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Volumn 78, Issue 1, 2004, Pages 473-481

A Point Mutation in the Binding Subunit of a Retroviral Envelope Protein Arrests Virus Entry at Hemifusion

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CHLORPROMAZINE; CINCHOCAINE; HISTIDINE; HYBRID PROTEIN; MEMBRANE PROTEIN; PROTEIN SUBUNIT; TRIFLUOPERAZINE; VIRUS ENVELOPE PROTEIN;

EID: 0346365290     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.1.473-481.2004     Document Type: Article
Times cited : (34)

References (42)
  • 1
    • 0028801976 scopus 로고
    • Infection by retroviral vectors outside of their host range in the presence of replication-defective adenovirus
    • Adams, R. M., M. Wang, D. Steffen, and F. D. Ledley. 1995. Infection by retroviral vectors outside of their host range in the presence of replication-defective adenovirus. J. Virol. 69:1887-1894.
    • (1995) J. Virol. , vol.69 , pp. 1887-1894
    • Adams, R.M.1    Wang, M.2    Steffen, D.3    Ledley, F.D.4
  • 2
    • 0034676041 scopus 로고    scopus 로고
    • The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition
    • Armstrong, R. T., A. S. Kushnir, and J. M. White. 2000. The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition. J. Cell Biol. 151:425-437.
    • (2000) J. Cell Biol. , vol.151 , pp. 425-437
    • Armstrong, R.T.1    Kushnir, A.S.2    White, J.M.3
  • 4
    • 0031058044 scopus 로고    scopus 로고
    • Functional dissection of the Moloney murine leukemia virus envelope protein gp70
    • Bae, Y., S. M. Kingsman, and A. J. Kingsman. 1997. Functional dissection of the Moloney murine leukemia virus envelope protein gp70. J. Virol. 71:2092-2099.
    • (1997) J. Virol. , vol.71 , pp. 2092-2099
    • Bae, Y.1    Kingsman, S.M.2    Kingsman, A.J.3
  • 5
    • 0031585569 scopus 로고    scopus 로고
    • A glycine to alanine substitution in the paramyxovirus SV5 fusion peptide increases the initial rate of fusion
    • Bagai, S., and R. A. Lamb. 1997. A glycine to alanine substitution in the paramyxovirus SV5 fusion peptide increases the initial rate of fusion. Virology 238:283-290.
    • (1997) Virology , vol.238 , pp. 283-290
    • Bagai, S.1    Lamb, R.A.2
  • 6
    • 0029819165 scopus 로고    scopus 로고
    • Truncation of the COOH-terminal region of the paramyxovirus SV5 fusion protein leads to hemifusion but not complete fusion
    • Bagai, S., and R. A. Lamb. 1996. Truncation of the COOH-terminal region of the paramyxovirus SV5 fusion protein leads to hemifusion but not complete fusion. J. Cell Biol. 135:73-84.
    • (1996) J. Cell Biol. , vol.135 , pp. 73-84
    • Bagai, S.1    Lamb, R.A.2
  • 7
    • 0035957377 scopus 로고    scopus 로고
    • Modular organization of the Friend murine leukemia virus envelope protein underlies the mechanism of infection
    • Barnett, A. L., R. A. Davey, and J. M. Cunningham. 2001. Modular organization of the Friend murine leukemia virus envelope protein underlies the mechanism of infection. Proc. Natl. Acad. Sci. USA 98:4113-4118.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4113-4118
    • Barnett, A.L.1    Davey, R.A.2    Cunningham, J.M.3
  • 8
    • 0026608630 scopus 로고
    • Receptor choice determinants in the envelope glycoproteins of amphotropic, xenotropic, and polytropic murine leukemia viruses
    • Battini, J. L., J. M. Heard, and O. Danos. 1992. Receptor choice determinants in the envelope glycoproteins of amphotropic, xenotropic, and polytropic murine leukemia viruses. J. Virol. 66:1468-1475.
    • (1992) J. Virol. , vol.66 , pp. 1468-1475
    • Battini, J.L.1    Heard, J.M.2    Danos, O.3
  • 9
    • 0023645644 scopus 로고
    • pH-dependent fusion of vesicular stomatitis virus with Vero cells. Measurement by dequenching of octadecyl rhodamine fluorescence
    • Erratum, 263:588, 1988
    • Blumenthal, R., A. Bali-Puri, A. Walter, D. Covell, and O. Eidelman. 1987. pH-dependent fusion of vesicular stomatitis virus with Vero cells. Measurement by dequenching of octadecyl rhodamine fluorescence. J. Biol. Chem. 262:13614-13619. (Erratum, 263:588, 1988.)
    • (1987) J. Biol. Chem. , vol.262 , pp. 13614-13619
    • Blumenthal, R.1    Bali-Puri, A.2    Walter, A.3    Covell, D.4    Eidelman, O.5
  • 10
    • 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
  • 11
    • 0032584146 scopus 로고    scopus 로고
    • The transmembrane domain in viral fusion: Essential role for a conserved glycine residue in vesicular stomatitis virus G protein
    • Cleverley, D. Z., and J. Lenard. 1998. The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein. Proc. Natl. Acad. Sci. USA 95:3425-3430.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3425-3430
    • Cleverley, D.Z.1    Lenard, J.2
  • 12
    • 0026582099 scopus 로고
    • Correlation between kinetics of soluble CD4 interactions with HIV-1-Env-expressing cells and inhibition of syncytia formation: Implications for mechanisms of cell fusion and therapy for AIDS
    • Dimitrov, D. S., K. Hillman, J. Manischewitz, R. Blumenthal, and H. Golding. 1992. Correlation between kinetics of soluble CD4 interactions with HIV-1-Env-expressing cells and inhibition of syncytia formation: implications for mechanisms of cell fusion and therapy for AIDS. AIDS 6:249-256.
    • (1992) AIDS , vol.6 , pp. 249-256
    • Dimitrov, D.S.1    Hillman, K.2    Manischewitz, J.3    Blumenthal, R.4    Golding, H.5
  • 13
    • 0036227316 scopus 로고    scopus 로고
    • Fusion-defective gibbon ape leukemia virus vectors can be rescued by homologous but not heterologous soluble envelope proteins
    • Farrell, K. B., Y. T. Ting, and M. V. Eiden. 2002. Fusion-defective gibbon ape leukemia virus vectors can be rescued by homologous but not heterologous soluble envelope proteins. J. Virol. 76:4267-4274.
    • (2002) J. Virol. , vol.76 , pp. 4267-4274
    • Farrell, K.B.1    Ting, Y.T.2    Eiden, M.V.3
  • 14
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng, Y., C. C. Broder, P. E. Kennedy, and E. A. Berger. 1996. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272:872-877.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 15
    • 0022619527 scopus 로고
    • Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus
    • Gething, M. J., R. W. Doms, D. York, and J. White. 1986. Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus. J. Cell Biol. 102:11-23.
    • (1986) J. Cell Biol. , vol.102 , pp. 11-23
    • Gething, M.J.1    Doms, R.W.2    York, D.3    White, J.4
  • 16
    • 0025093305 scopus 로고
    • Fusion of Rous sarcoma virus with host cells does not require exposure to low pH
    • Gilbert, J. M., D. Mason, and J. M. White. 1990. Fusion of Rous sarcoma virus with host cells does not require exposure to low pH. J. Virol. 64:5106-5113.
    • (1990) J. Virol. , vol.64 , pp. 5106-5113
    • Gilbert, J.M.1    Mason, D.2    White, J.M.3
  • 17
    • 0026011315 scopus 로고
    • Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120
    • Hart, T. K., R. Kirsh, H. Ellens, R. W. Sweet, D. M. Lambert, S. R. J. Petteway, J. Leary, and P. J. Bugelski. 1991. Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120. Proc. Natl. Acad. Sci. USA 88:2189-2193.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2189-2193
    • Hart, T.K.1    Kirsh, R.2    Ellens, H.3    Sweet, R.W.4    Lambert, D.M.5    Petteway, S.R.J.6    Leary, J.7    Bugelski, P.J.8
  • 18
    • 0019781006 scopus 로고
    • Influence of local and neutral anaesthetics on the polymorphic phase preferences of egg yolk phosphatidylethanolamine
    • Hornby, A. P., and P. R. Cullis. 1981. Influence of local and neutral anaesthetics on the polymorphic phase preferences of egg yolk phosphatidylethanolamine. Biochim. Biophys. Acta 647:285-292.
    • (1981) Biochim. Biophys. Acta , vol.647 , pp. 285-292
    • Hornby, A.P.1    Cullis, P.R.2
  • 19
    • 0029090984 scopus 로고
    • Fatty acid flip-flop in phospholipid bilayers is extremely fast
    • Kamp, F., D. Zakim, F. Zhang, N. Noy, and J. A. Hamilton. 1995. Fatty acid flip-flop in phospholipid bilayers is extremely fast. Biochemistry 34:11928-11937.
    • (1995) Biochemistry , vol.34 , pp. 11928-11937
    • Kamp, F.1    Zakim, D.2    Zhang, F.3    Noy, N.4    Hamilton, J.A.5
  • 20
    • 0026772024 scopus 로고
    • Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin
    • Kemble, G. W., D. L. Bodian, J. Rose, I. A. Wilson, and J. M. White. 1992. Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin. J. Virol. 66:4940-4950.
    • (1992) J. Virol. , vol.66 , pp. 4940-4950
    • Kemble, G.W.1    Bodian, D.L.2    Rose, J.3    Wilson, I.A.4    White, J.M.5
  • 21
    • 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
  • 22
    • 0001171130 scopus 로고
    • Possible mechanism of membrane fusion
    • Koslov, M. M., and V. S. Markin. 1983. Possible mechanism of membrane fusion. Biofizika 28:255-261.
    • (1983) Biofizika , vol.28 , pp. 255-261
    • Koslov, M.M.1    Markin, V.S.2
  • 23
    • 0033987002 scopus 로고    scopus 로고
    • Activation of a cell entry pathway common to type C mammalian retroviruses by soluble envelope fragments
    • Lavillette, D., A. Ruggieri, S. J. Russell, and F. L. Cosset. 2000. Activation of a cell entry pathway common to type C mammalian retroviruses by soluble envelope fragments. J. Virol. 74:295-304.
    • (2000) J. Virol. , vol.74 , pp. 295-304
    • Lavillette, D.1    Ruggieri, A.2    Russell, S.J.3    Cosset, F.L.4
  • 24
    • 0029656201 scopus 로고    scopus 로고
    • Analysis of the murine ecotropic leukemia virus receptor reveals a common biochemical determinant on diverse cell surface receptors that is essential to retrovirus entry
    • Malhotra, S., A. G. Scott, T. Zavorotinskaya, and L. M. Albritton. 1996. Analysis of the murine ecotropic leukemia virus receptor reveals a common biochemical determinant on diverse cell surface receptors that is essential to retrovirus entry. J. Virol. 70:321-326.
    • (1996) J. Virol. , vol.70 , pp. 321-326
    • Malhotra, S.1    Scott, A.G.2    Zavorotinskaya, T.3    Albritton, L.M.4
  • 25
    • 0034037991 scopus 로고    scopus 로고
    • The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores
    • Markosyan, R. M., F. S. Cohen, and G. B. Melikyan. 2000. The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores. Mol. Biol. Cell 11:1143-1152.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1143-1152
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 26
    • 0030899232 scopus 로고    scopus 로고
    • Inner but not outer membrane leaflets control the transition from glycosylphosphatidylinositol-anchored influenza hemagglutinin-induced hemifusion to full fusion
    • Melikyan, G. B., S. A. Brener, D. C. Ok, and F. S. Cohen. 1997. Inner but not outer membrane leaflets control the transition from glycosylphosphatidylinositol-anchored influenza hemagglutinin-induced hemifusion to full fusion. J. Cell Biol. 136:995-1005.
    • (1997) J. Cell Biol. , vol.136 , pp. 995-1005
    • Melikyan, G.B.1    Brener, S.A.2    Ok, D.C.3    Cohen, F.S.4
  • 27
    • 0033988562 scopus 로고    scopus 로고
    • Role of the cytoplasmic tail of ecotropic Moloney murine leukemia virus Env protein in fusion pore formation
    • Melikyan, G. B., R. M. Markosyan, S. A. Brener, Y. Rozenberg, and F. S. Cohen. 2000. Role of the cytoplasmic tail of ecotropic Moloney murine leukemia virus Env protein in fusion pore formation. J. Virol. 74:447-455.
    • (2000) J. Virol. , vol.74 , pp. 447-455
    • Melikyan, G.B.1    Markosyan, R.M.2    Brener, S.A.3    Rozenberg, Y.4    Cohen, F.S.5
  • 28
    • 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. 1995. 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
  • 29
    • 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
  • 30
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 virions induced by soluble CD4
    • Moore, J. P., J. A. McKeating, R. A. Weiss, and Q. J. Sattentau. 1990. Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 250:1139-1142.
    • (1990) Science , vol.250 , pp. 1139-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 31
    • 0032546590 scopus 로고    scopus 로고
    • Probe transfer with or without membrane fusion in a fluorescence fusion assay
    • Ohki, S., T. D. Flanagan, and D. Hoekstra. 1998. Probe transfer with or without membrane fusion in a fluorescence fusion assay. Biochemistry 37:7496-7503.
    • (1998) Biochemistry , vol.37 , pp. 7496-7503
    • Ohki, S.1    Flanagan, T.D.2    Hoekstra, D.3
  • 33
    • 0032812477 scopus 로고    scopus 로고
    • A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion 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 hemifusion 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
  • 34
    • 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
  • 35
    • 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
  • 36
    • 0001718634 scopus 로고
    • Biological membranes as bilayer couples: A molecular mechanism of drug-erythrocyte interactions
    • Sheetz, M. P., and S. J. Singer. 1974. Biological membranes as bilayer couples: a molecular mechanism of drug-erythrocyte interactions. Proc. Natl. Acad. Sci. USA 71:4457-4461.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4457-4461
    • Sheetz, M.P.1    Singer, S.J.2
  • 37
    • 0023737388 scopus 로고
    • Quantitative measurement of fusion between human immunodeficiency virus and cultured cells using membrane fluorescence dequenching
    • Sinangil, F., A. Loyter, and D. J. Volsky. 1988. Quantitative measurement of fusion between human immunodeficiency virus and cultured cells using membrane fluorescence dequenching. FEBS Lett. 239:88-92.
    • (1988) FEBS Lett. , vol.239 , pp. 88-92
    • Sinangil, F.1    Loyter, A.2    Volsky, D.J.3
  • 38
    • 0027434098 scopus 로고
    • Evaluation of viral membrane fusion assays. Comparison of the octadecylrhodamine dequenching assay with the pyrene excimer assay
    • Stegmann, T., P. Schoen, R. Bron, J. Wey, I. Bartoldus, A. Ortiz, J. Nieva, and J. Wilschut. 1993. Evaluation of viral membrane fusion assays. Comparison of the octadecylrhodamine dequenching assay with the pyrene excimer assay. Biochemistry 32:11330-11337.
    • (1993) Biochemistry , vol.32 , pp. 11330-11337
    • Stegmann, T.1    Schoen, P.2    Bron, R.3    Wey, J.4    Bartoldus, I.5    Ortiz, A.6    Nieva, J.7    Wilschut, J.8
  • 39
    • 0029864284 scopus 로고    scopus 로고
    • Studies of HIV-1 envelope glycoprotein-mediated fusion using a simple fluorescence assay
    • Weiss, C. D., S. W. Barnett, N. Cacalano, N. Killeen, D. R. Littman, and J. M. White. 1996. Studies of HIV-1 envelope glycoprotein-mediated fusion using a simple fluorescence assay. AIDS 10:241-246.
    • (1996) AIDS , vol.10 , pp. 241-246
    • Weiss, C.D.1    Barnett, S.W.2    Cacalano, N.3    Killeen, N.4    Littman, D.R.5    White, J.M.6
  • 40
    • 0031060516 scopus 로고    scopus 로고
    • Fusion of bovine leukemia virus with target cells monitored by R18 fluorescence and PCR assays
    • Zarkik, S., F. Defrise-Quertain, D. Portetelle, A. Burny, and J. M. Ruysschaert. 1997. Fusion of bovine leukemia virus with target cells monitored by R18 fluorescence and PCR assays. J. Virol. 71:738-740.
    • (1997) J. Virol. , vol.71 , pp. 738-740
    • Zarkik, S.1    Defrise-Quertain, F.2    Portetelle, D.3    Burny, A.4    Ruysschaert, J.M.5
  • 41
    • 0033033072 scopus 로고    scopus 로고
    • Suppression of a fusion defect by second site mutations in the ecotropic murine leukemia virus surface protein
    • Zavorotinskaya, T., and L. M. Albritton. 1999. Suppression of a fusion defect by second site mutations in the ecotropic murine leukemia virus surface protein. J. Virol. 73:5034-5042.
    • (1999) J. Virol. , vol.73 , pp. 5034-5042
    • Zavorotinskaya, T.1    Albritton, L.M.2
  • 42
    • 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


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