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Volumn 73, Issue 4, 1997, Pages 1977-1986

Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: Dose and sequence effects

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; HYBRID PROTEIN; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; VIRUS PROTEIN;

EID: 0342506479     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78228-6     Document Type: Article
Times cited : (133)

References (52)
  • 2
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • Aloia, R. C., H. R. Tian, and F. C. Jensen. 1993. Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc. Natl. Acad. Sci. USA. 90:5181-5185.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.R.2    Jensen, F.C.3
  • 3
    • 0027987495 scopus 로고
    • Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy
    • Arrondo, J. L. R., J. Castresana, J. M. Valpuesta, and F. M. Goñi. 1994. Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy. Biochemistry. 33:11650-11655.
    • (1994) Biochemistry , vol.33 , pp. 11650-11655
    • Arrondo, J.L.R.1    Castresana, J.2    Valpuesta, J.M.3    Goñi, F.M.4
  • 4
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transformed infrared spectroscopy
    • Arrondo, J. L. R., A. Muga, J. Castresana, and F. M. Goñi. 1993. Quantitative studies of the structure of proteins in solution by Fourier-transformed infrared spectroscopy. Prog. Biophys. Mol. Biol. 59:23-56.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3    Goñi, F.M.4
  • 5
    • 0013582272 scopus 로고    scopus 로고
    • Calcium-induced conformational changes of E. coli α-haemolysin. Implications for the mechanism of membrane insertion and lysis
    • in press
    • Bakás, L., M. P. Veiga, A. Soloaga, H. Ostolaza, and F. M. Goñi. 1997. Calcium-induced conformational changes of E. coli α-haemolysin. Implications for the mechanism of membrane insertion and lysis. Biochim. Biophys. Acta. (in press).
    • (1997) Biochim. Biophys. Acta
    • Bakás, L.1    Veiga, M.P.2    Soloaga, A.3    Ostolaza, H.4    Goñi, F.M.5
  • 6
    • 0029591840 scopus 로고
    • Binding of molten globule-like conformations to lipid bilayers. Structure of native and partially folded α-lactalbumin bound to model membranes
    • Bañuelos, S., and A. Muga. 1995. Binding of molten globule-like conformations to lipid bilayers. Structure of native and partially folded α-lactalbumin bound to model membranes. J. Biol. Chem. 270: 29910-29915.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29910-29915
    • Bañuelos, S.1    Muga, A.2
  • 7
    • 0038259804 scopus 로고    scopus 로고
    • Interaction of native and partially folded α-lactalbumin with lipid bilayers: Characterization of two membrane-bound states
    • Bañuelos, S., and A. Muga. 1996. Interaction of native and partially folded α-lactalbumin with lipid bilayers: characterization of two membrane-bound states. FEBS Lett. 386:21-25.
    • (1996) FEBS Lett. , vol.386 , pp. 21-25
    • Bañuelos, S.1    Muga, A.2
  • 9
    • 50549164858 scopus 로고
    • A rapid, and sensitive sub-micro phosphorus determination
    • Böttcher, C. S. F., C. M. van Gent, and C. Fries. 1961. A rapid, and sensitive sub-micro phosphorus determination. Anal. Chim. Acta. 24: 203-204.
    • (1961) Anal. Chim. Acta , vol.24 , pp. 203-204
    • Böttcher, C.S.F.1    Van Gent, C.M.2    Fries, C.3
  • 10
    • 0029766187 scopus 로고    scopus 로고
    • Folding proteins into membranes
    • Deber, C. M., and N. K. Goto. 1996. Folding proteins into membranes. Nature Struct. Biol. 3:815-818.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 815-818
    • Deber, C.M.1    Goto, N.K.2
  • 12
    • 0021890825 scopus 로고
    • 2+-induced fusion and destabilization of liposomes
    • 2+-induced fusion and destabilization of liposomes. Biochemistry. 24:3099-3106.
    • (1985) Biochemistry , vol.24 , pp. 3099-3106
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.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
    • 0026544416 scopus 로고
    • A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity
    • Freed, E. O., E. L. Delwart, G. L. Buchschacher, and A. T. Panganiban. 1992. A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity. Proc. Natl. Acad. Sci. USA. 89:70-74.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 70-74
    • Freed, E.O.1    Delwart, E.L.2    Buchschacher, G.L.3    Panganiban, A.T.4
  • 16
    • 0025297179 scopus 로고
    • Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41
    • Freed, E. O., D. J. Myers, and R. Risser. 1990. Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41. Proc. Natl. Acad. Sci. USA. 87:4650-4654.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4650-4654
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 17
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of the human immunodeficiency virus
    • Gallaher, W. R. 1987. Detection of a fusion peptide sequence in the transmembrane protein of the human immunodeficiency virus. Cell. 50:327-328.
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 18
    • 0026758352 scopus 로고
    • Are fusion peptides really sided insertional helices?
    • Gallaher, W. R., J. P. Segrest, and E. Hunter. 1992. Are fusion peptides really sided insertional helices? Cell. 70:531-532.
    • (1992) Cell , vol.70 , pp. 531-532
    • Gallaher, W.R.1    Segrest, J.P.2    Hunter, E.3
  • 19
    • 0026743982 scopus 로고
    • The amino terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: Peptide conformation, orientation and aggregation
    • Gordon, L. M., C. C. Curtain, Y. C. Zhong, A. Kirkpatrick, P. W. Mobley, and A. J. Waring. 1992. The amino terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: peptide conformation, orientation and aggregation. Biochim. Biophys. Acta. 1139: 257-274.
    • (1992) Biochim. Biophys. Acta , vol.1139 , pp. 257-274
    • Gordon, L.M.1    Curtain, C.C.2    Zhong, Y.C.3    Kirkpatrick, A.4    Mobley, P.W.5    Waring, A.J.6
  • 20
    • 0030012221 scopus 로고    scopus 로고
    • Effect of the N-terminal glycine on the secondary structure, orientation and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers
    • Gray, C., S. A. Tatulian, S. A. Wharton, and L. K. Tamm. 1996. Effect of the N-terminal glycine on the secondary structure, orientation and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers. Biophys. J. 70:2275-2286.
    • (1996) Biophys. J. , vol.70 , pp. 2275-2286
    • Gray, C.1    Tatulian, S.A.2    Wharton, S.A.3    Tamm, L.K.4
  • 21
    • 0024564217 scopus 로고
    • Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide."
    • Harter, C., P. James, T. Bächi, G. Semenza, and J. Brunner. 1989. Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide." J. Biol. Chem. 264: 6459-6454.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6459-16454
    • Harter, C.1    James, P.2    Bächi, T.3    Semenza, G.4    Brunner, J.5
  • 23
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential
    • Hope, M. J., M. B. Bally, G. Webb, and P. R. Cullis. 1985. Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential. Biochim. Biophys. Acta. 812:55-65.
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 24
    • 0026337666 scopus 로고
    • A peptide corresponding to an export-detective mutant OmpA signal sequence with asparagine in the hydrophobic core is unable to insert into model membranes
    • Hoyt, D. W., and L. M. Gierasch. 1991. A peptide corresponding to an export-detective mutant OmpA signal sequence with asparagine in the hydrophobic core is unable to insert into model membranes. J. Biol. Chem. 266:14406-14412.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14406-14412
    • Hoyt, D.W.1    Gierasch, L.M.2
  • 25
    • 0028142681 scopus 로고
    • Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB protein
    • Jones, J. D., and L. M. Gierasch. 1994. Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB protein. Biophys. J. 67:1534-1545.
    • (1994) Biophys. J. , vol.67 , pp. 1534-1545
    • Jones, J.D.1    Gierasch, L.M.2
  • 28
    • 0027327036 scopus 로고
    • Effect of salts on conformational change of basic amphipathic peptides from β-structure to α-helix in the presence of phospholipid liposomes and their channel-forming ability
    • Lee, S., T. Iwata, H. Oyagi, H. Aoyagi, M. Ohno, K. Anzai, Y. Kirino, and G. Sugihara. 1993. Effect of salts on conformational change of basic amphipathic peptides from β-structure to α-helix in the presence of phospholipid liposomes and their channel-forming ability. Biochim. Biophys. Acta. 1151:76-82.
    • (1993) Biochim. Biophys. Acta , vol.1151 , pp. 76-82
    • Lee, S.1    Iwata, T.2    Oyagi, H.3    Aoyagi, H.4    Ohno, M.5    Anzai, K.6    Kirino, Y.7    Sugihara, G.8
  • 29
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., S. C. Blacklow, and P. S. Kim. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Struct. Biol. 2: 1075-1082.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 30
    • 0028840940 scopus 로고
    • Structure and topology of influenza virus fusion peptide in lipid bilayers
    • Lüneberg, J., I. Martin, F. Nüssler, J. M. Ruysschaert, and A. Herrman. 1995. Structure and topology of influenza virus fusion peptide in lipid bilayers. J. Biol. Chem. 270:27606-27614.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27606-27614
    • Lüneberg, J.1    Martin, I.2    Nüssler, F.3    Ruysschaert, J.M.4    Herrman, A.5
  • 33
    • 0028293970 scopus 로고
    • Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion
    • Muga, A., W. Neugebauer, T. Hirama, and W. K. Surewicz. 1994. Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion. Biochemistry. 33:4444-4448.
    • (1994) Biochemistry , vol.33 , pp. 4444-4448
    • Muga, A.1    Neugebauer, W.2    Hirama, T.3    Surewicz, W.K.4
  • 34
    • 0028218423 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for leakage and fusion
    • Nieva, J. L., S. Nir, A. Muga, F. M. Goñi, and J. Wilschut. 1994. Interaction of the HIV-1 fusion peptide with phospholipid vesicles: different structural requirements for leakage and fusion. Biochemistry. 33:3201-3209.
    • (1994) Biochemistry , vol.33 , pp. 3201-3209
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goñi, F.M.4    Wilschut, J.5
  • 35
    • 0024284763 scopus 로고
    • Pyrene phospholipid as a biological fluorescent probe for studying fusion of virus membrane with liposomes
    • Pal, R., Y. Barenholz, and R. R. Wagner. 1988. Pyrene phospholipid as a biological fluorescent probe for studying fusion of virus membrane with liposomes. Biochemistry. 27:30-36.
    • (1988) Biochemistry , vol.27 , pp. 30-36
    • Pal, R.1    Barenholz, Y.2    Wagner, R.R.3
  • 36
    • 0028934164 scopus 로고
    • Liposome destabilization induced by the HIV-1 fusion peptide. Effect of a single amino acid substitution
    • Pereira, F. B., F. M. Goñi, and J. L. Nieva. 1995. Liposome destabilization induced by the HIV-1 fusion peptide. Effect of a single amino acid substitution. FEBS Lett. 362:243-246.
    • (1995) FEBS Lett. , vol.362 , pp. 243-246
    • Pereira, F.B.1    Goñi, F.M.2    Nieva, J.L.3
  • 37
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • Rafalski, M., J. Lear, and W. DeGrado. 1990. Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41. Biochemistry. 29:7917-7922.
    • (1990) Biochemistry , vol.29 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.2    DeGrado, W.3
  • 38
    • 0028023001 scopus 로고
    • Mode of membrane interaction of wild type and mutant signal peptides of the Escherichia coli outer membrane protein A
    • Sankaram, M. B., and J. D. Jones. 1994. Mode of membrane interaction of wild type and mutant signal peptides of the Escherichia coli outer membrane protein A. J. Biol. Chem. 269:23477-23483.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23477-23483
    • Sankaram, M.B.1    Jones, J.D.2
  • 40
    • 0028824850 scopus 로고
    • Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin
    • Steinhauer, D. A., S. A. Wharton, J. J. Skehel, and D. C. Wiley. 1995. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. J. Virol. 69:6643-6651.
    • (1995) J. Virol. , vol.69 , pp. 6643-6651
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4
  • 41
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D. K., D. Hoekstra, and R. E. Pagano. 1981. Use of resonance energy transfer to monitor membrane fusion. Biochemistry. 20: 4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 42
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • Surewicz, W. K., H. H. Manisch, and D. Chapman. 1993. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry. 32:389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Manisch, H.H.2    Chapman, D.3
  • 43
    • 0342573078 scopus 로고
    • Modulation of protein structure by the lipid environment
    • P. J. Quinn and R. J. Cherry, editors. Portland Press, London
    • Surewicz, W. K., A. Muga, and H. H. Mantsch. 1992. Modulation of protein structure by the lipid environment. In Structural and Dynamic Properties of Lipids and Membranes. P. J. Quinn and R. J. Cherry, editors. Portland Press, London. 153-164.
    • (1992) Structural and Dynamic Properties of Lipids and Membranes , pp. 153-164
    • Surewicz, W.K.1    Muga, A.2    Mantsch, H.H.3
  • 44
    • 0025369546 scopus 로고
    • Conformation of membrane fusion-active 20-residue peptides with or without iipid bilayers. Implicalion of α-helix formation for membrane fusion
    • Takahashi, S. 1990. Conformation of membrane fusion-active 20-residue peptides with or without iipid bilayers. Implicalion of α-helix formation for membrane fusion. Biochemistry. 29:6257-6264.
    • (1990) Biochemistry , vol.29 , pp. 6257-6264
    • Takahashi, S.1
  • 45
    • 0025913906 scopus 로고
    • Membrane insertion and lateral mobility of synthetic amphiphilic signal peplides in lipid model membranes
    • Tamm, L. K. 1991. Membrane insertion and lateral mobility of synthetic amphiphilic signal peplides in lipid model membranes. Biochim. Biophys. Acta. 1071:123-148.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 123-148
    • Tamm, L.K.1
  • 46
    • 0027298813 scopus 로고
    • Surface-induced conformational switching in amphiphilic peptide segments of apolipoproteins B and E and model peptides
    • Taylor, J. W., I. L. Shih, A. M. Lees, and R. S. Lees. 1993. Surface-induced conformational switching in amphiphilic peptide segments of apolipoproteins B and E and model peptides. Int. J. Pept. Protein Res. 41:536-547.
    • (1993) Int. J. Pept. Protein Res. , vol.41 , pp. 536-547
    • Taylor, J.W.1    Shih, I.L.2    Lees, A.M.3    Lees, R.S.4
  • 47
    • 0025276435 scopus 로고
    • Viral and cellular membrane fusion proteins
    • White, J. 1990. Viral and cellular membrane fusion proteins. Annu. Rev. Physiol. 52:675-697.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 675-697
    • White, J.1
  • 48
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J. 1992. Membrane fusion. Science. 258:917-923.
    • (1992) Science , vol.258 , pp. 917-923
    • White, J.1
  • 49
    • 0029097115 scopus 로고
    • Structure, function, and membrane integration of defensins
    • White, S. H., W. C. Wimley, and M. E. Selsted. 1995. Structure, function, and membrane integration of defensins. Curr. Opin. Struct. Biol. 5: 521-527.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 521-527
    • White, S.H.1    Wimley, W.C.2    Selsted, M.E.3
  • 50
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of human immunodeficiency virus type I gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild, C., J. W. Dubay, T. Greenwell, T. Baird, T. G. Oas, C. McDanal, E. Hunter, and T. Matthews. 1994. Propensity for a leucine zipper-like domain of human immunodeficiency virus type I gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proc. Natl. Acad. Sci. USA. 91: 12676-12680.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3    Baird, T.4    Oas, T.G.5    McDanal, C.6    Hunter, E.7    Matthews, T.8
  • 51
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W., and S. H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nature Struct. Biol. 3:842-848.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.1    White, S.H.2


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