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Volumn 238, Issue 1, 1997, Pages 128-134

The cysteine residues of the M2 protein are not required for influenza A virus replication

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; ION CHANNEL;

EID: 0031564063     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.8809     Document Type: Article
Times cited : (39)

References (42)
  • 1
    • 0027501043 scopus 로고
    • Mutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions
    • Bilsel, P., Castrucci, M. R., and Kawaoka, Y. (1993). Mutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions. J. Virol. 67, 6762-6767.
    • (1993) J. Virol. , vol.67 , pp. 6762-6767
    • Bilsel, P.1    Castrucci, M.R.2    Kawaoka, Y.3
  • 2
    • 0028965329 scopus 로고
    • Reverse genetics system for generation of an influenza A virus mutant containing a deletion of the carboxyl-terminal residue of M2 protein
    • Castrucci, M. R., and Kawaoka, Y. (1995). Reverse genetics system for generation of an influenza A virus mutant containing a deletion of the carboxyl-terminal residue of M2 protein. J. Virol. 69, 2725-2728.
    • (1995) J. Virol. , vol.69 , pp. 2725-2728
    • Castrucci, M.R.1    Kawaoka, Y.2
  • 3
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms, R. W., Lamb, R. A., Rose, J. K., and Helenius, A. (1993). Folding and assembly of viral membrane proteins. Virology 193, 545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 4
    • 0025314308 scopus 로고
    • Introduction of site-specific mutations into the genome of influenza virus
    • Enami, M., Luytjes, W., Krystal, M., and Palese, P. (1990). Introduction of site-specific mutations into the genome of influenza virus. Proc. Natl. Acad. Sci. USA 87, 3802-3805.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3802-3805
    • Enami, M.1    Luytjes, W.2    Krystal, M.3    Palese, P.4
  • 5
    • 0025850680 scopus 로고
    • High-efficiency formation of influenza virus transfectants
    • Enami, M., and Palese, P. (1991). High-efficiency formation of influenza virus transfectants. J. Virol. 65, 2711-2713.
    • (1991) J. Virol. , vol.65 , pp. 2711-2713
    • Enami, M.1    Palese, P.2
  • 6
    • 0025913578 scopus 로고
    • Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defects in virus assembly and budding
    • Gaedigk-Nitschko, K., and Schlesinger, M. J. (1991). Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defects in virus assembly and budding. Virology 183, 206-214.
    • (1991) Virology , vol.183 , pp. 206-214
    • Gaedigk-Nitschko, K.1    Schlesinger, M.J.2
  • 7
    • 0000689283 scopus 로고
    • (F. A. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl, Eds.)
    • Gallagher, S., Whinston, S. E., Fuller, S. A., and Hurrell, J. G. R. (1993). "Current Protocols in Molecular Biology" (F. A. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl, Eds.), pp. 10.8.1-10.8.14.
    • (1993) Current Protocols in Molecular Biology , pp. 1081-10814
    • Gallagher, S.1    Whinston, S.E.2    Fuller, S.A.3    Hurrell, J.G.R.4
  • 8
    • 0022157043 scopus 로고
    • The molecular basis of the specific anti-influenza action of amantadine
    • Hay, A. J., Wolstenholme, A. J., Skehel, J. J., and Smith, M. H. (1985). The molecular basis of the specific anti-influenza action of amantadine. EMBO J. 4, 3021-3024.
    • (1985) EMBO J. , vol.4 , pp. 3021-3024
    • Hay, A.J.1    Wolstenholme, A.J.2    Skehel, J.J.3    Smith, M.H.4
  • 10
    • 0025923280 scopus 로고
    • 2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds
    • 2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology 183, 32-43.
    • (1991) Virology , vol.183 , pp. 32-43
    • Holsinger, L.J.1    Lamb, R.A.2
  • 11
    • 0028895957 scopus 로고
    • Analysis of the posttranslational modifications of the influenza virus M2 protein
    • Holsinger, L. J., Shaughnessy, M. A., Micko, A., Pinto, L. H., and Lamb, R.A. (1995). Analysis of the posttranslational modifications of the influenza virus M2 protein. J. Virol. 69, 1219-1225.
    • (1995) J. Virol. , vol.69 , pp. 1219-1225
    • Holsinger, L.J.1    Shaughnessy, M.A.2    Micko, A.3    Pinto, L.H.4    Lamb, R.A.5
  • 12
    • 0020480083 scopus 로고
    • The sequence of the nucleoprotein gene of human influenza A virus strain, A/NT/60/68
    • Huddleston, J.A., and Brownlee, G.G. (1982). The sequence of the nucleoprotein gene of human influenza A virus strain, A/NT/60/68. Nucleic Acids Res. 10, 1029-1037.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 1029-1037
    • Huddleston, J.A.1    Brownlee, G.G.2
  • 13
    • 0026004791 scopus 로고
    • Evolutionary analysis of the influenza A virus M gene with comparison of the M1 and M2 proteins
    • Ito, T., German, O. T., Kawaoka, Y., Bean, W. J., and Webster, R. G. (1991). Evolutionary analysis of the influenza A virus M gene with comparison of the M1 and M2 proteins. J. Virol. 65, 5491-5498.
    • (1991) J. Virol. , vol.65 , pp. 5491-5498
    • Ito, T.1    German, O.T.2    Kawaoka, Y.3    Bean, W.J.4    Webster, R.G.5
  • 14
    • 0030026752 scopus 로고    scopus 로고
    • Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity
    • Jin, H., Subbarao, K., Bagai, S., Leser, G. P., Murphy, B. R., and Lamb, R.A. (1996). Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity. J. Virol. 70, 1406-1414.
    • (1996) J. Virol. , vol.70 , pp. 1406-1414
    • Jin, H.1    Subbarao, K.2    Bagai, S.3    Leser, G.P.4    Murphy, B.R.5    Lamb, R.A.6
  • 15
    • 0026511206 scopus 로고
    • Amino acid sequence identity between the HA1 of influenza A (H3N2) viruses grown in mammalian and primary chick kidney cells
    • Katz, J.M., and Webster, R.G. (1992). Amino acid sequence identity between the HA1 of influenza A (H3N2) viruses grown in mammalian and primary chick kidney cells. J. Gen. Virol. 73, 1159-1165.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1159-1165
    • Katz, J.M.1    Webster, R.G.2
  • 16
    • 0022999809 scopus 로고
    • The HLA-D-associated invariant chain binds palmitic acid at the cysteine adjacent to the membrane segment
    • Koch, N., and Hammerling, G. J. (1986). The HLA-D-associated invariant chain binds palmitic acid at the cysteine adjacent to the membrane segment. J. Biol. Chem. 261, 3434-3440.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3434-3440
    • Koch, N.1    Hammerling, G.J.2
  • 17
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., Roberts, J. D., and Zakour, R. A. (1987). Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154, 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 18
    • 0002774193 scopus 로고
    • (R. M. Krug, Ed.), Plenum, New York
    • Lamb, R. A. (1989). "The Influenza Viruses" (R. M. Krug, Ed.), pp. 1-87. Plenum, New York.
    • (1989) The Influenza Viruses , pp. 1-87
    • Lamb, R.A.1
  • 19
    • 0028972550 scopus 로고
    • Abortive infection of Vero cells by an influenza A virus (FPV)
    • Lau, S. C., and Scholtissek, C. (1995). Abortive infection of Vero cells by an influenza A virus (FPV). Virology 212, 225-231.
    • (1995) Virology , vol.212 , pp. 225-231
    • Lau, S.C.1    Scholtissek, C.2
  • 20
    • 0002865618 scopus 로고
    • (K. Habel and N. P. Salzman, Eds.), Academic Press, New York
    • Laver, W. G. (1969). In "Fundamental Techniques in Virology" (K. Habel and N. P. Salzman, Eds.), pp. 82-86. Academic Press, New York.
    • (1969) Fundamental Techniques in Virology , pp. 82-86
    • Laver, W.G.1
  • 21
    • 0025317460 scopus 로고
    • Dynamic nature of the quaternary structure of the vesicular stomatitis virus envelope glycoprotein
    • Lyles, D.S., Varela, V.A., and Parce, J.W. (1990). Dynamic nature of the quaternary structure of the vesicular stomatitis virus envelope glycoprotein. Biochemistry 29, 2442-2449.
    • (1990) Biochemistry , vol.29 , pp. 2442-2449
    • Lyles, D.S.1    Varela, V.A.2    Parce, J.W.3
  • 22
    • 0026584715 scopus 로고
    • Subunit interactions of vesicular stomatitis virus envelope glycoprotein stabilized by binding to viral matrix protein
    • Lyles, D. S., McKenzie, M., and Parce, J. W. (1992). Subunit interactions of vesicular stomatitis virus envelope glycoprotein stabilized by binding to viral matrix protein. J. Virol. 66, 349-358.
    • (1992) J. Virol. , vol.66 , pp. 349-358
    • Lyles, D.S.1    McKenzie, M.2    Parce, J.W.3
  • 24
    • 0025053668 scopus 로고
    • Fatty acids on the A/Japan/305/ 57 influenza virus hemagglutinin have a role in membrane fusion
    • Naeve, C. W., and Williams, D. (1990). Fatty acids on the A/Japan/305/ 57 influenza virus hemagglutinin have a role in membrane fusion. EMBO J. 9, 3857-3866.
    • (1990) EMBO J. , vol.9 , pp. 3857-3866
    • Naeve, C.W.1    Williams, D.2
  • 25
    • 0028081894 scopus 로고
    • Rescue of vector-expressed fowl plague virus hemagglutinin in biologically active form by acidotropic agents and coexpressed M2 protein
    • Ohuchi, M., Cramer, A., Vey, M., Ohuchi, R., Garten, W., and Klenk, H. D. (1994). Rescue of vector-expressed fowl plague virus hemagglutinin in biologically active form by acidotropic agents and coexpressed M2 protein. J. Virol. 68, 920-926.
    • (1994) J. Virol. , vol.68 , pp. 920-926
    • Ohuchi, M.1    Cramer, A.2    Vey, M.3    Ohuchi, R.4    Garten, W.5    Klenk, H.D.6
  • 26
  • 27
    • 0026502806 scopus 로고
    • Oligomeric organization and strain-specific proteolytic modification of the virion M2 protein of influenza A H1N1 viruses
    • Panayotov, P. P., and Schlesinger, R. W. (1992). Oligomeric organization and strain-specific proteolytic modification of the virion M2 protein of influenza A H1N1 viruses. Virology 186, 352-355.
    • (1992) Virology , vol.186 , pp. 352-355
    • Panayotov, P.P.1    Schlesinger, R.W.2
  • 28
  • 29
    • 0029033820 scopus 로고
    • Assessment of fusogenic properties of influenza virus hemagglutinin deacylated by site-directed mutagenesis and hydroxylamine treatment
    • Philipp, H. C., Schroth, B., Veit, M., Krumbiegel, M., Herrmann, A., and Schmidt, M. F. G. (1995). Assessment of fusogenic properties of influenza virus hemagglutinin deacylated by site-directed mutagenesis and hydroxylamine treatment. Virology 210, 20-28.
    • (1995) Virology , vol.210 , pp. 20-28
    • Philipp, H.C.1    Schroth, B.2    Veit, M.3    Krumbiegel, M.4    Herrmann, A.5    Schmidt, M.F.G.6
  • 32
    • 0025882934 scopus 로고
    • Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties
    • Steinhauer, D. A., Wharton, S. A., Wiley, D. C., and Skehel, J. J. (1991). Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties. Virology 184, 445-448.
    • (1991) Virology , vol.184 , pp. 445-448
    • Steinhauer, D.A.1    Wharton, S.A.2    Wiley, D.C.3    Skehel, J.J.4
  • 33
    • 0025076814 scopus 로고
    • Palmitoylation of the influenza A virus M2 protein
    • Sugrue, R. J., Belshe, R. B., and Hay, A. J. (1990). Palmitoylation of the influenza A virus M2 protein. Virology 179, 51-56.
    • (1990) Virology , vol.179 , pp. 51-56
    • Sugrue, R.J.1    Belshe, R.B.2    Hay, A.J.3
  • 34
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel
    • Sugrue, R. J., and Hay, A. J. (1991). Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel. Virology 180, 617-624.
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 35
    • 0028177960 scopus 로고
    • Influenza virus M2 protein ion channel activity stabilizes the native form of fowl plague virus hemagglutinin during intracellular transport
    • Takeuchi, K., and Lamb, R.A. (1994). Influenza virus M2 protein ion channel activity stabilizes the native form of fowl plague virus hemagglutinin during intracellular transport. J. Virol. 68, 911-919.
    • (1994) J. Virol. , vol.68 , pp. 911-919
    • Takeuchi, K.1    Lamb, R.A.2
  • 36
    • 0025754428 scopus 로고
    • The M2 protein of influenza A virus is acylated
    • Veit, M., Klenk, H.-D., Kendal, A., and Rott, R. (1991a). The M2 protein of influenza A virus is acylated. J. Gen. Virol. 72, 1461-1465.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1461-1465
    • Veit, M.1    Klenk, H.-D.2    Kendal, A.3    Rott, R.4
  • 37
    • 0025815364 scopus 로고
    • Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin
    • Veit, M., Kretzschmar, E., Kuroda, K., Garten, W., Schmidt, M. F. G., Klenk, H.-D., and Rott, R. (1991b). Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin. J. Virol. 65, 2491-2500.
    • (1991) J. Virol. , vol.65 , pp. 2491-2500
    • Veit, M.1    Kretzschmar, E.2    Kuroda, K.3    Garten, W.4    Schmidt, M.F.G.5    Klenk, H.-D.6    Rott, R.7
  • 38
    • 0026326156 scopus 로고
    • Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions
    • Whitt, M. A., and Rose, J. K. (1991). Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions. Virology 185, 875-878.
    • (1991) Virology , vol.185 , pp. 875-878
    • Whitt, M.A.1    Rose, J.K.2
  • 39
    • 0026480797 scopus 로고
    • Subunit interactions of vesicular stomatitis virus envelope glycoprotein influenced by detergent micelles and lipid bilayers
    • Wilcox, M. D., McKenzie, M.O., Parce, J.W., and Lyles, D.S. (1992). Subunit interactions of vesicular stomatitis virus envelope glycoprotein influenced by detergent micelles and lipid bilayers. Biochemistry 31, 10458-10464.
    • (1992) Biochemistry , vol.31 , pp. 10458-10464
    • Wilcox, M.D.1    McKenzie, M.O.2    Parce, J.W.3    Lyles, D.S.4
  • 40
    • 0027428435 scopus 로고
    • Dynamic equilibrium between vesicular stomatitis virus glycoprotein monomers and trimers in the Golgi and at the cell surface
    • Zagouras, P., and Rose, J. K. (1993). Dynamic equilibrium between vesicular stomatitis virus glycoprotein monomers and trimers in the Golgi and at the cell surface. J. Virol. 67, 7533-7538.
    • (1993) J. Virol. , vol.67 , pp. 7533-7538
    • Zagouras, P.1    Rose, J.K.2
  • 41
    • 0023820458 scopus 로고
    • Influenza A virus M2 protein: Monoclonal antibody restriction of virus growth and detection of M2 in virions
    • Zebedee, S. L., and Lamb, R.A. (1988). Influenza A virus M2 protein: Monoclonal antibody restriction of virus growth and detection of M2 in virions. J. Virol. 62, 2762-2772.
    • (1988) J. Virol. , vol.62 , pp. 2762-2772
    • Zebedee, S.L.1    Lamb, R.A.2
  • 42
    • 0028018138 scopus 로고
    • Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation
    • Zurcher, T., Luo, G., and Palese, P. (1994). Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation. J. Virol. 68, 5748-5754.
    • (1994) J. Virol. , vol.68 , pp. 5748-5754
    • Zurcher, T.1    Luo, G.2    Palese, P.3


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