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Volumn 79, Issue 18, 2005, Pages 11705-11715

Sialidase activity of influenza A virus in an endocytic pathway enhances viral replication

Author keywords

[No Author keywords available]

Indexed keywords

5 BROMO 4 CHLOROINDOL 3 YL ALPHA N ACETYLNEURAMINIC ACID; NEURAMINIC ACID DERIVATIVE; SIALIDASE; UNCLASSIFIED DRUG; ZANAMIVIR;

EID: 24644489051     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.18.11705-11715.2005     Document Type: Article
Times cited : (76)

References (34)
  • 1
    • 0032374044 scopus 로고    scopus 로고
    • Molecular aspects of the endocytic pathway
    • Clague, M. J. 1998. Molecular aspects of the endocytic pathway. Biochem. J. 336:271-282.
    • (1998) Biochem. J. , vol.336 , pp. 271-282
    • Clague, M.J.1
  • 3
    • 0032544055 scopus 로고    scopus 로고
    • A novel mechanism for the acquisition of virulence by a human influenza A virus
    • Goto, H., and Y. Kawaoka. 1998. A novel mechanism for the acquisition of virulence by a human influenza A virus. Proc. Natl. Acad. Sci. USA 95:10224-10228.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10224-10228
    • Goto, H.1    Kawaoka, Y.2
  • 4
    • 0035823083 scopus 로고    scopus 로고
    • Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses
    • Hatta, M., P. Gao, P. Halfmann, and Y. Kawaoka. 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
  • 5
    • 0032513021 scopus 로고
    • Influenza virus M2 protein slows traffic along the secretory pathway. pH perturbation of acidified compartments affects early Golgi transport steps
    • Henkel, J. R., and O. A. Weisz. 1988. Influenza virus M2 protein slows traffic along the secretory pathway. pH perturbation of acidified compartments affects early Golgi transport steps. J. Biol. Chem. 273:6518-6524.
    • (1988) J. Biol. Chem. , vol.273 , pp. 6518-6524
    • Henkel, J.R.1    Weisz, O.A.2
  • 6
    • 0020546479 scopus 로고
    • Altered tissue tropism of human-avian reassortant influenza viruses
    • Hinshaw, V. S., R. G. Webster, C. W. Naeve, and B. R. Murphy. 1983. Altered tissue tropism of human-avian reassortant influenza viruses. Virology 128:260-263.
    • (1983) Virology , vol.128 , pp. 260-263
    • Hinshaw, V.S.1    Webster, R.G.2    Naeve, C.W.3    Murphy, B.R.4
  • 7
    • 0019165295 scopus 로고
    • The function of the neuraminidase in membrane fusion induced by myxoviruses
    • Huang, R. T., R. Rott, K. Wahn, H.-D. Klenk, and T. Kohama. 1980. The function of the neuraminidase in membrane fusion induced by myxoviruses. Virology 107:313-319.
    • (1980) Virology , vol.107 , pp. 313-319
    • Huang, R.T.1    Rott, R.2    Wahn, K.3    Klenk, H.-D.4    Kohama, T.5
  • 8
    • 0036678137 scopus 로고    scopus 로고
    • Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression
    • Kakugawa, Y., T. Wada, K. Yamaguchi, H. Yamanami, K. Ouchi, I. Sato, and T. Miyagi. 2002. Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression. Proc. Natl. Acad. Sci. USA 99:10718-10723.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10718-10723
    • Kakugawa, Y.1    Wada, T.2    Yamaguchi, K.3    Yamanami, H.4    Ouchi, K.5    Sato, I.6    Miyagi, T.7
  • 9
    • 0027519686 scopus 로고
    • Glycosylation of neuraminidase determines the neurovirulence of influenza A/WSN/33 virus
    • Li, S., J. Schulman, S. Itamura, and P. Palese. 1993. Glycosylation of neuraminidase determines the neurovirulence of influenza A/WSN/33 virus. J. Virol. 6:6667-6673.
    • (1993) J. Virol. , vol.6 , pp. 6667-6673
    • Li, S.1    Schulman, J.2    Itamura, S.3    Palese, P.4
  • 10
    • 0036297142 scopus 로고    scopus 로고
    • Analysis of the desialidation process of the haemagglutinin protein of influenza B virus: The host-dependent desialidation step
    • Luo, C., E. Nobusawa, and K. Nakajima. 2002. Analysis of the desialidation process of the haemagglutinin protein of influenza B virus: the host-dependent desialidation step. J. Gen. Virol. 83:1729-1734.
    • (2002) J. Gen. Virol. , vol.83 , pp. 1729-1734
    • Luo, C.1    Nobusawa, E.2    Nakajima, K.3
  • 11
    • 7644241814 scopus 로고    scopus 로고
    • Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium
    • Matrosovich, M. N., T. Y. Matrosovich, T. Gray, N. A. Roberts, and H.-D. Klenk. 2004. Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J. Virol. 78:12665-12667.
    • (2004) J. Virol. , vol.78 , pp. 12665-12667
    • Matrosovich, M.N.1    Matrosovich, T.Y.2    Gray, T.3    Roberts, N.A.4    Klenk, H.-D.5
  • 12
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman, I., R. Fuchs, and A. Helenius. 1986. Acidification of the endocytic and exocytic pathways. Annu. Rev. Biochem. 55:663-700.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 13
    • 0030907066 scopus 로고    scopus 로고
    • Establishment of a monoclonal antibody directed against Gb3Cer/CD77: A useful immunochemical reagent for a differentiation marker in Burkitt's lymphoma and germinal centre B cells
    • Miyamoto, D., T. Ueno, S. Takashima, K. Ohta, T. Miyawaki, T. Suzuki, and Y. Suzuki. 1997. Establishment of a monoclonal antibody directed against Gb3Cer/CD77: a useful immunochemical reagent for a differentiation marker in Burkitt's lymphoma and germinal centre B cells. Glycoconjugate J. 14:379-388.
    • (1997) Glycoconjugate J. , vol.14 , pp. 379-388
    • Miyamoto, D.1    Ueno, T.2    Takashima, S.3    Ohta, K.4    Miyawaki, T.5    Suzuki, T.6    Suzuki, Y.7
  • 16
    • 0033986824 scopus 로고    scopus 로고
    • Plasmid-driven formation of influenza virus-like particles
    • Neumann, G., T. Watanabe, and Y. Kawaoka. 2000. Plasmid-driven formation of influenza virus-like particles. J. Virol. 74:547-551.
    • (2000) J. Virol. , vol.74 , pp. 547-551
    • Neumann, G.1    Watanabe, T.2    Kawaoka, Y.3
  • 17
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa, H., K. Yamamura, and J. Miyazaki. 1991. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 108:193-199.
    • (1991) Gene , vol.108 , pp. 193-199
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 18
    • 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 6:397-410.
    • (1974) Virology , vol.6 , pp. 397-410
    • Palese, P.1    Tobita, K.2    Ueda, M.3    Compans, R.W.4
  • 19
    • 0030704753 scopus 로고    scopus 로고
    • Differential induction of cytotoxicity and apoptosis by influenza virus strains of differing virulence
    • Price, G. E., H. Smith, and C. Sweet. 1997. Differential induction of cytotoxicity and apoptosis by influenza virus strains of differing virulence. J. Gen. Virol. 78:2821-2829.
    • (1997) J. Gen. Virol. , vol.78 , pp. 2821-2829
    • Price, G.E.1    Smith, H.2    Sweet, C.3
  • 20
    • 0036261855 scopus 로고    scopus 로고
    • Fluorescent cytochemical detection of sialidase activity using 5-bromo-4-chloroindol-3-yl-alpha-D-N-acetylneuraminic acid as the substrate
    • Saito, M., H. Hagita, Y. Iwabuchi, I. Fujii, K. Ikeda, and M. Ito. 2002. Fluorescent cytochemical detection of sialidase activity using 5-bromo-4-chloroindol-3-yl-alpha-D-N-acetylneuraminic acid as the substrate. Histochem. Cell. Biol. 117:453-458.
    • (2002) Histochem. Cell. Biol. , vol.117 , pp. 453-458
    • Saito, M.1    Hagita, H.2    Iwabuchi, Y.3    Fujii, I.4    Ikeda, K.5    Ito, M.6
  • 21
    • 0029929748 scopus 로고    scopus 로고
    • The ion channel activity of the influenza virus M2 protein affects transport through the Golgi apparatus
    • Sakaguchi, T., G. P. Leser, and R. A. Lamb. 1996. The ion channel activity of the influenza virus M2 protein affects transport through the Golgi apparatus. J. Cell Biol. 133:733-747.
    • (1996) J. Cell Biol. , vol.133 , pp. 733-747
    • Sakaguchi, T.1    Leser, G.P.2    Lamb, R.A.3
  • 22
    • 0036229532 scopus 로고    scopus 로고
    • Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore formation
    • Sakai, T., R. Ohuchi, and M. Ohuchi. 2002. Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore formation. J. Virol. 76:4603-4611.
    • (2002) J. Virol. , vol.76 , pp. 4603-4611
    • Sakai, T.1    Ohuchi, R.2    Ohuchi, M.3
  • 23
    • 0017703567 scopus 로고
    • Virulence factors of influenza A viruses: WSN virus neuraminidase required for plaque production in MDBK cells
    • Schulman, J. L., and P. Palese. 1977. Virulence factors of influenza A viruses: WSN virus neuraminidase required for plaque production in MDBK cells. J. Virol. 24:170-176.
    • (1977) J. Virol. , vol.24 , pp. 170-176
    • Schulman, J.L.1    Palese, P.2
  • 24
    • 0036784565 scopus 로고    scopus 로고
    • Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis
    • Sieczkarski, S. B., and G. R. Whittaker. 2002. Influenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis. J. Virol. 76:10455-10464.
    • (2002) J. Virol. , vol.76 , pp. 10455-10464
    • Sieczkarski, S.B.1    Whittaker, G.R.2
  • 27
    • 1642491743 scopus 로고    scopus 로고
    • Evolutional analysis of human influenza A virus N2 neuraminidase genes based on the transition of the low-pH stability of sialidase activity
    • Suzuki, T., T. Takahashi, T. Saito, C.-T. Guo, K. I.-P. J. Hidari, D. Miyamoto, and Y. Suzuki. 2004. Evolutional analysis of human influenza A virus N2 neuraminidase genes based on the transition of the low-pH stability of sialidase activity. FEBS Lett. 557:228-232.
    • (2004) FEBS Lett. , vol.557 , pp. 228-232
    • Suzuki, T.1    Takahashi, T.2    Saito, T.3    Guo, C.-T.4    Hidari, K.I.-P.J.5    Miyamoto, D.6    Suzuki, Y.7
  • 29
    • 0038393119 scopus 로고    scopus 로고
    • A molecular mechanism for the low-pH stability of sialidase activity of influenza A virus N2 neuraminidases
    • Takahashi, T., T. Suzuki, K. I.-P. J. Hidari, D. Miyamoto, and Y. Suzuki. 2003. A molecular mechanism for the low-pH stability of sialidase activity of influenza A virus N2 neuraminidases. FEBS Lett. 543:71-75.
    • (2003) FEBS Lett. , vol.543 , pp. 71-75
    • Takahashi, T.1    Suzuki, T.2    Hidari, K.I.-P.J.3    Miyamoto, D.4    Suzuki, Y.5
  • 30
    • 0029003145 scopus 로고
    • Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase
    • Varghese, J. N., V. C. Epa, and P. M. Colman. 1995. Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase. Protein Sci. 4:1081-1087.
    • (1995) Protein Sci. , vol.4 , pp. 1081-1087
    • Varghese, J.N.1    Epa, V.C.2    Colman, P.M.3
  • 32
    • 0033934134 scopus 로고    scopus 로고
    • Inter-dependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: A study by reverse genetics
    • Wagner, R., T. Wolff, A. Herwig, S. Pleschka, and H.-D. Klenk. 2000. Inter-dependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: a study by reverse genetics. J. Virol. 74:6316-6323.
    • (2000) J. Virol. , vol.74 , pp. 6316-6323
    • Wagner, R.1    Wolff, T.2    Herwig, A.3    Pleschka, S.4    Klenk, H.-D.5
  • 33
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley, D. C., and J. J. Skehel. 1987. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:365-394.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2


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