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Volumn 93, Issue 6, 2007, Pages 2048-2055

HIV-1 fusion peptide decreases bending energy and promotes curved fusion intermediates

Author keywords

[No Author keywords available]

Indexed keywords

DIOLEOYLPHOSPHATIDYLCHOLINE; HYBRID PROTEIN;

EID: 34548726186     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.109181     Document Type: Article
Times cited : (89)

References (45)
  • 3
    • 0023651341 scopus 로고
    • Delineation of a region of the hyman-immunodeficiency-virus type-1 gp120 glycoprotein critical for interaction with the CD4 receptor
    • Lasky, A. L., G. Nakamura, D. H. Smith, C. Fennie, C. Shimasaki, E. Patzer, P. Berman, T. Gregory, and D. J. Capon. 1987. Delineation of a region of the hyman-immunodeficiency-virus type-1 gp120 glycoprotein critical for interaction with the CD4 receptor. Cell. 50:975-985.
    • (1987) Cell , vol.50 , pp. 975-985
    • Lasky, A.L.1    Nakamura, G.2    Smith, D.H.3    Fennie, C.4    Shimasaki, C.5    Patzer, E.6    Berman, P.7    Gregory, T.8    Capon, D.J.9
  • 5
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human-immunodeficiency-virus
    • Gallaher, W. R. 1987. Detection of a fusion peptide sequence in the transmembrane protein of human-immunodeficiency-virus. Cell. 50:327-328.
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 7
    • 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
  • 9
    • 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
  • 10
    • 0032934830 scopus 로고    scopus 로고
    • Membrane interactions of the synthetic N-terminal peptide of HIV-1 gp41 and its structural analogs
    • Mobley, P. W., A. J. Waring, M. A. Sherman, and L. M. Gordon. 1999. Membrane interactions of the synthetic N-terminal peptide of HIV-1 gp41 and its structural analogs. Biochim. Biophys. Acta. 1418:1-18.
    • (1999) Biochim. Biophys. Acta , vol.1418 , pp. 1-18
    • Mobley, P.W.1    Waring, A.J.2    Sherman, M.A.3    Gordon, L.M.4
  • 11
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R., and T. C. Sudhof. 1999. Membrane fusion and exocytosis. Annu. Rev. Biochem. 68:863-911.
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 12
    • 0038290760 scopus 로고    scopus 로고
    • Lipid intermediates in membrane fusion: Formation, structure, and decay of hemifusion diaphragm
    • Chernomordik, L. V., and M. M. Kozlov. 2003. Lipid intermediates in membrane fusion: formation, structure, and decay of hemifusion diaphragm. Annu. Rev. Biochem. 72:175-207.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 13
    • 0041428123 scopus 로고    scopus 로고
    • Membrane fusion: A structural perspective on the interplay of lipids and proteins
    • Tamm, L. K., J. Crane, and V. Kiessling. 2003. Membrane fusion: a structural perspective on the interplay of lipids and proteins. Curr. Opin. Struct. Biol. 13:453-466.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 453-466
    • Tamm, L.K.1    Crane, J.2    Kiessling, V.3
  • 15
    • 2942635759 scopus 로고    scopus 로고
    • The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement
    • Cohen, F. S., and G. B. Melikyan. 2004. The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement. J. Membr. Biol. 199:1-14.
    • (2004) J. Membr. Biol , vol.199 , pp. 1-14
    • Cohen, F.S.1    Melikyan, G.B.2
  • 17
    • 2142712534 scopus 로고    scopus 로고
    • Energetics of vesicle fusion intermediates: Comparison of calculations with observed effects of osmotic and curvature stresses
    • Malinin, V. S., and B. R. Lentz. 2004. Energetics of vesicle fusion intermediates: comparison of calculations with observed effects of osmotic and curvature stresses. Biophys. J. 86:2951-2964.
    • (2004) Biophys. J , vol.86 , pp. 2951-2964
    • Malinin, V.S.1    Lentz, B.R.2
  • 18
    • 0036151868 scopus 로고    scopus 로고
    • Filling potholes on the path to fusion pores
    • Lentz, B. R., D. P. Siegel, and V. Malinin. 2002. Filling potholes on the path to fusion pores. Biophys. J. 82:555-557.
    • (2002) Biophys. J , vol.82 , pp. 555-557
    • Lentz, B.R.1    Siegel, D.P.2    Malinin, V.3
  • 19
    • 0036154247 scopus 로고    scopus 로고
    • Stalk model of membrane fusion: Solution of energy crisis
    • Kozlovsky, Y., and M. M. Kozlov. 2002. Stalk model of membrane fusion: solution of energy crisis. Biophys. J. 82:882-895.
    • (2002) Biophys. J , vol.82 , pp. 882-895
    • Kozlovsky, Y.1    Kozlov, M.M.2
  • 20
    • 0036158070 scopus 로고    scopus 로고
    • Membrane fusion: Stalk model revisited
    • Markin, V. S., and J. P. Albanesi. 2002. Membrane fusion: stalk model revisited. Biophys. J. 82:693-712.
    • (2002) Biophys. J , vol.82 , pp. 693-712
    • Markin, V.S.1    Albanesi, J.P.2
  • 21
    • 11844266389 scopus 로고    scopus 로고
    • Stalk phase formation: Effects of dehydration and saddle splay modulus
    • Kozlovsky, Y., A. Efrat, D. P. Siegel, and M. M. Kozlov. 2004. Stalk phase formation: effects of dehydration and saddle splay modulus. Biophys. J. 87:2508-2521.
    • (2004) Biophys. J , vol.87 , pp. 2508-2521
    • Kozlovsky, Y.1    Efrat, A.2    Siegel, D.P.3    Kozlov, M.M.4
  • 22
    • 0037072603 scopus 로고    scopus 로고
    • Observation of a membrane fusion intermediate structure
    • Yang, L., and H. W. Huang. 2002. Observation of a membrane fusion intermediate structure. Science. 297:1877-1879.
    • (2002) Science , vol.297 , pp. 1877-1879
    • Yang, L.1    Huang, H.W.2
  • 23
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: Crossing a chasm in two leaps
    • Chernomordik, L. V., and M. M. Kozlov. 2005. Membrane hemifusion: crossing a chasm in two leaps. Cell. 123:375-382.
    • (2005) Cell , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 24
    • 37649031391 scopus 로고    scopus 로고
    • Diffuse scattering provides material parameters and electron density profiles of biomembranes
    • Liu, Y., and J. F. Nagle. 2004. Diffuse scattering provides material parameters and electron density profiles of biomembranes. Phys. Rev. E. 69:040901.
    • (2004) Phys. Rev. E , vol.69 , pp. 040901
    • Liu, Y.1    Nagle, J.F.2
  • 25
    • 22144486884 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase DMPC and DLPC lipid bilayers using x-ray scattering from oriented multilamellar arrays and from unilamellar vesicles
    • Kučerka, N., Y. Liu, N. Chu, H. I. Petrache, S. Tristram-Nagle, and J. F. Nagle. 2005a. Structure of fully hydrated fluid phase DMPC and DLPC lipid bilayers using x-ray scattering from oriented multilamellar arrays and from unilamellar vesicles. Biophys. J. 88:1-12.
    • (2005) Biophys. J , vol.88 , pp. 1-12
    • Kučerka, N.1    Liu, Y.2    Chu, N.3    Petrache, H.I.4    Tristram-Nagle, S.5    Nagle, J.F.6
  • 26
    • 33646446451 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains
    • Kučerka, N., S. Tristram-Nagle, and J. F. Nagle. 2005b. Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains. J. Membr. Biol. 208:193-202.
    • (2005) J. Membr. Biol , vol.208 , pp. 193-202
    • Kučerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 27
    • 33744920795 scopus 로고    scopus 로고
    • Closer look at structure of fully hydrated fluid phase DPPC bilayers
    • Kučerka, N., S. Tristram-Nagle, and J. F. Nagle. 2006. Closer look at structure of fully hydrated fluid phase DPPC bilayers. Biophys. J. 90:L83-L85.
    • (2006) Biophys. J , vol.90
    • Kučerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 28
    • 0033516703 scopus 로고    scopus 로고
    • An amphipathic alpha-helix at a membrane interface: A structural study using a novel x-ray diffraction method
    • Hristova, K., W. W. Wimley, V. K. Mishra, G. M. Anantharamiah, J. P. Segrest, and S. H. White. 1999. An amphipathic alpha-helix at a membrane interface: a structural study using a novel x-ray diffraction method. J. Mol. Biol. 290:99-117.
    • (1999) J. Mol. Biol , vol.290 , pp. 99-117
    • Hristova, K.1    Wimley, W.W.2    Mishra, V.K.3    Anantharamiah, G.M.4    Segrest, J.P.5    White, S.H.6
  • 29
    • 0025889072 scopus 로고
    • Lipid-alamethicin interactions in-fluence alamethicin orientation
    • Huang, H. W., and Y. Wu. 1991. Lipid-alamethicin interactions in-fluence alamethicin orientation. Biophys. J. 60:1079-1087.
    • (1991) Biophys. J , vol.60 , pp. 1079-1087
    • Huang, H.W.1    Wu, Y.2
  • 30
    • 0033905953 scopus 로고    scopus 로고
    • Neutron diffraction studies of viral fusion peptides
    • Bradshaw, J. P., M. J. M. Darkes, J. Katsaras, and R. M. Epand. 2000. Neutron diffraction studies of viral fusion peptides. Physica B. 276-278:495-498.
    • (2000) Physica B , vol.276-278 , pp. 495-498
    • Bradshaw, J.P.1    Darkes, M.J.M.2    Katsaras, J.3    Epand, R.M.4
  • 32
    • 36549088496 scopus 로고    scopus 로고
    • Tristram-Nagle, S. 2007. Preparation of oriented, fully hydrated lipids samples for structure determination using x-ray scattering. In Methods in Molecular Biology, 400: Methods in Membrane Lipids. A. M. Dopico, editor. Humana Press, Totowa, NJ. 63-75.
    • Tristram-Nagle, S. 2007. Preparation of oriented, fully hydrated lipids samples for structure determination using x-ray scattering. In Methods in Molecular Biology, Vol. 400: Methods in Membrane Lipids. A. M. Dopico, editor. Humana Press, Totowa, NJ. 63-75.
  • 33
    • 4244085863 scopus 로고    scopus 로고
    • Lyatskaya, Y., Y. Liu, S. Tristram-Nagle, J. Katsaras, and J. F. Nagle. 2001. Method for obtaining structure and interactions from oriented lipid bilayers. Phys. Rev. E. 63:0119071-0119079.
    • Lyatskaya, Y., Y. Liu, S. Tristram-Nagle, J. Katsaras, and J. F. Nagle. 2001. Method for obtaining structure and interactions from oriented lipid bilayers. Phys. Rev. E. 63:0119071-0119079.
  • 36
    • 0024378918 scopus 로고
    • Hydration forces between phospholipid bilayers
    • Rand, R. P., and V. A. Parsegian. 1989. Hydration forces between phospholipid bilayers. Biochim. Biophys. Acta. 988:351-376.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 351-376
    • Rand, R.P.1    Parsegian, V.A.2
  • 37
    • 37649032524 scopus 로고    scopus 로고
    • Anomalous swelling of lipid bilayer stacks is caused by softening of the bending modulus
    • Chu, N., N. Kučerka, Y. Liu, S. Tristram-Nagle, and J. F. Nagle. 2005. Anomalous swelling of lipid bilayer stacks is caused by softening of the bending modulus. Phys. Rev. E. 71:041904.
    • (2005) Phys. Rev. E , vol.71 , pp. 041904
    • Chu, N.1    Kučerka, N.2    Liu, Y.3    Tristram-Nagle, S.4    Nagle, J.F.5
  • 38
    • 0033932837 scopus 로고    scopus 로고
    • Effect of chain length and unsaturation on elasticity of lipid bilayers
    • Rawicz, W., K. C. Olbrich, T. J. McIntosh, D. Needham, and E. Evans. 2000. Effect of chain length and unsaturation on elasticity of lipid bilayers. Biophys. J. 79:328-339.
    • (2000) Biophys. J , vol.79 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    McIntosh, T.J.3    Needham, D.4    Evans, E.5
  • 40
    • 84943997802 scopus 로고
    • Elastic properties of lipid bilayers - theory and possible experiments
    • Helfrich, W. 1973. Elastic properties of lipid bilayers - theory and possible experiments. Z. Naturforsch. 28:693-703.
    • (1973) Z. Naturforsch , vol.28 , pp. 693-703
    • Helfrich, W.1
  • 41
    • 0003266076 scopus 로고    scopus 로고
    • Adhesion between phosphatidylethanolamine bilayers
    • McIntosh, T. J., and S. A. Simon. 1996. Adhesion between phosphatidylethanolamine bilayers. Langmuir. 12:1622-1630.
    • (1996) Langmuir , vol.12 , pp. 1622-1630
    • McIntosh, T.J.1    Simon, S.A.2
  • 43
    • 0026813513 scopus 로고
    • Thermal mechanical fluctuations of fluid membranes in confined geometries - the case of soft confinement
    • Podgornik, R., and V. A. Parsegian. 1992. Thermal mechanical fluctuations of fluid membranes in confined geometries - the case of soft confinement. Langmuir. 8:557-562.
    • (1992) Langmuir , vol.8 , pp. 557-562
    • Podgornik, R.1    Parsegian, V.A.2
  • 44
    • 16844379486 scopus 로고    scopus 로고
    • Steric accessibility of the HIV-1 gp41 N-trimer region
    • Hamburger, A. E., S. Kim, B. D. Welch, and M. S. Kay. 2005. Steric accessibility of the HIV-1 gp41 N-trimer region. J. Biol. Chem. 280:12567-12572.
    • (2005) J. Biol. Chem , vol.280 , pp. 12567-12572
    • Hamburger, A.E.1    Kim, S.2    Welch, B.D.3    Kay, M.S.4
  • 45
    • 0034462310 scopus 로고    scopus 로고
    • Modulation of membrane curvature by peptides
    • Epand, R. M., and R. F. Epand. 2000. Modulation of membrane curvature by peptides. Biopolymers. 55:358-363.
    • (2000) Biopolymers , vol.55 , pp. 358-363
    • Epand, R.M.1    Epand, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.