메뉴 건너뛰기




Volumn 77, Issue 6, 1999, Pages 3144-3151

Hemifusion between cells expressing hemagglutinin of influenza virus and planar membranes can precede the formation of fusion pores that subsequently fully enlarge

Author keywords

[No Author keywords available]

Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ;

EID: 0032785902     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77144-4     Document Type: Article
Times cited : (36)

References (32)
  • 1
    • 0029823936 scopus 로고    scopus 로고
    • Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events
    • Blumenthal, R., D. P. Sarkar, S. Durell, D. E. Howard, and S. J. Morris. 1996. Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events. J. Cell Biol. 135: 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., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza hemagglutinin 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
  • 3
    • 0031445916 scopus 로고    scopus 로고
    • Flickering fusion pores comparable with initial exocytotic pores occur in protein-free phospholipid bilayers
    • Chanturiya, A., L. V. Chernomordik, and J. Zimmerberg. 1997. Flickering fusion pores comparable with initial exocytotic pores occur in protein-free phospholipid bilayers. Proc. Natl. Acad. Sci. USA. 94: 14423-14428.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14423-14428
    • Chanturiya, A.1    Chernomordik, L.V.2    Zimmerberg, J.3
  • 4
    • 0031012628 scopus 로고    scopus 로고
    • An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids
    • Chernomordik, L. V., E. Leikina, V. Frolov, P. Bronk, and J. Zimmerberg. 1997. An early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids. J. Cell Biol. 136:81-93.
    • (1997) J. Cell Biol. , vol.136 , pp. 81-93
    • Chernomordik, L.V.1    Leikina, E.2    Frolov, V.3    Bronk, P.4    Zimmerberg, J.5
  • 5
    • 0032559801 scopus 로고    scopus 로고
    • The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pore formation
    • Chernomordik, L. V., V. A. Frolov, E. Leikina, P. Bronk, and J. Zimmerberg. 1998. The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation. J. Cell Biol. 140:1369-1382.
    • (1998) J. Cell Biol. , vol.140 , pp. 1369-1382
    • Chernomordik, L.V.1    Frolov, V.A.2    Leikina, E.3    Bronk, P.4    Zimmerberg, J.5
  • 7
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • Danieli, T., S. L. Pelletier, Y. I. Henis, and J. M. White. 1996. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 133: 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
  • 8
    • 0021879568 scopus 로고
    • An efficient method for introducing macromolecules into living cells
    • Doxsey, S. J., J. Sambrook, A. Helenius, and J. White. 1985. An efficient method for introducing macromolecules into living cells. J. Cell Biol. 101:19-27.
    • (1985) J. Cell Biol. , vol.101 , pp. 19-27
    • Doxsey, S.J.1    Sambrook, J.2    Helenius, A.3    White, J.4
  • 9
    • 0024395540 scopus 로고
    • Digital fluorescence imaging of fusion of influenza virus with erythrocytes
    • Georgiou, G. N., I. E. Morrison, and R. J. Cherry. 1989. Digital fluorescence imaging of fusion of influenza virus with erythrocytes. FEBS Lett. 250:487-492.
    • (1989) FEBS Lett. , vol.250 , pp. 487-492
    • Georgiou, G.N.1    Morrison, I.E.2    Cherry, R.J.3
  • 11
    • 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
  • 12
    • 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
  • 13
    • 0027517094 scopus 로고
    • Early events of Semliki Forest virus-induced cell-cell fusion
    • Lanzrein, M., N. K. Esermann, R. Weingart, and C. Kempf. 1993. Early events of Semliki Forest virus-induced cell-cell fusion. Virology. 196: 541-547.
    • (1993) Virology , vol.196 , pp. 541-547
    • Lanzrein, M.1    Esermann, N.K.2    Weingart, R.3    Kempf, C.4
  • 14
    • 0030943586 scopus 로고    scopus 로고
    • Evolution of lipidic structures during model membrane fusion and the relation of this process to cell membrane fusion
    • Lee, J., and B. R. Lentz. 1997. Evolution of lipidic structures during model membrane fusion and the relation of this process to cell membrane fusion. Biochemistry. 36:6251-6259.
    • (1997) Biochemistry , vol.36 , pp. 6251-6259
    • Lee, J.1    Lentz, B.R.2
  • 15
    • 0029156059 scopus 로고
    • Structure and function of fusion pores in exocytosis and ectoplasmic membrane fusion
    • Lindau, M., and W. Almers. 1995. Structure and function of fusion pores in exocytosis and ectoplasmic membrane fusion. Curr. Opin. Cell Biol. 7:509-517.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 509-517
    • Lindau, M.1    Almers, W.2
  • 16
    • 0025192947 scopus 로고
    • Observation of single influenza virus-cell fusion and measurement by fluorescence video microscopy
    • Lowy, R. J., D. P. Sarkar, Y. Chen, and R. Blumenthal. 1990. Observation of single influenza virus-cell fusion and measurement by fluorescence video microscopy. Proc. Natl. Acad Sci. USA. 87:1850-1854.
    • (1990) Proc. Natl. Acad Sci. USA , vol.87 , pp. 1850-1854
    • Lowy, R.J.1    Sarkar, D.P.2    Chen, Y.3    Blumenthal, R.4
  • 17
    • 0028838681 scopus 로고
    • Comparison of transient and successful fusion pores connecting influenza hemagglutinin expressing cells to planar membranes
    • Melikyan, G. B., W. D. Niles, V. A. Ratinov, M. Karhanek, J. Zimmerberg, and F. S. Cohen. 1995a. Comparison of transient and successful fusion pores connecting influenza hemagglutinin expressing cells to planar membranes. J. Gen. Physiol. 106:803-819.
    • (1995) J. Gen. Physiol. , vol.106 , pp. 803-819
    • Melikyan, G.B.1    Niles, W.D.2    Ratinov, V.A.3    Karhanek, M.4    Zimmerberg, J.5    Cohen, F.S.6
  • 18
    • 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. 1995b. 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
  • 19
    • 0029998570 scopus 로고    scopus 로고
    • Voltage-dependent translocation of R18 and Dil across lipid bilayers leads to fluorescence changes
    • Melikyan, G. B., B. N. Deriy, D. C. Ok, and F. S. Cohen. 1996. Voltage-dependent translocation of R18 and Dil across lipid bilayers leads to fluorescence changes. Biophys. J. 71:2680-2691.
    • (1996) Biophys. J. , vol.71 , pp. 2680-2691
    • Melikyan, G.B.1    Deriy, B.N.2    Ok, D.C.3    Cohen, F.S.4
  • 20
    • 0033017030 scopus 로고    scopus 로고
    • Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion
    • Melikyan, G. B., S. Lin, M. G. Roth, and F. S. Cohen. 1999. Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion. Molec. Biol. Cell. 10:1821-1836.
    • (1999) Molec. Biol. Cell. , vol.10 , pp. 1821-1836
    • Melikyan, G.B.1    Lin, S.2    Roth, M.G.3    Cohen, F.S.4
  • 22
    • 0026352906 scopus 로고
    • Fusion of influenza virions with a planar lipid membrane detected bv video fluorescence microscopy
    • Niles, W. D., and F. S. Cohen. 1991. Fusion of influenza virions with a planar lipid membrane detected bv video fluorescence microscopy. J. Gen. Physiol. 97:1101-1119.
    • (1991) J. Gen. Physiol. , vol.97 , pp. 1101-1119
    • Niles, W.D.1    Cohen, F.S.2
  • 23
    • 0242671942 scopus 로고    scopus 로고
    • Meta-stability of the hemifusion intermediate induced by glycosylphosphatidylinositol-anchored influenza hemagglutinin
    • Nüssler, F., M. J. Clague, and A. Herrmann. 1997. Meta-stability of the hemifusion intermediate induced by glycosylphosphatidylinositol-anchored influenza hemagglutinin. Biophys. J. 73:2280-2291.
    • (1997) Biophys. J. , vol.73 , pp. 2280-2291
    • Nüssler, F.1    Clague, M.J.2    Herrmann, A.3
  • 24
    • 0033166840 scopus 로고    scopus 로고
    • Directly observed membrane fusion between oppositely charged phospholipid bilayers
    • Pantazatos, D. P., and R. C. MacDonald. 1999. Directly observed membrane fusion between oppositely charged phospholipid bilayers. J. Membrane Biol. 170:27-38.
    • (1999) J. Membrane Biol. , vol.170 , pp. 27-38
    • Pantazatos, D.P.1    MacDonald, R.C.2
  • 25
    • 0030472394 scopus 로고    scopus 로고
    • The initial fusion pore induced by baculovirus GP64 is large and forms quickly
    • Plonsky, I., and J. Zimmerberg. 1996. The initial fusion pore induced by baculovirus GP64 is large and forms quickly. J. Cell Biol. 135: 1831-1839.
    • (1996) J. Cell Biol. , vol.135 , pp. 1831-1839
    • Plonsky, I.1    Zimmerberg, J.2
  • 26
    • 0032812477 scopus 로고    scopus 로고
    • A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusisn phenotype
    • Qiao, H., R. T. Armstrong, G. B. Melikyan, F. S. Cohen, and J. M. White. 1999. A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusisn phenotype. Mol. Biol. Cell. 10:2759-2769.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 2759-2769
    • Qiao, H.1    Armstrong, R.T.2    Melikyan, G.B.3    Cohen, F.S.4    White, J.M.5
  • 27
    • 0031954979 scopus 로고    scopus 로고
    • Fusion pore conductance: Experimental approaches and theoretical algorithms
    • Ratihov, V., I. Plonsky, and J. Zimmerberg. 1998. Fusion pore conductance: experimental approaches and theoretical algorithms. Biophys. J. 74:2374-2387.
    • (1998) Biophys. J. , vol.74 , pp. 2374-2387
    • Ratihov, V.1    Plonsky, I.2    Zimmerberg, J.3
  • 28
    • 0031697748 scopus 로고    scopus 로고
    • Effects of spontaneous bilayer curvature on influenza virus-mediated fusion pores
    • Razinkov, V. I., G. B. Melikyan, R. M. Epand, R. F. Epand, and F. S. Cohen. 1998. Effects of spontaneous bilayer curvature on influenza virus-mediated fusion pores. J. Gen. Physiol. 112:409-422.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 409-422
    • Razinkov, V.I.1    Melikyan, G.B.2    Epand, R.M.3    Epand, R.F.4    Cohen, F.S.5
  • 29
    • 0022970310 scopus 로고
    • Human influenza A virus hemagglutinin distinguishes sialyloligosaccharides in membrane-associated gangliosides as its receptor which mediates the adsorption and fusion processes of virus infection. Specificity for oligosaccharides and sialic acids and the sequence to which sialic acid is attached
    • Suzuki, Y., Y. Nagao, H. Kato, M. Matsumoto, K. Nerome, K. Nakajima, and E. Nobusawa. 1986. Human influenza A virus hemagglutinin distinguishes sialyloligosaccharides in membrane-associated gangliosides as its receptor which mediates the adsorption and fusion processes of virus infection. Specificity for oligosaccharides and sialic acids and the sequence to which sialic acid is attached. J. Biol. Chem. 261: 17057-17061.
    • (1986) J. Biol. Chem. , vol.261 , pp. 17057-17061
    • Suzuki, Y.1    Nagao, Y.2    Kato, H.3    Matsumoto, M.4    Nerome, K.5    Nakajima, K.6    Nobusawa, E.7
  • 30
    • 0027180538 scopus 로고
    • Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion
    • Tse, F. W., A. Iwata, and W. Almers. 1993. Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion. J. Cell Biol. 121:543-552.
    • (1993) J. Cell Biol. , vol.121 , pp. 543-552
    • Tse, F.W.1    Iwata, A.2    Almers, W.3
  • 31
    • 0030986975 scopus 로고    scopus 로고
    • Monovalent ion selectivity sequences of the rat connexin43 gap junction channel
    • Wang, H. Z., and R. D. Veenstra. 1997. Monovalent ion selectivity sequences of the rat connexin43 gap junction channel. J. Gen. Physiol. 109:491-507.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 491-507
    • Wang, H.Z.1    Veenstra, R.D.2
  • 32
    • 0028587209 scopus 로고
    • Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion
    • Zimmerberg, J., R. Blumenthal, D. P. Sarkar, M. Curran, and S. J. Morris. 1994. Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion. J. Cell Biol. 127:1885-1894.
    • (1994) J. Cell Biol. , vol.127 , pp. 1885-1894
    • Zimmerberg, J.1    Blumenthal, R.2    Sarkar, D.P.3    Curran, M.4    Morris, S.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.