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Volumn 72, Issue 5, 1998, Pages 3554-3559

Elongation of the cytoplasmic tail interferes with the fusion activity of influenza virus hemagglutinin

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; VIRUS HEMAGGLUTININ; VIRUS PROTEIN;

EID: 0031958411     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.5.3554-3559.1998     Document Type: Article
Times cited : (35)

References (39)
  • 1
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371: 37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 2
    • 0021931766 scopus 로고
    • A deletion mutation in the 5′ part of the pol gene of Moloney murine leukemia virus blocks proteolytic processing of the Gag and Pol polyproteins
    • Crawford, S., and S. P. Goff. 1985. A deletion mutation in the 5′ part of the pol gene of Moloney murine leukemia virus blocks proteolytic processing of the Gag and Pol polyproteins. J. Virol. 53:899-907.
    • (1985) J. Virol. , vol.53 , pp. 899-907
    • Crawford, S.1    Goff, S.P.2
  • 3
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 angstrom resolution
    • Fass, D., S. C. Harrison, and P. S. Kim. 1996. Retrovirus envelope domain at 1.7 angstrom resolution. Nat. Struct. Biol. 3:465-469.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 465-469
    • Fass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 5
    • 0019844429 scopus 로고
    • Sequence-specific antibodies show that maturation of Moloney leukemia virus envelope polyprotein involves removal of a COOH-terminal peptide
    • Green, N., T. M. Shinnick, O. Witte, A. Ponticelli, J. G. Sutcliffe, and R. A. Lerner. 1981. Sequence-specific antibodies show that maturation of Moloney leukemia virus envelope polyprotein involves removal of a COOH-terminal peptide. Proc. Natl. Acad. Sci. USA 78:6023-6027.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6023-6027
    • Green, N.1    Shinnick, T.M.2    Witte, O.3    Ponticelli, A.4    Sutcliffe, J.G.5    Lerner, R.A.6
  • 6
    • 0019483995 scopus 로고
    • Influenza viruses cause hemolysis and fusion of cells
    • Huang, R. T., R. Rott, and H.-D. Klenk. 1981. Influenza viruses cause hemolysis and fusion of cells. Virology 110:243-247.
    • (1981) Virology , vol.110 , pp. 243-247
    • Huang, R.T.1    Rott, R.2    Klenk, H.-D.3
  • 7
    • 0028102718 scopus 로고
    • The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity
    • Jin, H., G. P. Leser, and R. A. Lamb. 1994. The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity. EMBO J. 13: 5504-5515.
    • (1994) EMBO J. , vol.13 , pp. 5504-5515
    • Jin, H.1    Leser, G.P.2    Lamb, R.A.3
  • 8
    • 0030026752 scopus 로고    scopus 로고
    • Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity
    • Jin, H., K. Subbarao, S. Bagai, G. P. Leser, B. R. Murphy, and R. A. Lamb. 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
  • 10
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble, G. W., T. Danieli, and J. M. White. 1994. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 76:383-391.
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 11
    • 0027199871 scopus 로고
    • GPI- and transmembrane-anchored influenza hemagglutinin differ in structure and receptor binding activity
    • Kemble, G. W., Y. I. Henis, and J. M. White. 1993. GPI- and transmembrane-anchored influenza hemagglutinin differ in structure and receptor binding activity. J. Cell Biol. 122:1253-1265.
    • (1993) J. Cell Biol. , vol.122 , pp. 1253-1265
    • Kemble, G.W.1    Henis, Y.I.2    White, J.M.3
  • 12
    • 0019203091 scopus 로고
    • Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytes
    • Maeda, T., and S. Ohnishi. 1980. Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytes. FEBS Lett. 122:283-287.
    • (1980) FEBS Lett. , vol.122 , pp. 283-287
    • Maeda, T.1    Ohnishi, S.2
  • 13
    • 0030776258 scopus 로고    scopus 로고
    • Membrane rearrangements in fusion mediated by viral proteins
    • Melikyan, G. B., and L. V. Chernomordik. 1997. Membrane rearrangements in fusion mediated by viral proteins. Trends Microbiol. 5:349-355.
    • (1997) Trends Microbiol. , vol.5 , pp. 349-355
    • Melikyan, G.B.1    Chernomordik, L.V.2
  • 14
    • 0030848463 scopus 로고    scopus 로고
    • The role of the cytoplasmic tail region of influenza virus hemagglutinin in formation and growth of fusion pores
    • Melikyan, G. B., H. Jin, R. A. Lamb, and F. S. Cohen. 1997. The role of the cytoplasmic tail region of influenza virus hemagglutinin in formation and growth of fusion pores. Virology 235:118-128.
    • (1997) Virology , vol.235 , pp. 118-128
    • Melikyan, G.B.1    Jin, H.2    Lamb, R.A.3    Cohen, F.S.4
  • 15
    • 0028865392 scopus 로고
    • GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes
    • Melikyan, G. B., J. M. White, and F. S. Cohen. 1995. GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes. J. Cell Biol. 131:679-691.
    • (1995) J. Cell Biol. , vol.131 , pp. 679-691
    • Melikyan, G.B.1    White, J.M.2    Cohen, F.S.3
  • 16
    • 0024564649 scopus 로고
    • Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin and red blood cells
    • Morris, S. J., D. P. Sarkar, J. M. White, and R. Blumenthal. 1989. Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin and red blood cells. J. Biol. Chem. 264:3972-3978.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3972-3978
    • Morris, S.J.1    Sarkar, D.P.2    White, J.M.3    Blumenthal, R.4
  • 17
    • 0026725456 scopus 로고
    • Cytoplasmic domain truncation enhances fusion activity by the exterior glycoprotein complex of human immunodeficiency virus type 2 in selected cell types
    • Mulligan, M. J., G. V. Yamshchikov, G. D. Ritter, Jr., F. Gao, M. J. Jin, C. D. Nail, C. P. Spies, B. H. Hahn, and R. W. Compans. 1992. Cytoplasmic domain truncation enhances fusion activity by the exterior glycoprotein complex of human immunodeficiency virus type 2 in selected cell types. J. Virol. 66:3971-3975.
    • (1992) J. Virol. , vol.66 , pp. 3971-3975
    • Mulligan, M.J.1    Yamshchikov, G.V.2    Ritter Jr., G.D.3    Gao, F.4    Jin, M.J.5    Nail, C.D.6    Spies, C.P.7    Hahn, B.H.8    Compans, R.W.9
  • 18
    • 0025053668 scopus 로고
    • Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion
    • Naeve, C. W., and D. Williams. 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
  • 19
    • 0026447375 scopus 로고
    • Effects of altering palmitylation sites on biosynthesis and function of the influenza virus hemagglutinin
    • Naim, H. Y., B. Amarneh, N. T. Ktistakis, and M. G. Roth. 1992. Effects of altering palmitylation sites on biosynthesis and function of the influenza virus hemagglutinin. J. Virol. 66:7585-7588.
    • (1992) J. Virol. , vol.66 , pp. 7585-7588
    • Naim, H.Y.1    Amarneh, B.2    Ktistakis, N.T.3    Roth, M.G.4
  • 20
    • 0028081894 scopus 로고
    • Rescue of vector-expressed fowl plague virus hemagglutinin in biologically active form by acidotropic agents and coexpressed M2 protein
    • Ohuchi, M., A. Cramer, M. Vey, R. Ohuchi, W. Garten, and H.-D. Klenk. 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
  • 21
    • 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
  • 22
    • 0028271720 scopus 로고
    • pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: Implications for the role of the R peptide and p12E TM in viral entry
    • Ragheb, J. A., and W. F. Anderson. 1994. pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: implications for the role of the R peptide and p12E TM in viral entry. J. Virol. 68:3220-3231.
    • (1994) J. Virol. , vol.68 , pp. 3220-3231
    • Ragheb, J.A.1    Anderson, W.F.2
  • 23
    • 0028047579 scopus 로고
    • Function of the cytoplasmic domain of a retroviral transmembrane protein: p15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein
    • Rein, A., J. Mirro, J. G. Haynes, S. M. Ernst, and K. Nagashima. 1994. Function of the cytoplasmic domain of a retroviral transmembrane protein: p15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein. J. Virol. 68:1773-1781.
    • (1994) J. Virol. , vol.68 , pp. 1773-1781
    • Rein, A.1    Mirro, J.2    Haynes, J.G.3    Ernst, S.M.4    Nagashima, K.5
  • 24
    • 0025282289 scopus 로고
    • Synthesis and processing of the transmembrane envelope protein of equine infectious anemia virus
    • Rice, N. R., L. E. Henderson, R. C. Sowder, T. D. Copeland, S. Oroszlan, and J. F. Edwards. 1990. Synthesis and processing of the transmembrane envelope protein of equine infectious anemia virus. J. Virol. 64:3770-3778.
    • (1990) J. Virol. , vol.64 , pp. 3770-3778
    • Rice, N.R.1    Henderson, L.E.2    Sowder, R.C.3    Copeland, T.D.4    Oroszlan, S.5    Edwards, J.F.6
  • 25
    • 0027428352 scopus 로고
    • Cell fusion activity of the simian immunodeficiency virus envelope protein is modulated by the intracytoplasmic domain
    • Ritter, G. D., Jr., M. J. Mulligan, S. L. Jydy, and R. W. Compans. 1993. Cell fusion activity of the simian immunodeficiency virus envelope protein is modulated by the intracytoplasmic domain. Virology 197:255-264.
    • (1993) Virology , vol.197 , pp. 255-264
    • Ritter Jr., G.D.1    Mulligan, M.J.2    Jydy, S.L.3    Compans, R.W.4
  • 26
    • 0026531034 scopus 로고
    • Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity
    • Simpson, D. A., and R. A. Lamb. 1992. Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity. J. Virol. 66:790-803.
    • (1992) J. Virol. , vol.66 , pp. 790-803
    • Simpson, D.A.1    Lamb, R.A.2
  • 27
    • 0022518143 scopus 로고
    • Role of the HTLV-III/LAV envelope in syncytium formation and cytopathicity
    • Sodroski, J., W. C. Goh, C. Rosen, K. Campbell, and W. A. Haseltine. 1986. Role of the HTLV-III/LAV envelope in syncytium formation and cytopathicity. Nature 322:470-474.
    • (1986) Nature , vol.322 , pp. 470-474
    • Sodroski, J.1    Goh, W.C.2    Rosen, C.3    Campbell, K.4    Haseltine, W.A.5
  • 28
    • 0026764061 scopus 로고
    • Effect of retroviral proteinase inhibitors on Mason-Pfizer monkey virus maturation and transmembrane glycoprotein cleavage
    • Sommerfelt, M. A., S. R. Petteway, Jr., G. B. Dreyer, and E. Hunter. 1992. Effect of retroviral proteinase inhibitors on Mason-Pfizer monkey virus maturation and transmembrane glycoprotein cleavage. J. Virol. 66:4220-4227.
    • (1992) J. Virol. , vol.66 , pp. 4220-4227
    • Sommerfelt, M.A.1    Petteway Jr., S.R.2    Dreyer, G.B.3    Hunter, E.4
  • 29
    • 0025882934 scopus 로고
    • Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties
    • Steinhauer, D. A., S. A. Wharton, D. C. Wiley, and J. J. Skehel. 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
  • 30
    • 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 R. A. Lamb. 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
  • 31
    • 0025815364 scopus 로고
    • Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin
    • Veit, M., E. Kretzschmar, K. Kuroda, W. Garten, M. F. G. Schmidt, H.-D. Klenk, and R. Rott. 1991. 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
  • 33
    • 0028855669 scopus 로고
    • Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
    • Wharton, S. A., L. J. Calder, R. W. Ruigrok, J. J. Skehel, D. A. Steinhauer, and D. C. Wiley. 1995. Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation. EMBO J. 14: 240-246.
    • (1995) EMBO J. , vol.14 , pp. 240-246
    • Wharton, S.A.1    Calder, L.J.2    Ruigrok, R.W.3    Skehel, J.J.4    Steinhauer, D.A.5    Wiley, D.C.6
  • 34
    • 0023574003 scopus 로고
    • Anti-peptide antibodies detect steps in a protein conformational change: Low pH activation of influenza virus hemagglutinin
    • White, J. M., and I. A. Wilson. 1987. Anti-peptide antibodies detect steps in a protein conformational change: low pH activation of influenza virus hemagglutinin. J. Cell Biol. 105:2887-2896.
    • (1987) J. Cell Biol. , vol.105 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 35
    • 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. 56:365-395.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-395
    • Wiley, D.C.1    Skehel, J.J.2
  • 36
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I. A., J. J. Skehel, and D. C. Wiley. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 182:366-373.
    • (1981) Nature , vol.182 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 37
    • 0029656198 scopus 로고    scopus 로고
    • Analysis of the cell fusion activities of chimeric simian immunodeficiency virus-murine leukemia virus envelope proteins: Inhibitory effects of the R peptide
    • Yang, C., and R. W. Compans. 1996. Analysis of the cell fusion activities of chimeric simian immunodeficiency virus-murine leukemia virus envelope proteins: inhibitory effects of the R peptide. J. Virol. 70:248-254.
    • (1996) J. Virol. , vol.70 , pp. 248-254
    • Yang, C.1    Compans, R.W.2
  • 38
    • 0027523446 scopus 로고
    • Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein increases Env incorporation into particles and fusogenicity and infectivity
    • Zingler, K., and D. R. Littman. 1993. Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein increases Env incorporation into particles and fusogenicity and infectivity. J. Virol. 67: 2824-2831.
    • (1993) J. Virol. , vol.67 , pp. 2824-2831
    • Zingler, K.1    Littman, D.R.2
  • 39
    • 0028018138 scopus 로고
    • Mutations at palmitylation sites of the influenza virus hemaggiutinin affect virus formation
    • Zürcher, T., G. Luo, and P. Palese. 1994. Mutations at palmitylation sites of the influenza virus hemaggiutinin affect virus formation. J. Virol. 68:5748-5754.
    • (1994) J. Virol. , vol.68 , pp. 5748-5754
    • Zürcher, T.1    Luo, G.2    Palese, P.3


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