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Volumn 248, Issue 2, 1998, Pages 284-294

Acylation of the influenza hemagglutinin modulates fusion activity

Author keywords

[No Author keywords available]

Indexed keywords

HEMAGGLUTININ;

EID: 0032169620     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9286     Document Type: Article
Times cited : (36)

References (44)
  • 1
    • 0029823936 scopus 로고    scopus 로고
    • Dilation of the hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events
    • Blumenthal R., Sarkar D. P., Durell S., Howard D. E., Morris S. J. Dilation of the hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events. J. Cell Biol. 135:1996;63-71.
    • (1996) J. Cell Biol. , vol.135 , pp. 63-71
    • Blumenthal, R.1    Sarkar, D.P.2    Durell, S.3    Howard, D.E.4    Morris, S.J.5
  • 2
    • 0028023726 scopus 로고
    • Structure of influenza hemagglutinin at the pH of membrane fusion
    • Bullough P. A., Hughson F. M., Skehel J. J., Wiley D. C. Structure of influenza hemagglutinin at the pH of membrane fusion. Nature. 371:1994;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
  • 3
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr C. M., Kim P. S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell. 73:1993;823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 4
    • 0025816519 scopus 로고
    • Delay time for influenza virus hemagglutinin-induced membrane fusion depends on hemagglutinin surface density
    • Clague M. J., Schoch C., Blumenthal R. Delay time for influenza virus hemagglutinin-induced membrane fusion depends on hemagglutinin surface density. J. Virol. 65:1991;2402-2407.
    • (1991) J. Virol. , vol.65 , pp. 2402-2407
    • Clague, M.J.1    Schoch, C.2    Blumenthal, R.3
  • 5
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • Danieli T., Pelletier S. L., Henis Y. I., White J. M. Membrane fusion mediated by influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 133:1996;559-569.
    • (1996) J. Cell Biol. , vol.133 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 7
    • 0025109728 scopus 로고
    • Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: Role of hemagglutinin surface density
    • Ellens H., Bentz J., Mason D., Zhang F., White J. Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: Role of hemagglutinin surface density. Biochemitsry. 29:1990;9697-9707.
    • (1990) Biochemitsry , vol.29 , pp. 9697-9707
    • Ellens, H.1    Bentz, J.2    Mason, D.3    Zhang, F.4    White, J.5
  • 8
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1,7 Å resolution
    • Fass D., Harrison S. C., Kim P. S. Retrovirus envelope domain at 1,7 Å resolution. Nature Struct. Biol. 3:1996;465-469.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 465-469
    • Fass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 10
    • 0022619527 scopus 로고
    • Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus
    • Gething M.-J., Doms R. W., York D., White J. Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus. J. Cell Biol. 102:1986a;11-23.
    • (1986) J. Cell Biol. , vol.102 , pp. 11-23
    • Gething, M.-J.1    Doms, R.W.2    York, D.3    White, J.4
  • 11
    • 0022552149 scopus 로고
    • Expression of wild type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
    • Gething M.-J., McCammon K., Sambrook J. Expression of wild type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport. Cell. 46:1986b;939-950.
    • (1986) Cell , vol.46 , pp. 939-950
    • Gething, M.-J.1    McCammon, K.2    Sambrook, J.3
  • 12
    • 0019483995 scopus 로고
    • Influenza viruses cause hemolysis and fusion of cells
    • Huang R. T. C., Rott R., Klenk H.-D. Influenza viruses cause hemolysis and fusion of cells. Virology. 110:1981;243-247.
    • (1981) Virology , vol.110 , pp. 243-247
    • Huang, R.T.C.1    Rott, R.2    Klenk, H.-D.3
  • 13
    • 0028102718 scopus 로고
    • The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity
    • Jin H., Leser G. P., Lamb R. A. The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity. EMBO J. 13:1994;5504-5515.
    • (1994) EMBO J. , vol.13 , pp. 5504-5515
    • Jin, H.1    Leser, G.P.2    Lamb, R.A.3
  • 14
    • 0030991137 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape
    • Jin H., Leser G. P, Zhang J., Lamb R. A. Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape. EMBO J. 16:1997;1236-1247.
    • (1997) EMBO J. , vol.16 , pp. 1236-1247
    • Jin, H.1    Leser, G.P.2    Zhang, J.3    Lamb, R.A.4
  • 15
    • 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., Lamb R. A. Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity. J. Virol. 70:1996;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
  • 16
    • 0030965051 scopus 로고    scopus 로고
    • Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopy
    • Kanaseki T., Kawasaki K., Murata M., Ikeuchi Y., Ohnishi S. J. Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopy. J. Cell Biol. 137:1997;1041-1056.
    • (1997) J. Cell Biol. , vol.137 , pp. 1041-1056
    • Kanaseki, T.1    Kawasaki, K.2    Murata, M.3    Ikeuchi, Y.4    Ohnishi, S.J.5
  • 17
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble G. W., Danieli T., White J. M. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell. 76:1994;383-391.
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 18
    • 0028123337 scopus 로고
    • Host cell proteases controlling virus pathogenicity
    • Klenk H.-D., Garten W. Host cell proteases controlling virus pathogenicity. Trends Microbiol. 2:1994;39-43.
    • (1994) Trends Microbiol. , vol.2 , pp. 39-43
    • Klenk, H.-D.1    Garten, W.2
  • 19
    • 0001178028 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • 1445, Lippincott-Raven Publishers, Philadelphia
    • Lamb, R. A. Krug, R. M. 1996, Orthomyxoviridae: The viruses and their replication, In, Fields Virology, 1353, 1445, Lippincott-Raven Publishers, Philadelphia.
    • (1996) In, Fields Virology , pp. 1353
    • Lamb, R.A.1    Krug, R.M.2
  • 20
    • 0022467016 scopus 로고
    • Membrane fusion induced by influenza virus hemagglutinin requires protein bound fatty acids
    • Lambrecht B., Schmidt M. F. G. Membrane fusion induced by influenza virus hemagglutinin requires protein bound fatty acids. FEBS Lett. 202:1986;127-132.
    • (1986) FEBS Lett. , vol.202 , pp. 127-132
    • Lambrecht, B.1    Schmidt, M.F.G.2
  • 21
    • 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., Jin H., Lamb R. A., Cohen F. S. The role of the cytoplasmic tail region of influenza virus hemagglutinin in formation and growth of fusion pores. Virology. 235:1997;118-128.
    • (1997) Virology , vol.235 , pp. 118-128
    • Melikyan, G.B.1    Jin, H.2    Lamb, R.A.3    Cohen, F.S.4
  • 22
    • 0028865392 scopus 로고
    • GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes
    • Melikyan G. B., Whihte J. M., Cohen F. S. GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes. J. Cell Biol. 131:1995;679-691.
    • (1995) J. Cell Biol. , vol.131 , pp. 679-691
    • Melikyan, G.B.1    Whihte, J.M.2    Cohen, F.S.3
  • 23
    • 0024564649 scopus 로고
    • Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin red blood cells
    • Morris S. J., Sarkar D. P., White J. M., Blumenthal R. Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin red blood cells. J. Biol. Chem. 264:1989;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
  • 24
    • 0025053668 scopus 로고
    • Fatty acids on the A/Japan/305/57 influenza virus have a role in membrane fusion
    • Naeve C. W., Williams D. Fatty acids on the A/Japan/305/57 influenza virus have a role in membrane fusion. EMBO J. 9:1990;3957-3866.
    • (1990) EMBO J. , vol.9 , pp. 3957-3866
    • Naeve, C.W.1    Williams, D.2
  • 25
    • 0026447375 scopus 로고
    • Effects of altering palmitoylation sites on biosynthesis and function of the influenza virus hemagglutinin
    • Naim H. Y., Amarneh B., Ktistakis N. T., Roth M. G. Effects of altering palmitoylation sites on biosynthesis and function of the influenza virus hemagglutinin. J. Virol. 66:1992;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
  • 26
    • 0026175939 scopus 로고
    • Comparison of complete amino acid sequences and receptor binding properties among 13 serotypes of hemagglutinins of influenza A viruses
    • Nobusawa E., Aoyama T., Kato H., Suzuki Y., Tateno Y., Nakajima K. Comparison of complete amino acid sequences and receptor binding properties among 13 serotypes of hemagglutinins of influenza A viruses. Virlolgy. 182:1991;475-485.
    • (1991) Virlolgy , vol.182 , pp. 475-485
    • Nobusawa, E.1    Aoyama, T.2    Kato, H.3    Suzuki, Y.4    Tateno, Y.5    Nakajima, K.6
  • 27
    • 0242671942 scopus 로고    scopus 로고
    • Meta-stability of the hemifusion intermediate induced by glycosylphosphatidylinositol-anchored influenza hemagglutinin
    • Nüssler F., Clague M., Herrmann A. Meta-stability of the hemifusion intermediate induced by glycosylphosphatidylinositol-anchored influenza hemagglutinin. Biophys. J. 73:1997;2280-2291.
    • (1997) Biophys. J. , vol.73 , pp. 2280-2291
    • Nüssler, F.1    Clague, M.2    Herrmann, A.3
  • 29
    • 0028828081 scopus 로고
    • Neuraminidase is essential for fowl plaque virus hemagglutinin to show hemagglutinating activity
    • Ohuchi M., Feldmann A., Ohuchi R., Klenk H.-D. Neuraminidase is essential for fowl plaque virus hemagglutinin to show hemagglutinating activity. Virology. 212:1995;77-83.
    • (1995) Virology , vol.212 , pp. 77-83
    • Ohuchi, M.1    Feldmann, A.2    Ohuchi, R.3    Klenk, H.-D.4
  • 30
    • 0031958411 scopus 로고    scopus 로고
    • Elongation of the cytoplasmic tail interferes with the fusion activity of influenza virus hemagglutinin
    • Ohuchi M., Fischer C., Ohuchi R., Herwig A., Klenk H.-D. Elongation of the cytoplasmic tail interferes with the fusion activity of influenza virus hemagglutinin. J. Virol. 72:1998;3554-3559.
    • (1998) J. Virol. , vol.72 , pp. 3554-3559
    • Ohuchi, M.1    Fischer, C.2    Ohuchi, R.3    Herwig, A.4    Klenk, H.-D.5
  • 31
    • 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., Schmidt M. F. G. Assessment of fusogenic properties of influenza virus hemagglutinin deacylated by site directed mutagenesis and hydroxylamine treatment. Virology. 210:1995;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
    • 0020077726 scopus 로고
    • Acylation of viral spike glycoproteins: A feature of enveloped RNA viruses
    • Schmidt M. F. G. Acylation of viral spike glycoproteins: A feature of enveloped RNA viruses. Virology. 116:1982;327-338.
    • (1982) Virology , vol.116 , pp. 327-338
    • Schmidt, M.F.G.1
  • 33
    • 0027190432 scopus 로고
    • Role of the fusion peptide sequence in initial stages of influenza hemagglutinin-induced cell fusion
    • Schoch C., Blumenthal R. Role of the fusion peptide sequence in initial stages of influenza hemagglutinin-induced cell fusion. J. Biol. Chem. 268:1993;9267-9274.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9267-9274
    • Schoch, C.1    Blumenthal, R.2
  • 34
    • 0031975822 scopus 로고    scopus 로고
    • Fusion activity of transmembrane and cytoplasmic chimeras of the influenza virus glycoprotein hemagglutinin
    • Schroth-Diez B., Ponimaskin E., Reverey H., Schmidt M. F. G., Herrmann A. Fusion activity of transmembrane and cytoplasmic chimeras of the influenza virus glycoprotein hemagglutinin. J. Virol. 72:1998;133-141.
    • (1998) J. Virol. , vol.72 , pp. 133-141
    • Schroth-Diez, B.1    Ponimaskin, E.2    Reverey, H.3    Schmidt, M.F.G.4    Herrmann, A.5
  • 35
    • 0026531034 scopus 로고
    • Alterations to influenza virus hemagglutinin cytoplasmic tail modulates virus infectivity
    • Simpson D. A., Lamb R. A. Alterations to influenza virus hemagglutinin cytoplasmic tail modulates virus infectivity. J. Virol. 66:1992;790-803.
    • (1992) J. Virol. , vol.66 , pp. 790-803
    • Simpson, D.A.1    Lamb, R.A.2
  • 36
    • 0028824850 scopus 로고
    • Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin
    • Steinhauer D. A., Wharton S. A., Skehel J. J., Wiley D. C. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. J. Virol. 69:1995;6643-6651.
    • (1995) J. Virol. , vol.69 , pp. 6643-6651
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4
  • 37
    • 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., Skehel J. J. Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties. Virology. 184:1991;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
  • 38
    • 0025815364 scopus 로고
    • Site-specific mutagenesis identifies three cysteine residues in the cytoplasmtic tail as acylation sites of influenza virus hemagglutinin
    • Veit M., Kretzschmar E., Kuroda K., Garten W., Schmidt M. F. G., Klenk H.-D., Rott R. Site-specific mutagenesis identifies three cysteine residues in the cytoplasmtic tail as acylation sites of influenza virus hemagglutinin. J. Virol. 65:1991;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
  • 39
    • 0026748702 scopus 로고
    • Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R
    • Vey M., Orlich M., Adler S., Klenk H.-D., Rott R., Garten W. Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R. Virology. 188:1992;408-413.
    • (1992) Virology , vol.188 , pp. 408-413
    • Vey, M.1    Orlich, M.2    Adler, S.3    Klenk, H.-D.4    Rott, R.5    Garten, W.6
  • 41
    • 0028855669 scopus 로고
    • Electron microscopy of antibody complexes of influenza virus hemagglutinin in the fusion pH conformation
    • Wharton S. A., Cadler L. J., Ruigrok R. W. H., Skehel J. J., Steinhauser D. A., Wiley D. C. Electron microscopy of antibody complexes of influenza virus hemagglutinin in the fusion pH conformation. EMBO J. 14:1995;240-246.
    • (1995) EMBO J. , vol.14 , pp. 240-246
    • Wharton, S.A.1    Cadler, L.J.2    Ruigrok, R.W.H.3    Skehel, J.J.4    Steinhauser, D.A.5    Wiley, D.C.6
  • 42
    • 0002641729 scopus 로고
    • Fusion of influenza virus in endosomes: role of hemagglutinin
    • E. Wimmer, 301, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • White, J. M. 1994, Fusion of influenza virus in endosomes: role of hemagglutinin, In, Cellular Receptors for Animal Viruses, E. Wimmer, 281, 301, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1994) In, Cellular Receptors for Animal Viruses , pp. 281
    • White, J.M.1
  • 43
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley D. C., Skehel J. J. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:1987;365-394.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 44
    • 0028018138 scopus 로고
    • Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation
    • Zurcher T., Luo G., Palese P. Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation. J. Virol. 68:1994;5748-5754.
    • (1994) J. Virol. , vol.68 , pp. 5748-5754
    • Zurcher, T.1    Luo, G.2    Palese, P.3


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