메뉴 건너뛰기




Volumn 1798, Issue 2, 2010, Pages 194-201

Nuclear magnetic resonance evidence for retention of a lamellar membrane phase with curvature in the presence of large quantities of the HIV fusion peptide

Author keywords

Curvature; Fusion; HIV; Membrane; NMR; Peptide

Indexed keywords

CHOLESTEROL; HUMAN IMMUNODEFICIENCY VIRUS FUSION PEPTIDE; LIPID; UNCLASSIFIED DRUG; VIRUS FUSION PROTEIN;

EID: 74249088667     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.07.007     Document Type: Article
Times cited : (21)

References (49)
  • 1
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme
    • White J.M., Delos S.E., Brecher M., and Schornberg K. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43 (2008) 189-219
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 2
    • 0030682144 scopus 로고    scopus 로고
    • What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion
    • Durell S.R., Martin I., Ruysschaert J.M., Shai Y., and Blumenthal R. What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion. Mol. Membr. Biol. 14 (1997) 97-112
    • (1997) Mol. Membr. Biol. , vol.14 , pp. 97-112
    • Durell, S.R.1    Martin, I.2    Ruysschaert, J.M.3    Shai, Y.4    Blumenthal, R.5
  • 3
    • 42949163133 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy of human immunodeficiency virus fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strand registries
    • Qiang W., Bodner M.L., and Weliky D.P. Solid-state NMR spectroscopy of human immunodeficiency virus fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strand registries. J. Am. Chem. Soc. 130 (2008) 5459-5471
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 5459-5471
    • Qiang, W.1    Bodner, M.L.2    Weliky, D.P.3
  • 4
    • 34247556394 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance measurements of HIV fusion peptide to lipid distances reveal the intimate contact of beta strand peptide with membranes and the proximity of the Ala-14-Gly-16 region with lipid headgroups
    • Qiang W., Yang J., and Weliky D.P. Solid-state nuclear magnetic resonance measurements of HIV fusion peptide to lipid distances reveal the intimate contact of beta strand peptide with membranes and the proximity of the Ala-14-Gly-16 region with lipid headgroups. Biochemistry 46 (2007) 4997-5008
    • (2007) Biochemistry , vol.46 , pp. 4997-5008
    • Qiang, W.1    Yang, J.2    Weliky, D.P.3
  • 5
    • 59849106607 scopus 로고    scopus 로고
    • HIV fusion peptide and its cross-linked oligomers: efficient syntheses, significance of the trimer in fusion activity, correlation of β strand conformation with membrane cholesterol, and proximity to lipid headgroups
    • Qiang W., and Weliky D.P. HIV fusion peptide and its cross-linked oligomers: efficient syntheses, significance of the trimer in fusion activity, correlation of β strand conformation with membrane cholesterol, and proximity to lipid headgroups. Biochemistry 48 (2009) 289-301
    • (2009) Biochemistry , vol.48 , pp. 289-301
    • Qiang, W.1    Weliky, D.P.2
  • 6
    • 0028576923 scopus 로고
    • Membrane orientation of the SIV fusion peptide determines its effect on bilayer stability and ability to promote membrane fusion
    • Epand R.F., Martin I., Ruysschaert J.-M., and Epand R.M. Membrane orientation of the SIV fusion peptide determines its effect on bilayer stability and ability to promote membrane fusion. Biochem. Biophys. Res. Comm. 205 (1994) 1938-1943
    • (1994) Biochem. Biophys. Res. Comm. , vol.205 , pp. 1938-1943
    • Epand, R.F.1    Martin, I.2    Ruysschaert, J.-M.3    Epand, R.M.4
  • 8
    • 0032747031 scopus 로고    scopus 로고
    • Interbilayer lipid mixing induced by the human immunodeficiency virus type-1 fusion peptide on large unilamellar vesicles: the nature of the nonlamellar intermediates
    • Pereira F.B., Valpuesta J.M., Basanez G., Goni F.M., and Nieva J.L. Interbilayer lipid mixing induced by the human immunodeficiency virus type-1 fusion peptide on large unilamellar vesicles: the nature of the nonlamellar intermediates. Chem. Phys. Lipids 103 (1999) 11-20
    • (1999) Chem. Phys. Lipids , vol.103 , pp. 11-20
    • Pereira, F.B.1    Valpuesta, J.M.2    Basanez, G.3    Goni, F.M.4    Nieva, J.L.5
  • 9
    • 0034700998 scopus 로고    scopus 로고
    • The polar region consecutive to the HIV fusion peptide participates in membrane fusion
    • Peisajovich S.G., Epand R.F., Pritsker M., Shai Y., and Epand R.M. The polar region consecutive to the HIV fusion peptide participates in membrane fusion. Biochemistry 39 (2000) 1826-1833
    • (2000) Biochemistry , vol.39 , pp. 1826-1833
    • Peisajovich, S.G.1    Epand, R.F.2    Pritsker, M.3    Shai, Y.4    Epand, R.M.5
  • 10
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein-lipid interactions
    • Epand R.M. Lipid polymorphism and protein-lipid interactions. Biochim. Biophys. Acta 1376 (1998) 353-368
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 11
    • 0027362739 scopus 로고
    • The energetics of intermediates in membrane fusion: comparison of stalk and inverted micellar intermediate mechanisms
    • Siegel D.P. The energetics of intermediates in membrane fusion: comparison of stalk and inverted micellar intermediate mechanisms. Biophys. J. 65 (1993) 2124-2140
    • (1993) Biophys. J. , vol.65 , pp. 2124-2140
    • Siegel, D.P.1
  • 12
    • 0030783371 scopus 로고    scopus 로고
    • The mechanism of lamellar-to-inverted hexagonal phase transitions in phosphatidylethanolamine: implications for membrane fusion mechanisms
    • Siegel D.P., and Epand R.M. The mechanism of lamellar-to-inverted hexagonal phase transitions in phosphatidylethanolamine: implications for membrane fusion mechanisms. Biophys. J. 73 (1997) 3089-3111
    • (1997) Biophys. J. , vol.73 , pp. 3089-3111
    • Siegel, D.P.1    Epand, R.M.2
  • 13
    • 0038487375 scopus 로고    scopus 로고
    • Fusion peptides and the mechanism of viral fusion
    • Epand R.M. Fusion peptides and the mechanism of viral fusion. Biochim. Biophys. Acta 1614 (2003) 116-121
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 116-121
    • Epand, R.M.1
  • 14
    • 0025993884 scopus 로고
    • Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective
    • Bloom M., Evans E., and Mouritsen O.G. Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective. Quart. Rev. Biophys. 24 (1991) 293-397
    • (1991) Quart. Rev. Biophys. , vol.24 , pp. 293-397
    • Bloom, M.1    Evans, E.2    Mouritsen, O.G.3
  • 15
    • 0017752553 scopus 로고
    • Deuterium magnetic resonance: theory and application to lipid membranes
    • Seelig J. Deuterium magnetic resonance: theory and application to lipid membranes. Quart. Rev. Biophys. 10 (1977) 353-418
    • (1977) Quart. Rev. Biophys. , vol.10 , pp. 353-418
    • Seelig, J.1
  • 16
    • 0018982584 scopus 로고
    • Lipid conformation in model membranes
    • Seelig J., and Seelig A. Lipid conformation in model membranes. Quart. Rev. Biophys. 13 (1980) 19-64
    • (1980) Quart. Rev. Biophys. , vol.13 , pp. 19-64
    • Seelig, J.1    Seelig, A.2
  • 17
    • 0000510171 scopus 로고
    • Transverse nuclear spin relaxation in phospholipid bilayer membranes
    • Bloom M., and Sternin E. Transverse nuclear spin relaxation in phospholipid bilayer membranes. Biochemistry 26 (1987) 2101-2105
    • (1987) Biochemistry , vol.26 , pp. 2101-2105
    • Bloom, M.1    Sternin, E.2
  • 18
    • 0018812791 scopus 로고
    • Preparation and properties of N-α-9-fluorenylmethyloxycarbonylamino acids bearing tert-butyl side chain protection
    • Chang C.D., Waki M., Ahmad M., Meienhofer J., Lundell E.O., and Haug J.D. Preparation and properties of N-α-9-fluorenylmethyloxycarbonylamino acids bearing tert-butyl side chain protection. Int. J. Pept. Protein Res. 15 (1980) 59-66
    • (1980) Int. J. Pept. Protein Res. , vol.15 , pp. 59-66
    • Chang, C.D.1    Waki, M.2    Ahmad, M.3    Meienhofer, J.4    Lundell, E.O.5    Haug, J.D.6
  • 19
    • 85004753289 scopus 로고
    • Synthesis of N-2,2,2-(trichloroethoxycarbonyl)-l-amino acids and N-(9-fluorenylmethoxycarbonyl)-l-amino acids involving succinimidoxy anion as a leaving group in amino-acid protection
    • Lapatsanis L., Milias G., Froussios K., and Kolovos M. Synthesis of N-2,2,2-(trichloroethoxycarbonyl)-l-amino acids and N-(9-fluorenylmethoxycarbonyl)-l-amino acids involving succinimidoxy anion as a leaving group in amino-acid protection. Synthesis 8 (1983) 671-673
    • (1983) Synthesis , vol.8 , pp. 671-673
    • Lapatsanis, L.1    Milias, G.2    Froussios, K.3    Kolovos, M.4
  • 20
    • 0026544416 scopus 로고
    • A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity
    • Freed E.O., Delwart E.L., Buchschacher Jr. G.L., and Panganiban A.T. A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 70-74
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 70-74
    • Freed, E.O.1    Delwart, E.L.2    Buchschacher Jr., G.L.3    Panganiban, A.T.4
  • 21
    • 0028934164 scopus 로고
    • Liposome destabilization induced by the HIV-1 fusion peptide effect of a single amino acid substitution
    • Pereira F.B., Goni F.M., and Nieva J.L. Liposome destabilization induced by the HIV-1 fusion peptide effect of a single amino acid substitution. FEBS Lett. 362 (1995) 243-246
    • (1995) FEBS Lett. , vol.362 , pp. 243-246
    • Pereira, F.B.1    Goni, F.M.2    Nieva, J.L.3
  • 22
    • 7644220365 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance studies of HIV and influenza fusion peptide orientations in membrane bilayers using stacked glass plate samples
    • Wasniewski C.M., Parkanzky P.D., Bodner M.L., and Weliky D.P. Solid-state nuclear magnetic resonance studies of HIV and influenza fusion peptide orientations in membrane bilayers using stacked glass plate samples. Chem. Phys. Lipids 132 (2004) 89-100
    • (2004) Chem. Phys. Lipids , vol.132 , pp. 89-100
    • Wasniewski, C.M.1    Parkanzky, P.D.2    Bodner, M.L.3    Weliky, D.P.4
  • 23
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • Dempsey C.E. The actions of melittin on membranes. Biochim. Biophys. Acta 1031 (1990) 143-161
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 25
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • Aloia R.C., Tian H., and Jensen F.C. Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 5181-5185
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.2    Jensen, F.C.3
  • 27
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck D.K., Hoekstra D., and Pagano R.E. Use of resonance energy transfer to monitor membrane fusion. Biochemistry 20 (1981) 4093-4099
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 28
    • 0035838516 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance evidence for an extended beta strand conformation of the membrane-bound HIV-1 fusion peptide
    • Yang J., Gabrys C.M., and Weliky D.P. Solid-state nuclear magnetic resonance evidence for an extended beta strand conformation of the membrane-bound HIV-1 fusion peptide. Biochemistry 40 (2001) 8126-8137
    • (2001) Biochemistry , vol.40 , pp. 8126-8137
    • Yang, J.1    Gabrys, C.M.2    Weliky, D.P.3
  • 29
    • 0342506479 scopus 로고    scopus 로고
    • Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: dose and sequence effects
    • Pereira F.B., Goni F.M., Muga A., and Nieva J.L. Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: dose and sequence effects. Biophys. J. 73 (1997) 1977-1986
    • (1997) Biophys. J. , vol.73 , pp. 1977-1986
    • Pereira, F.B.1    Goni, F.M.2    Muga, A.3    Nieva, J.L.4
  • 30
    • 45149145322 scopus 로고
    • Rotational-echo double-resonance NMR
    • Gullion T., and Schaefer J. Rotational-echo double-resonance NMR. J. Magn. Reson. 81 (1989) 196-200
    • (1989) J. Magn. Reson. , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 33
    • 0000734747 scopus 로고
    • Elimination of resonance offset effects in rotational-echo, double-resonance NMR
    • Gullion T., and Schaefer J. Elimination of resonance offset effects in rotational-echo, double-resonance NMR. J. Magn. Reson. 92 (1991) 439-442
    • (1991) J. Magn. Reson. , vol.92 , pp. 439-442
    • Gullion, T.1    Schaefer, J.2
  • 34
    • 0042995329 scopus 로고    scopus 로고
    • Chemical shift referencing in MAS solid state NMR
    • Morcombe C.R., and Zilm K.W. Chemical shift referencing in MAS solid state NMR. J. Magn. Reson. 162 (2003) 479-486
    • (2003) J. Magn. Reson. , vol.162 , pp. 479-486
    • Morcombe, C.R.1    Zilm, K.W.2
  • 35
    • 0000068844 scopus 로고
    • Critical factors in the design of sensitive high resolution nuclear magnetic resonance spectrometers
    • Hoult D.I., and Richards R.E. Critical factors in the design of sensitive high resolution nuclear magnetic resonance spectrometers. Proc. R. Soc. Lond., Ser. A 344 (1975) 311-340
    • (1975) Proc. R. Soc. Lond., Ser. A , vol.344 , pp. 311-340
    • Hoult, D.I.1    Richards, R.E.2
  • 36
    • 8844279069 scopus 로고    scopus 로고
    • A trimeric HIV-1 fusion peptide construct which does not self-associate in aqueous solution and which has 15-fold higher membrane fusion rate
    • Yang R., Prorok M., Castellino F.J., and Weliky D.P. A trimeric HIV-1 fusion peptide construct which does not self-associate in aqueous solution and which has 15-fold higher membrane fusion rate. J. Am. Chem. Soc. 126 (2004) 14722-14723
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 14722-14723
    • Yang, R.1    Prorok, M.2    Castellino, F.J.3    Weliky, D.P.4
  • 37
    • 0036931991 scopus 로고    scopus 로고
    • Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides
    • Yang J., Parkanzky P.D., Bodner M.L., Duskin C.G., and Weliky D.P. Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides. J. Magn. Reson. 159 (2002) 101-110
    • (2002) J. Magn. Reson. , vol.159 , pp. 101-110
    • Yang, J.1    Parkanzky, P.D.2    Bodner, M.L.3    Duskin, C.G.4    Weliky, D.P.5
  • 38
    • 4444320707 scopus 로고    scopus 로고
    • Oligomeric beta structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers
    • Yang J., Prorok M., Castellino F.J., and Weliky D.P. Oligomeric beta structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers. Biophys. J. 87 (2004) 1951-1963
    • (2004) Biophys. J. , vol.87 , pp. 1951-1963
    • Yang, J.1    Prorok, M.2    Castellino, F.J.3    Weliky, D.P.4
  • 39
    • 0037354231 scopus 로고    scopus 로고
    • RefDB: a database of uniformly referenced protein chemical shifts
    • Zhang H.Y., Neal S., and Wishart D.S. RefDB: a database of uniformly referenced protein chemical shifts. J. Biomol. NMR 25 (2003) 173-195
    • (2003) J. Biomol. NMR , vol.25 , pp. 173-195
    • Zhang, H.Y.1    Neal, S.2    Wishart, D.S.3
  • 41
    • 0023052450 scopus 로고
    • Relationship between three-dimensional arrays of "lipidic particles" and bicontinuous cubic lipid phases
    • Rilfors L., Eriksson P.-O., Arvidson G., and Lindblom G. Relationship between three-dimensional arrays of "lipidic particles" and bicontinuous cubic lipid phases. Biochemistry 25 (1986) 7702-7711
    • (1986) Biochemistry , vol.25 , pp. 7702-7711
    • Rilfors, L.1    Eriksson, P.-O.2    Arvidson, G.3    Lindblom, G.4
  • 42
    • 0024278433 scopus 로고
    • Observation of inverted cubic phase in hydrated dioleoylphosphatidylethanolamine membranes
    • Shyamsunder E., Gruner S.M., Tate M.W., Turner D.C., So P.T.C., and Tilcock C.P.S. Observation of inverted cubic phase in hydrated dioleoylphosphatidylethanolamine membranes. Biochemistry 27 (1988) 2332-2336
    • (1988) Biochemistry , vol.27 , pp. 2332-2336
    • Shyamsunder, E.1    Gruner, S.M.2    Tate, M.W.3    Turner, D.C.4    So, P.T.C.5    Tilcock, C.P.S.6
  • 43
    • 0017099492 scopus 로고
    • 2H and divalent cations on the motion in the phosphate region of the polar headgroup
    • 2H and divalent cations on the motion in the phosphate region of the polar headgroup. Biochim. Biophys. Acta 436 (1976) 523-540
    • (1976) Biochim. Biophys. Acta , vol.436 , pp. 523-540
    • Cullis, P.R.1    DeKruijff, B.2
  • 44
    • 65249174493 scopus 로고    scopus 로고
    • Hairpin folding of HIV gp41 abrogates lipid mixing function at physiologic pH and inhibits lipid mixing by exposed gp41 constructs
    • Sackett K., Nethercott M.J., Shai Y., and Weliky D.P. Hairpin folding of HIV gp41 abrogates lipid mixing function at physiologic pH and inhibits lipid mixing by exposed gp41 constructs. Biochemistry 48 (2009) 2714-2722
    • (2009) Biochemistry , vol.48 , pp. 2714-2722
    • Sackett, K.1    Nethercott, M.J.2    Shai, Y.3    Weliky, D.P.4
  • 45
    • 0033024286 scopus 로고    scopus 로고
    • The interactions of the N-terminal fusogenic peptide of HIV-1 gp41 with neutral phospholipids
    • Curtain C., Separovic F., Nielsen K., Craik D., Zhong Y., and Kirkpatrick A. The interactions of the N-terminal fusogenic peptide of HIV-1 gp41 with neutral phospholipids. Eur. Biophys. J. 28 (1999) 427-436
    • (1999) Eur. Biophys. J. , vol.28 , pp. 427-436
    • Curtain, C.1    Separovic, F.2    Nielsen, K.3    Craik, D.4    Zhong, Y.5    Kirkpatrick, A.6
  • 46
    • 0035006138 scopus 로고    scopus 로고
    • Solid state NMR measurements of conformation and conformational distributions in the membrane-bound HIV-1 fusion peptide
    • Yang J., Parkanzky P.D., Khunte B.A., Canlas C.G., Yang R., Gabrys C.M., and Weliky D.P. Solid state NMR measurements of conformation and conformational distributions in the membrane-bound HIV-1 fusion peptide. J. Mol. Graph. Model. 19 (2001) 129-135
    • (2001) J. Mol. Graph. Model. , vol.19 , pp. 129-135
    • Yang, J.1    Parkanzky, P.D.2    Khunte, B.A.3    Canlas, C.G.4    Yang, R.5    Gabrys, C.M.6    Weliky, D.P.7
  • 47
    • 34447647665 scopus 로고    scopus 로고
    • Solid state NMR investigation of the interaction between biomimetic lipid bilayers and de novo designed fusogenic peptides
    • Agrawal P., Kiihne S., Hollander J., Hulsbergen F., Hofmann M., Langosch D., and de Groot H. Solid state NMR investigation of the interaction between biomimetic lipid bilayers and de novo designed fusogenic peptides. Chembiochem 8 (2007) 493-496
    • (2007) Chembiochem , vol.8 , pp. 493-496
    • Agrawal, P.1    Kiihne, S.2    Hollander, J.3    Hulsbergen, F.4    Hofmann, M.5    Langosch, D.6    de Groot, H.7
  • 48
    • 34548726186 scopus 로고    scopus 로고
    • HIV-1 fusion peptide decreases bending energy and promotes curved fusion intermediates
    • Tristram-Nagle S., and Nagle J.F. HIV-1 fusion peptide decreases bending energy and promotes curved fusion intermediates. Biophys. J. 93 (2007) 2048-2055
    • (2007) Biophys. J. , vol.93 , pp. 2048-2055
    • Tristram-Nagle, S.1    Nagle, J.F.2
  • 49
    • 0030790364 scopus 로고    scopus 로고
    • Structural study of the relationship between the rate of membrane fusion and the ability of the fusion peptide of influenza virus to perturb bilayers
    • Colotto A., and Epand R.M. Structural study of the relationship between the rate of membrane fusion and the ability of the fusion peptide of influenza virus to perturb bilayers. Biochemistry 36 (1997) 7644-7651
    • (1997) Biochemistry , vol.36 , pp. 7644-7651
    • Colotto, A.1    Epand, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.