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Volumn 235, Issue 2, 1997, Pages 201-208

How lysophosphatidylcholine inhibits cell-cell fusion mediated by the envelope glycoprotein of human immunodeficiency virus

Author keywords

[No Author keywords available]

Indexed keywords

LYSOPHOSPHATIDYLCHOLINE; VIRUS ENVELOPE PROTEIN;

EID: 0242316982     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.8699     Document Type: Article
Times cited : (32)

References (53)
  • 1
    • 0026434572 scopus 로고
    • Receptor-mediated activation of immunodeficiency viruses in viral fusion
    • Allan J. S. Receptor-mediated activation of immunodeficiency viruses in viral fusion. Science. 252:1991;1322.
    • (1991) Science , vol.252 , pp. 1322
    • Allan, J.S.1
  • 2
    • 0000007950 scopus 로고
    • The use of vectors based on gene amplification for the expression of cloned genes in mammalian cells
    • Oxford: IRL Press
    • Bebbington C. R., Hentschel C. C. G. The use of vectors based on gene amplification for the expression of cloned genes in mammalian cells. DNA Cloning. 1987;IRL Press, Oxford.
    • (1987) DNA Cloning
    • Bebbington, C.R.1    Hentschel, C.C.G.2
  • 4
    • 0026747863 scopus 로고
    • Association and metabolism of exogenously-derived lysophosphatidylcholine by cultured mammalian cells: Kinetics and mechanisms
    • Bestermann J. M., Domanico P. L. Association and metabolism of exogenously-derived lysophosphatidylcholine by cultured mammalian cells: Kinetics and mechanisms. Biochemistry. 31:1992;2046-2056.
    • (1992) Biochemistry , vol.31 , pp. 2046-2056
    • Bestermann, J.M.1    Domanico, P.L.2
  • 7
    • 0029148061 scopus 로고
    • The hemifusion intermediate and its conversion to complete fusion: Regulation by membrane composition
    • Chernomordik L. V., Chanturiya A., Green J., Zimmerberg J. The hemifusion intermediate and its conversion to complete fusion: Regulation by membrane composition. Biophys. J. 69:1995a;922-929.
    • (1995) Biophys. J. , vol.69 , pp. 922-929
    • Chernomordik, L.V.1    Chanturiya, A.2    Green, J.3    Zimmerberg, J.4
  • 10
    • 0028969738 scopus 로고
    • Control of baculovirus gp64-induced syncytium formation by membrane lipid composition
    • Chernomordik L. V., Leikina E. A., Cho M.-S., Zimmerberg J. Control of baculovirus gp64-induced syncytium formation by membrane lipid composition. J. Virol. 69:1995c;3049-3058.
    • (1995) J. Virol. , vol.69 , pp. 3049-3058
    • Chernomordik, L.V.1    Leikina, E.A.2    Cho, M.-S.3    Zimmerberg, J.4
  • 12
    • 0029144334 scopus 로고
    • Bending membranes to the task: Structural intermediates in bilayer fusion
    • Chernomordik L. V., Zimmerberg J. Bending membranes to the task: Structural intermediates in bilayer fusion. Curr. Opin. Struct. Biol. 5:1995;541-547.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 541-547
    • Chernomordik, L.V.1    Zimmerberg, J.2
  • 13
    • 0030041468 scopus 로고    scopus 로고
    • Structural study of the interaction between the SIV fusion peptide and model membranes
    • Colotto A., Martin I., Ruysschaert J.-M., Sen A., Hui S. W., Epand R. M. Structural study of the interaction between the SIV fusion peptide and model membranes. Biochemistry. 35:1996;980-999.
    • (1996) Biochemistry , vol.35 , pp. 980-999
    • Colotto, A.1    Martin, I.2    Ruysschaert, J.-M.3    Sen, A.4    Hui, S.W.5    Epand, R.M.6
  • 14
    • 0017341454 scopus 로고
    • Outside-inside distribution and translocation of lysophosphatidylcholine vesicles as determined by 13C-NMR using (N-13CH3)-enriched lipids
    • De Kruijff B., Van den Besselaar A. M. H. P., Van Deenen L. L. M. Outside-inside distribution and translocation of lysophosphatidylcholine vesicles as determined by 13C-NMR using (N-13CH3)-enriched lipids. Biochim. Biophys. Acta. 465:1977;443-453.
    • (1977) Biochim. Biophys. Acta , vol.465 , pp. 443-453
    • De Kruijff, B.1    Van Den Besselaar, A.M.H.P.2    Van Deenen, L.L.M.3
  • 15
    • 0021879568 scopus 로고
    • An efficient method for introducing macromolecules into living cells
    • Doxsey S., Sambrook J., Helenius A., White J. An efficient method for introducing macromolecules into living cells. J. Cell Biol. 101:1985;19-27.
    • (1985) J. Cell Biol. , vol.101 , pp. 19-27
    • Doxsey, S.1    Sambrook, J.2    Helenius, A.3    White, J.4
  • 16
    • 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. Biochemistry. 29:1990;9697-9707.
    • (1990) Biochemistry , vol.29 , pp. 9697-9707
    • Ellens, H.1    Bentz, J.2    Mason, D.3    Zhang, F.4    White, J.5
  • 17
    • 0024316282 scopus 로고
    • A syncytic assay for human immunodeficiency virus envelope protein and its use in studying HIV-1 mutations
    • Felser J. M., Klimkait T., Silver J. A syncytic assay for human immunodeficiency virus envelope protein and its use in studying HIV-1 mutations. Virology. 170:1989;566-570.
    • (1989) Virology , vol.170 , pp. 566-570
    • Felser, J.M.1    Klimkait, T.2    Silver, J.3
  • 18
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissues
    • Folch J., Lees M., Sloane-Stanley G. H. A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226:1957;497-509.
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane-Stanley, G.H.3
  • 19
    • 0028788472 scopus 로고
    • The role of human immunodeficiency virus type 1 envelope glycoprotein in virus infection
    • Freed E. O., Martin M. A. The role of human immunodeficiency virus type 1 envelope glycoprotein in virus infection. J. Biol. Chem. 270:1995;23883-23886.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23883-23886
    • Freed, E.O.1    Martin, M.A.2
  • 20
    • 0026785547 scopus 로고
    • Identification and characterization of fusion and processing domains of HIV-2 glycoprotein
    • Freed E. O., Myers D. J., Risser. Identification and characterization of fusion and processing domains of HIV-2 glycoprotein. J. Virol. 66:1992;5472-5478.
    • (1992) J. Virol. , vol.66 , pp. 5472-5478
    • Freed, E.O.1    Myers, D.J.2    Risser3
  • 21
    • 0025297179 scopus 로고
    • Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp 41
    • Freed E. O., Myers D. J., Risser R. Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp 41. Proc. Natl. Acad. Sci. USA. 87:1990;4650-4654.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4650-4654
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 22
    • 0028851288 scopus 로고
    • Temperature dependence of cell-cell fusion induced by the envelope glycoprotein of human immunodeficiency Virus-1
    • Frey S., Marsh M., Günther S., Pelchen-Matthews A., Stephens P., Ortlepp S., Stegmann T. Temperature dependence of cell-cell fusion induced by the envelope glycoprotein of human immunodeficiency Virus-1. J. Virol. 69:1995;1462-1472.
    • (1995) J. Virol. , vol.69 , pp. 1462-1472
    • Frey, S.1    Marsh, M.2    Günther, S.3    Pelchen-Matthews, A.4    Stephens, P.5    Ortlepp, S.6    Stegmann, T.7
  • 23
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus
    • Gallaher W. R. Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell. 50:1987;327-328.
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 24
    • 0028864309 scopus 로고
    • Inhibition of influenza-induced membrane fusion by lysophosphatidylcholine
    • Günther-Ausborn S., Praetor A., Stegmann T. Inhibition of influenza-induced membrane fusion by lysophosphatidylcholine. J. Biol. Chem. 270:1995;29279-29285.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29279-29285
    • Günther-Ausborn, S.1    Praetor, A.2    Stegmann, T.3
  • 25
    • 0029257245 scopus 로고
    • Structural characterization of viral fusion proteins
    • Hughson F. M. Structural characterization of viral fusion proteins. Curr. Biology. 5:1995;265-274.
    • (1995) Curr. Biology , vol.5 , pp. 265-274
    • Hughson, F.M.1
  • 26
    • 0025187179 scopus 로고
    • A non-exchangeable fluorescent phospholipid analog as a membrane traffic marker of the endocytic pathway
    • Kok J. W., ter Beest M., Scherphof G., Hoekstra D. A non-exchangeable fluorescent phospholipid analog as a membrane traffic marker of the endocytic pathway. Eur. J. Cell Biol. 53:1990;173-184.
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 173-184
    • Kok, J.W.1    Ter Beest, M.2    Scherphof, G.3    Hoekstra, D.4
  • 28
    • 0026057849 scopus 로고
    • Complementary molecular shapes and additivity of the packing parameter of lipids
    • Kumar V. V. Complementary molecular shapes and additivity of the packing parameter of lipids. Proc. Natl. Acad. Sci. USA. 88:1991;444-448.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 444-448
    • Kumar, V.V.1
  • 29
    • 0029805881 scopus 로고    scopus 로고
    • Evidence for cell-surface association between fusin and the CD4-gp120 complex in human cell lines
    • Lapham C. K., Ouyang J., Chandrasekhar B., Nguyen N. Y., Dimitrov D. S., Golding H. Evidence for cell-surface association between fusin and the CD4-gp120 complex in human cell lines. Science. 274:1996;602-605.
    • (1996) Science , vol.274 , pp. 602-605
    • Lapham, C.K.1    Ouyang, J.2    Chandrasekhar, B.3    Nguyen, N.Y.4    Dimitrov, D.S.5    Golding, H.6
  • 30
    • 0342434132 scopus 로고
    • Membrane fusion induced by the HIV env glycoprotein
    • R.C. Aloia, C.C. Curtain, & L.L. Gordon. New York: Wiley-Liss
    • Larsen C., Ellens H., Bentz J. Membrane fusion induced by the HIV env glycoprotein. Aloia R. C., Curtain C. C., Gordon L. L. Advances in Membrane Fluidity. 1992;143-156 Wiley-Liss, New York.
    • (1992) Advances in Membrane Fluidity , pp. 143-156
    • Larsen, C.1    Ellens, H.2    Bentz, J.3
  • 31
    • 0027367886 scopus 로고
    • Lysophosphatidylcholine mediates the mode of insertion of the NH2-terminal SIV fusion peptide into the lipid bilayer
    • Martin I., Dubois M.-C., Saermark T., Epand R. M., Ruysschaert J. M. Lysophosphatidylcholine mediates the mode of insertion of the NH2-terminal SIV fusion peptide into the lipid bilayer. FEBS Lett. 333:1993;325-330.
    • (1993) FEBS Lett. , vol.333 , pp. 325-330
    • Martin, I.1    Dubois, M.-C.2    Saermark, T.3    Epand, R.M.4    Ruysschaert, J.M.5
  • 32
    • 0028882377 scopus 로고
    • Lysophosphatidylcholine inhibits vesicles fusion induced by the NH2-terminal extremity of SIV/HIV fusogenic proteins
    • Martin I., Ruysschaert J. M. Lysophosphatidylcholine inhibits vesicles fusion induced by the NH2-terminal extremity of SIV/HIV fusogenic proteins. Biochim. Biophys. Acta. 1240:1995;95-100.
    • (1995) Biochim. Biophys. Acta , vol.1240 , pp. 95-100
    • Martin, I.1    Ruysschaert, J.M.2
  • 33
    • 0029655419 scopus 로고    scopus 로고
    • Lipid membrane fusion induced by the human immunodeficieny virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer
    • Martin I., Schaal H., Scheid A., Ruysschaert J. M. Lipid membrane fusion induced by the human immunodeficieny virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer. J. Virol. 70:1996;298-304.
    • (1996) J. Virol. , vol.70 , pp. 298-304
    • Martin, I.1    Schaal, H.2    Scheid, A.3    Ruysschaert, J.M.4
  • 35
    • 0026434572 scopus 로고
    • Receptor-mediated activation of immunodeficiency viruses in viral fusion
    • Moore J. P., McKeating J. A., Weiss R., Clapham P. R., Sattentau Q. Receptor-mediated activation of immunodeficiency viruses in viral fusion. Science. 252:1991;1322-1323.
    • (1991) Science , vol.252 , pp. 1322-1323
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.3    Clapham, P.R.4    Sattentau, Q.5
  • 36
    • 0028824903 scopus 로고
    • Role of CD4 endocytosis in human immunodeficiency virus infection
    • Pelchen-Matthews A., Clapham P., Marsh M. Role of CD4 endocytosis in human immunodeficiency virus infection. J. Virol. 69:1995;8164-8168.
    • (1995) J. Virol. , vol.69 , pp. 8164-8168
    • Pelchen-Matthews, A.1    Clapham, P.2    Marsh, M.3
  • 37
    • 0023230264 scopus 로고
    • The activation of porcine pancreas phospholipase A2 by dipalmitoylphosphatidylcholine large unilamellar vesicles
    • Romero G., Thompson K., Biltonen R. L. The activation of porcine pancreas phospholipase A2 by dipalmitoylphosphatidylcholine large unilamellar vesicles. J. Biol. Chem. 262:1987;13476-13482.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13476-13482
    • Romero, G.1    Thompson, K.2    Biltonen, R.L.3
  • 38
    • 0028801450 scopus 로고
    • Epitope exposure on functional, oligomeric HIV-1 gp41 molecules
    • Sattentau Q., Zolla-Pazner S., Poignard P. Epitope exposure on functional, oligomeric HIV-1 gp41 molecules. Virology. 206:1995;713-717.
    • (1995) Virology , vol.206 , pp. 713-717
    • Sattentau, Q.1    Zolla-Pazner, S.2    Poignard, P.3
  • 39
    • 0029918812 scopus 로고    scopus 로고
    • Influenza-virus lipid mixing is leaky and largely insensitive to the material properties of the target membrane
    • Shangguan T., Alford D., Bentz J. Influenza-virus lipid mixing is leaky and largely insensitive to the material properties of the target membrane. Biochemistry. 35:1996;4956-4965.
    • (1996) Biochemistry , vol.35 , pp. 4956-4965
    • Shangguan, T.1    Alford, D.2    Bentz, J.3
  • 40
    • 0027362739 scopus 로고
    • Energetics of intermediates in membrane fusion: Comparison of stalk and inverted micellar intermediate mechanisms
    • Siegel D. P. Energetics of intermediates in membrane fusion: Comparison of stalk and inverted micellar intermediate mechanisms. Biophys. J. 65:1993a;2124-2140.
    • (1993) Biophys. J. , vol.65 , pp. 2124-2140
    • Siegel, D.P.1
  • 41
    • 0001835372 scopus 로고
    • Modeling protein-induced fusion: Insights from the relative stability of lipidic structures
    • J. Bentz. Boca Raton: CRC Press
    • Siegel D. P. Modeling protein-induced fusion: Insights from the relative stability of lipidic structures. Bentz J. Viral Fusion Mechanisms. 1993b;475-512 CRC Press, Boca Raton.
    • (1993) Viral Fusion Mechanisms , pp. 475-512
    • Siegel, D.P.1
  • 42
    • 0026735967 scopus 로고
    • Role of the fusogenic peptide sequence in syncytium formation and infectivity of human immunodeficiency type 2 virus
    • Steffy K. R., Kraus G., Looney D. J., Wong-Staal F. Role of the fusogenic peptide sequence in syncytium formation and infectivity of human immunodeficiency type 2 virus. J. Virol. 66:1992;4532-4535.
    • (1992) J. Virol. , vol.66 , pp. 4532-4535
    • Steffy, K.R.1    Kraus, G.2    Looney, D.J.3    Wong-Staal, F.4
  • 43
    • 0026062948 scopus 로고
    • The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion
    • Stegmann T., Delfino J. M., Richards F. M., Helenius A. The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion. J. Biol. Chem. 266:1991;18404-18410.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18404-18410
    • Stegmann, T.1    Delfino, J.M.2    Richards, F.M.3    Helenius, A.4
  • 45
    • 0024445907 scopus 로고
    • The construction of a highly efficient and versatile set of mammalian expression vectors
    • Stephens P. E., Cockett M. I. The construction of a highly efficient and versatile set of mammalian expression vectors. Nucleic Acids Res. 17:1989;7110.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 7110
    • Stephens, P.E.1    Cockett, M.I.2
  • 47
    • 0026705651 scopus 로고
    • Mechanism of influenza induced-membrane fusion: Membrane insertion of the "fusion peptide" of hemagglutinin
    • Tsurudome M., Glück R., Graf R., Falchetto R., Schaller U., Brunner J. Mechanism of influenza induced-membrane fusion: Membrane insertion of the "fusion peptide" of hemagglutinin. J. Biol. Chem. 267:1992;20225-20232.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20225-20232
    • Tsurudome, M.1    Glück, R.2    Graf, R.3    Falchetto, R.4    Schaller, U.5    Brunner, J.6
  • 48
    • 0027441876 scopus 로고
    • Lysophosphatidylcholine reversibly arrests exocytosis and viral fusion at a stage between triggering and membrane merger
    • Vogel S. S., Leikina E. A., Chernomordik L. V. Lysophosphatidylcholine reversibly arrests exocytosis and viral fusion at a stage between triggering and membrane merger. J. Biol. Chem. 268:1993;25764-25768.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25764-25768
    • Vogel, S.S.1    Leikina, E.A.2    Chernomordik, L.V.3
  • 49
    • 0018797112 scopus 로고
    • Cytolytic and membrane-perturbing properties of lysophospatidylcholine
    • Weltzien H. U. Cytolytic and membrane-perturbing properties of lysophospatidylcholine. Biochim. Biophys. Acta. 559:1979;259-287.
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 259-287
    • Weltzien, H.U.1
  • 50
    • 0019870337 scopus 로고
    • Cell fusion by Semliki Forest, influenza and vesicular stomatitis viruses
    • White J., Matlin K., Helenius A. Cell fusion by Semliki Forest, influenza and vesicular stomatitis viruses. J. Cell Biol. 89:1981;674-679.
    • (1981) J. Cell Biol. , vol.89 , pp. 674-679
    • White, J.1    Matlin, K.2    Helenius, A.3
  • 51
    • 0022468229 scopus 로고
    • Membrane fusion: Lipid vesicles as a model system
    • Wilschut J., Hoekstra D. Membrane fusion: Lipid vesicles as a model system. Chem. Phys. Lipids. 40:1986;145-166.
    • (1986) Chem. Phys. Lipids , vol.40 , pp. 145-166
    • Wilschut, J.1    Hoekstra, D.2
  • 53
    • 0028271679 scopus 로고
    • Inhibition of membrane fusion by lysophosphatidylcholine
    • Yeagle P. L., Smith F. T., Young J. E., Flanagan T. D. Inhibition of membrane fusion by lysophosphatidylcholine. Biochemistry. 33:1994;1820-1827.
    • (1994) Biochemistry , vol.33 , pp. 1820-1827
    • Yeagle, P.L.1    Smith, F.T.2    Young, J.E.3    Flanagan, T.D.4


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