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Volumn 74, Issue 13, 2000, Pages 6015-6020

Balanced hemagglutinin and neuraminidase activities are critical for efficient replication of influenza A virus

Author keywords

[No Author keywords available]

Indexed keywords

HEMAGGLUTININ; RECOMBINANT RNA; SIALIDASE;

EID: 0034099655     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.74.13.6015-6020.2000     Document Type: Article
Times cited : (329)

References (30)
  • 2
    • 0026464671 scopus 로고
    • Transfection-mediated recombination of influenza A virus
    • Bergmann, M., A. Garcia-Sastre, and P. Palese. 1992. Transfection-mediated recombination of influenza A virus. J. Virol. 66:7576-7580.
    • (1992) J. Virol. , vol.66 , pp. 7576-7580
    • Bergmann, M.1    Garcia-Sastre, A.2    Palese, P.3
  • 3
    • 0032551234 scopus 로고    scopus 로고
    • The interaction of neuraminidase and hemagglutinin mutations in influenza virus resistance to 4-guanidino-Neu5Ac2en
    • Blick, T. J., A. Sahasrabudhe, M. McDonald, I. J. Owens, P. J. Morley, K. J. Fenton, and J. L. McKimm-Breschkin. 1998. The interaction of neuraminidase and hemagglutinin mutations in influenza virus resistance to 4-guanidino-Neu5Ac2en. Virology 246:95-103.
    • (1998) Virology , vol.246 , pp. 95-103
    • Blick, T.J.1    Sahasrabudhe, A.2    McDonald, M.3    Owens, I.J.4    Morley, P.J.5    Fenton, K.J.6    McKimm-Breschkin, J.L.7
  • 5
    • 0026632415 scopus 로고
    • Attenuation of influenza A virus by insertion of a foreign epitope into the neuraminidase
    • Castrucci, M. R., P. Bilsel, and Y. Kawaoka. 1992. Attenuation of influenza A virus by insertion of a foreign epitope into the neuraminidase. J. Virol. 66:4647-4653.
    • (1992) J. Virol. , vol.66 , pp. 4647-4653
    • Castrucci, M.R.1    Bilsel, P.2    Kawaoka, Y.3
  • 6
    • 0027397591 scopus 로고
    • Biologic importance of neuraminidase stalk length in influenza A virus
    • Castrucci, M. R., and Y. Kawaoka. 1993. Biologic importance of neuraminidase stalk length in influenza A virus. J. Virol. 67:759-764.
    • (1993) J. Virol. , vol.67 , pp. 759-764
    • Castrucci, M.R.1    Kawaoka, Y.2
  • 8
    • 0021739837 scopus 로고
    • Biological properties of a hemagglutinin mutant of influenza virus selected by host cells
    • Crecelius, D. M., C. M. Deom, and I. T. Schulze. 1984. Biological properties of a hemagglutinin mutant of influenza virus selected by host cells. Virology 139:164-177.
    • (1984) Virology , vol.139 , pp. 164-177
    • Crecelius, D.M.1    Deom, C.M.2    Schulze, I.T.3
  • 9
    • 0026698245 scopus 로고
    • A solid-phase enzyme-linked assay for influenza virus receptor-binding activity
    • Gambaryan, A. S., and M. N. Matrosovich. 1992. A solid-phase enzyme-linked assay for influenza virus receptor-binding activity. J. Virol. Methods 39:111-123.
    • (1992) J. Virol. Methods , vol.39 , pp. 111-123
    • Gambaryan, A.S.1    Matrosovich, M.N.2
  • 10
    • 0030028671 scopus 로고    scopus 로고
    • Characterization of mutants of influenza A virus selected with the neuraminidase inhibitor 4-guanidino-Neu5Ac2en
    • Gubareva, L. V., R. C. Bethell, G. J. Hart, K. G. Murti, and R. G. Webster. 1996. Characterization of mutants of influenza A virus selected with the neuraminidase inhibitor 4-guanidino-Neu5Ac2en. J. Virol. 70:1818-1827.
    • (1996) J. Virol. , vol.70 , pp. 1818-1827
    • Gubareva, L.V.1    Bethell, R.C.2    Hart, G.J.3    Murti, K.G.4    Webster, R.G.5
  • 11
    • 0026742195 scopus 로고
    • Proton nuclear magnetic resonance studies of the binding of sialosides to intact influenza virus
    • Hanson, J. E., N. K. Sauter, J. J. Skehel, and D. C. Wiley. 1992. Proton nuclear magnetic resonance studies of the binding of sialosides to intact influenza virus. Virology 189:525-533.
    • (1992) Virology , vol.189 , pp. 525-533
    • Hanson, J.E.1    Sauter, N.K.2    Skehel, J.J.3    Wiley, D.C.4
  • 12
    • 0024347652 scopus 로고
    • Increased viral pathogenicity after insertion of a 28S ribosomal RNA sequence into the haemagglutinin gene of an influenza virus
    • Khatchikian, D., M. Orlich, and R. Rott. 1989. Increased viral pathogenicity after insertion of a 28S ribosomal RNA sequence into the haemagglutinin gene of an influenza virus. Nature (London) 340:156-157.
    • (1989) Nature (London) , vol.340 , pp. 156-157
    • Khatchikian, D.1    Orlich, M.2    Rott, R.3
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0003090424 scopus 로고
    • The influenza virus RNA segments and their encoded proteins
    • P. Palese and D. W. Kingsbury (ed.). Springer-Verlag, Vienna, Austria
    • Lamb, R. 1983. The influenza virus RNA segments and their encoded proteins, p. 26-69. In P. Palese and D. W. Kingsbury (ed.). Genetics of influenza viruses. Springer-Verlag, Vienna, Austria.
    • (1983) Genetics of Influenza Viruses , pp. 26-69
    • Lamb, R.1
  • 15
    • 0020696905 scopus 로고
    • The gene structure and replication of influenza virus
    • Lamb, R. A., and P. W. Choppin. 1983. The gene structure and replication of influenza virus. Annu. Rev. Biochem. 52:467-506.
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 467-506
    • Lamb, R.A.1    Choppin, P.W.2
  • 16
    • 0001178028 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.) Lippincott-Raven Publishers, Philadelphia, Pa.
    • Lamb, R. A., and R. M. Krug. 1996. Orthomyxoviridae: the viruses and their replication, p. 1353-1445. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 1353-1445
    • Lamb, R.A.1    Krug, R.M.2
  • 17
    • 0028813628 scopus 로고
    • Influenza type A virus neuraminidase does not play a role in virus entry, replication, assembly, or budding
    • Liu, C., M. C. Eichelberger, R. W. Compans, and G. M. Air. 1995. Influenza type A virus neuraminidase does not play a role in virus entry, replication, assembly, or budding. J. Virol. 69:1099-1106.
    • (1995) J. Virol. , vol.69 , pp. 1099-1106
    • Liu, C.1    Eichelberger, M.C.2    Compans, R.W.3    Air, G.M.4
  • 18
    • 0027236107 scopus 로고
    • Alterations of the stalk of the influenza virus neuraminidase: Deletions and insertions
    • Luo, G., J. Chung, and P. Palese. 1993. Alterations of the stalk of the influenza virus neuraminidase: deletions and insertions. Virus Res. 29:141-153.
    • (1993) Virus Res. , vol.29 , pp. 141-153
    • Luo, G.1    Chung, J.2    Palese, P.3
  • 20
    • 0031911783 scopus 로고    scopus 로고
    • Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors
    • McKimm-Breschkin, J. L., A. Sahasrabudhe, T. J. Blick, M. McDonlad, P. M. Colman, J. H. Grahm, R. C. Bethell, and J. N. Varghese. 1998. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J. Virol. 72:2456-2462.
    • (1998) J. Virol. , vol.72 , pp. 2456-2462
    • McKimm-Breschkin, J.L.1    Sahasrabudhe, A.2    Blick, T.J.3    McDonlad, M.4    Colman, P.M.5    Grahm, J.H.6    Bethell, R.C.7    Varghese, J.N.8
  • 21
    • 0030069140 scopus 로고    scopus 로고
    • The cytoplasmic tail of influenza neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication
    • Mitnaul, L., M. R. Castrucci, K. G. Murti, and Y. Kawaoka. 1996. The cytoplasmic tail of influenza neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication. J. Virol. 70:873-879.
    • (1996) J. Virol. , vol.70 , pp. 873-879
    • Mitnaul, L.1    Castrucci, M.R.2    Murti, K.G.3    Kawaoka, Y.4
  • 22
    • 0026175939 scopus 로고
    • Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses
    • Nobusawa, E., T. Aoyama, H. Kato, Y. Suzuki, Y. Tateno, and K. Nakajima. 1991. Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses. Virology 182:475-485.
    • (1991) Virology , vol.182 , pp. 475-485
    • Nobusawa, E.1    Aoyama, T.2    Kato, H.3    Suzuki, Y.4    Tateno, Y.5    Nakajima, K.6
  • 23
    • 0028828081 scopus 로고
    • Neuraminidase is essential for fowl plague virus hemagglutinin to show hemagglutinating activity
    • Ohuchi, M., A. Feldmann, R. Ohuchi, and H. D. Klenk. 1995. Neuraminidase is essential for fowl plague virus hemagglutinin to show hemagglutinating activity. Virology 212:77-83.
    • (1995) Virology , vol.212 , pp. 77-83
    • Ohuchi, M.1    Feldmann, A.2    Ohuchi, R.3    Klenk, H.D.4
  • 24
    • 0028086229 scopus 로고
    • Nonhomologous recombination between the hemagglutinin gene and the nucleoprotein gene of an influenza virus
    • Orlich, M., H. Gottwald, and R. Rott. 1994. Nonhomologous recombination between the hemagglutinin gene and the nucleoprotein gene of an influenza virus. Virology 204:462-465.
    • (1994) Virology , vol.204 , pp. 462-465
    • Orlich, M.1    Gottwald, H.2    Rott, R.3
  • 25
    • 0016272701 scopus 로고
    • Characterization of temperature sensitive influenza virus mutants defective in neuraminidase
    • Palese, P., K. Tobita, M. Ueda, and R. W. Compans. 1974. Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61:397-410.
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Tobita, K.2    Ueda, M.3    Compans, R.W.4
  • 26
    • 0027346651 scopus 로고
    • Analysis of influenza A virus nucleoproteins for the assessment of molecular genetic mechanisms leading to new phylogenetic virus lineages
    • Scholtissek, C., S. Ludwig, and W. M. Fitch. 1993. Analysis of influenza A virus nucleoproteins for the assessment of molecular genetic mechanisms leading to new phylogenetic virus lineages. Arch. Virol. 131:237-250.
    • (1993) Arch. Virol. , vol.131 , pp. 237-250
    • Scholtissek, C.1    Ludwig, S.2    Fitch, W.M.3
  • 27
    • 0026561520 scopus 로고
    • Heterogeneity of the mutation rates of influenza A viruses: Isolation of mutator mutants
    • Suárez, P., J. Valcárcel, and J. Ortín. 1992. Heterogeneity of the mutation rates of influenza A viruses: isolation of mutator mutants. J. Virol. 66:2491-2494.
    • (1992) J. Virol. , vol.66 , pp. 2491-2494
    • Suárez, P.1    Valcárcel, J.2    Ortín, J.3
  • 28
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9Å resolution
    • Varghese, J. N., W. G. Laver, and P. M. Colman. 1983. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9Å resolution. Nature 303:35-40.
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 30
    • 0023915219 scopus 로고
    • Structure of the influenza virus hemagglutinin complexed with its receptor, sialic acid
    • Weis, W., J. H. Brown, S. Cusack, J. C. Paulson, J. J. Skehel, and D. C. Wiley. 1988. Structure of the influenza virus hemagglutinin complexed with its receptor, sialic acid. Nature 333:426-431.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6


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