.7    Paulson, J.C.8    Wilson, I.A.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.