메뉴 건너뛰기




Volumn 1818, Issue 11, 2012, Pages 2521-2528

Mechanism of membrane perturbation by the HIV-1 gp41 membrane-proximal external region and its modulation by cholesterol

Author keywords

HIV gp41; Lytic pore; Membrane curvature; MPER lipid interaction; X ray scattering

Indexed keywords

CHOLESTEROL; EPITOPE; GLYCOPROTEIN GP 41; MONOCLONAL ANTIBODY 4E10;

EID: 84864075527     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2012.06.002     Document Type: Article
Times cited : (22)

References (49)
  • 2
    • 59849107898 scopus 로고    scopus 로고
    • Common principles and intermediates of viral protein-mediated fusion: The HIV-1 paradigm
    • G.B. Melikyan Common principles and intermediates of viral protein-mediated fusion: the HIV-1 paradigm Retrovirology 5 2008 111
    • (2008) Retrovirology , vol.5 , pp. 111
    • Melikyan, G.B.1
  • 3
    • 0037810986 scopus 로고    scopus 로고
    • Viral fusion proteins: Multiple regions contribute to membrane fusion
    • DOI 10.1016/S0005-2736(03)00170-6
    • S.G. Peisajovich, and Y. Shai Viral fusion proteins: multiple regions contribute to membrane fusion Biochim. Biophys. Acta 1614 2003 122 129 (Pubitemid 36851610)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1614 , Issue.1 , pp. 122-129
    • Peisajovich, S.G.1    Shai, Y.2
  • 4
    • 0038487379 scopus 로고    scopus 로고
    • Are fusion peptides a good model to study viral cell fusion?
    • DOI 10.1016/S0005-2736(03)00168-8
    • J.L. Nieva, and A. Agirre Are fusion peptides a good model to study viral cell fusion? Biochim. Biophys. Acta 1614 2003 104 115 (Pubitemid 36851608)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1614 , Issue.1 , pp. 104-115
    • Nieva, J.L.1    Agirre, A.2
  • 5
    • 45449105978 scopus 로고    scopus 로고
    • Interfacial pre-transmembrane domains in viral proteins promoting membrane fusion and fission
    • M. Lorizate, N. Huarte, A. Saez-Cirion, and J.L. Nieva Interfacial pre-transmembrane domains in viral proteins promoting membrane fusion and fission Biochim. Biophys. Acta 1778 2008 1624 1639
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1624-1639
    • Lorizate, M.1    Huarte, N.2    Saez-Cirion, A.3    Nieva, J.L.4
  • 6
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env- mediated fusion and virus infectivity
    • K. Salzwedel, J.T. West, and E. Hunter A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity J. Virol. 73 1999 2469 2480 (Pubitemid 29098154)
    • (1999) Journal of Virology , vol.73 , Issue.3 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 7
    • 0033869815 scopus 로고    scopus 로고
    • Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: Putative role during viral fusion
    • DOI 10.1128/JVI.74.17.8038-8047.2000
    • T. Suarez, W.R. Gallaher, A. Agirre, F.M. Goni, and J.L. Nieva Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion J. Virol. 74 2000 8038 8047 (Pubitemid 30641649)
    • (2000) Journal of Virology , vol.74 , Issue.17 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 8
    • 58149517729 scopus 로고    scopus 로고
    • Identification of the LWYIK motif located in the human immunodeficiency virus type 1 transmembrane gp41 protein as a distinct determinant for viral infection
    • S.S. Chen, P. Yang, P.Y. Ke, H.F. Li, W.E. Chan, D.K. Chang, C.K. Chuang, Y. Tsai, and S.C. Huang Identification of the LWYIK motif located in the human immunodeficiency virus type 1 transmembrane gp41 protein as a distinct determinant for viral infection J. Virol. 83 2009 870 883
    • (2009) J. Virol. , vol.83 , pp. 870-883
    • Chen, S.S.1    Yang, P.2    Ke, P.Y.3    Li, H.F.4    Chan, W.E.5    Chang, D.K.6    Chuang, C.K.7    Tsai, Y.8    Huang, S.C.9
  • 9
    • 81255164798 scopus 로고    scopus 로고
    • Membrane-proximal external HIV-1 gp41 motif adapted for destabilizing the highly rigid viral envelope
    • B. Apellaniz, A. Ivankin, S. Nir, D. Gidalevitz, and J.L. Nieva Membrane-proximal external HIV-1 gp41 motif adapted for destabilizing the highly rigid viral envelope Biophys. J. 101 2011 2426 2435
    • (2011) Biophys. J. , vol.101 , pp. 2426-2435
    • Apellaniz, B.1    Ivankin, A.2    Nir, S.3    Gidalevitz, D.4    Nieva, J.L.5
  • 11
    • 0035859948 scopus 로고    scopus 로고
    • The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles
    • DOI 10.1021/bi010640u
    • D.J. Schibli, R.C. Montelaro, and H.J. Vogel The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles Biochemistry 40 2001 9570 9578 (Pubitemid 32757895)
    • (2001) Biochemistry , vol.40 , Issue.32 , pp. 9570-9578
    • Schibli, D.J.1    Montelaro, R.C.2    Vogel, H.J.3
  • 12
    • 37849000389 scopus 로고    scopus 로고
    • HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane
    • Z.Y. Sun, K.J. Oh, M. Kim, J. Yu, V. Brusic, L. Song, Z. Qiao, J.H. Wang, G. Wagner, and E.L. Reinherz HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane Immunity 28 2008 52 63
    • (2008) Immunity , vol.28 , pp. 52-63
    • Sun, Z.Y.1    Oh, K.J.2    Kim, M.3    Yu, J.4    Brusic, V.5    Song, L.6    Qiao, Z.7    Wang, J.H.8    Wagner, G.9    Reinherz, E.L.10
  • 13
    • 0038418536 scopus 로고    scopus 로고
    • The pre-transmembrane region of the human immunodeficiency virus type-1 glycoprotein: A novel fusogenic sequence
    • DOI 10.1016/S0014-5793(00)01785-3, PII S0014579300017853
    • T. Suarez, S. Nir, F.M. Goni, A. Saez-Cirion, and J.L. Nieva The pre-transmembrane region of the human immunodeficiency virus type-1 glycoprotein: a novel fusogenic sequence FEBS Lett. 477 2000 145 149 (Pubitemid 30438873)
    • (2000) FEBS Letters , vol.477 , Issue.1-2 , pp. 145-149
    • Suarez, T.1    Nir, S.2    Goni, F.M.3    Saez-Cirion, A.4    Nieva, J.L.5
  • 14
    • 2442559243 scopus 로고    scopus 로고
    • The C- and the N-terminal Regions of Glycoprotein 41 Ectodomain Fuse Membranes Enriched and Not Enriched with Cholesterol, Respectively
    • DOI 10.1074/jbc.M304950200
    • S. Shnaper, K. Sackett, S.A. Gallo, R. Blumenthal, and Y. Shai The C- and the N-terminal regions of glycoprotein 41 ectodomain fuse membranes enriched and not enriched with cholesterol, respectively J. Biol. Chem. 279 2004 18526 18534 (Pubitemid 38623272)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18526-18534
    • Shnaper, S.1    Sackett, K.2    Gallo, S.A.3    Blumenthal, R.4    Shai, Y.5
  • 15
    • 77952305288 scopus 로고    scopus 로고
    • Cholesterol interaction with proteins that partition into membrane domains: An overview
    • R.M. Epand, A. Thomas, R. Brasseur, and R.F. Epand Cholesterol interaction with proteins that partition into membrane domains: an overview Subcell. Biochem. 51 2010 253 278
    • (2010) Subcell. Biochem. , vol.51 , pp. 253-278
    • Epand, R.M.1    Thomas, A.2    Brasseur, R.3    Epand, R.F.4
  • 16
    • 33845987097 scopus 로고    scopus 로고
    • Recognition and blocking of HIV-1 gp41 pre-transmembrane sequence by monoclonal 4E10 antibody in a raft-like membrane environment
    • DOI 10.1074/jbc.M605998200
    • M. Lorizate, A. Cruz, N. Huarte, R. Kunert, J. Perez-Gil, and J.L. Nieva Recognition and blocking of HIV-1 gp41 pre-transmembrane sequence by monoclonal 4E10 antibody in a Raft-like membrane environment J. Biol. Chem. 281 2006 39598 39606 (Pubitemid 46041919)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.51 , pp. 39598-39606
    • Lorizate, M.1    Cruz, A.2    Huarte, N.3    Kunert, R.4    Perez-Gil, J.5    Nieva, J.L.6
  • 17
    • 40849136223 scopus 로고    scopus 로고
    • The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: Dominant site of antibody neutralization and target for vaccine design
    • DOI 10.1128/MMBR.00020-07
    • M. Montero, N.E. van Houten, X. Wang, and J.K. Scott The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design Microbiol. Mol. Biol. Rev. 72 2008 54 84 (Pubitemid 351398055)
    • (2008) Microbiology and Molecular Biology Reviews , vol.72 , Issue.1 , pp. 54-84
    • Montero, M.1    Van Houten, N.E.2    Wang, X.3    Scott, J.K.4
  • 19
    • 80052311947 scopus 로고    scopus 로고
    • A new paradigm in molecular recognition? Specific antibody binding to membrane-inserted HIV-1 epitopes
    • J.L. Nieva, B. Apellaniz, N. Huarte, and M. Lorizate A new paradigm in molecular recognition? Specific antibody binding to membrane-inserted HIV-1 epitopes J. Mol. Recognit. 24 2011 642 646
    • (2011) J. Mol. Recognit. , vol.24 , pp. 642-646
    • Nieva, J.L.1    Apellaniz, B.2    Huarte, N.3    Lorizate, M.4
  • 20
    • 43949135190 scopus 로고    scopus 로고
    • Importance of the membrane-perturbing properties of the membrane-proximal external region of human immunodeficiency virus type 1 gp41 to viral fusion
    • DOI 10.1128/JVI.00305-08
    • S.A. Vishwanathan, and E. Hunter Importance of the membrane-perturbing properties of the membrane-proximal external region of human immunodeficiency virus type 1 gp41 to viral fusion J. Virol. 82 2008 5118 5126 (Pubitemid 351705220)
    • (2008) Journal of Virology , vol.82 , Issue.11 , pp. 5118-5126
    • Vishwanathan, S.A.1    Hunter, E.2
  • 21
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y. Shai Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim. Biophys. Acta 1462 1999 55 70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 24
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • R.M. Epand, and H.J. Vogel Diversity of antimicrobial peptides and their mechanisms of action Biochim. Biophys. Acta 1462 1999 11 28
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 25
    • 77954059555 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions
    • V. Buzon, G. Natrajan, D. Schibli, F. Campelo, M.M. Kozlov, and W. Weissenhorn Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions PLoS Pathog. 6 2010 e1000880
    • (2010) PLoS Pathog. , vol.6 , pp. 1000880
    • Buzon, V.1    Natrajan, G.2    Schibli, D.3    Campelo, F.4    Kozlov, M.M.5    Weissenhorn, W.6
  • 27
    • 0021890825 scopus 로고
    • 2+-induced fusion and destabilization of liposomes
    • DOI 10.1021/bi00334a005
    • 2 +-induced fusion and destabilization of liposomes Biochemistry 24 1985 3099 3106 (Pubitemid 15028709)
    • (1985) Biochemistry , vol.24 , Issue.13 , pp. 3099-3106
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.3
  • 28
    • 77749289129 scopus 로고    scopus 로고
    • Cholesterol-phospholipid interactions: New insights from surface x-ray scattering data
    • A. Ivankin, I. Kuzmenko, and D. Gidalevitz Cholesterol-phospholipid interactions: new insights from surface x-ray scattering data Phys. Rev. Lett. 104 2010 108101
    • (2010) Phys. Rev. Lett. , vol.104 , pp. 108101
    • Ivankin, A.1    Kuzmenko, I.2    Gidalevitz, D.3
  • 29
    • 33646270878 scopus 로고    scopus 로고
    • In situ characterization of lipid A interaction with antimicrobial peptides using surface X-ray scattering
    • F. Neville, C.S. Hodges, C. Liu, O. Konovalov, and D. Gidalevitz In situ characterization of lipid A interaction with antimicrobial peptides using surface X-ray scattering Biochim. Biophys. Acta 1758 2006 232 240
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 232-240
    • Neville, F.1    Hodges, C.S.2    Liu, C.3    Konovalov, O.4    Gidalevitz, D.5
  • 31
    • 0022414150 scopus 로고
    • Effects of a novel compound (AL 721) on HTLV-III infectivity in vitro
    • P.S. Sarin, R.C. Gallo, D.I. Scheer, F. Crews, and A.S. Lippa Effects of a novel compound (AL 721) on HTLV-III infectivity in vitro N. Engl. J. Med. 313 1985 1289 1290 (Pubitemid 16217055)
    • (1985) New England Journal of Medicine , vol.313 , Issue.20 , pp. 1289-1290
    • Sarin, P.S.1    Gallo, R.C.2    Scheer, D.I.3
  • 32
    • 0023026131 scopus 로고
    • Anti-viral activity of amphotericin B methyl ester: inhibition of HTLV-III replication in cell culture
    • DOI 10.1016/0006-2952(86)90037-7
    • C.P. Schaffner, O.J. Plescia, D. Pontani, D. Sun, A. Thornton, R.C. Pandey, and P.S. Sarin Anti-viral activity of amphotericin B methyl ester: inhibition of HTLV-III replication in cell culture Biochem. Pharmacol. 35 1986 4110 4113 (Pubitemid 17186165)
    • (1986) Biochemical Pharmacology , vol.35 , Issue.22 , pp. 4110-4113
    • Schaffner, C.P.1    Plescia, O.J.2    Pontani, D.3
  • 33
    • 0037771098 scopus 로고    scopus 로고
    • Cholesterol depletion of human immunodeficiency virus type 1 and simian immunodeficiency virus with β-cyclodextrin inactivates and permeabilizes the virions: Evidence for virion-associated lipid rafts
    • DOI 10.1128/JVI.77.15.8237-8248.2003
    • D.R. Graham, E. Chertova, J.M. Hilburn, L.O. Arthur, and J.E. Hildreth Cholesterol depletion of human immunodeficiency virus type 1 and simian immunodeficiency virus with beta-cyclodextrin inactivates and permeabilizes the virions: evidence for virion-associated lipid rafts J. Virol. 77 2003 8237 8248 (Pubitemid 36871451)
    • (2003) Journal of Virology , vol.77 , Issue.15 , pp. 8237-8248
    • Graham, D.R.M.1    Chertova, E.2    Hilburn, J.M.3    Arthur, L.O.4    Hildreth, J.E.K.5
  • 34
    • 0041823452 scopus 로고    scopus 로고
    • Lipid rafts and HIV pathogenesis: Virion-associated cholesterol is required for fusion and infection of susceptible cells
    • DOI 10.1089/088922203322280900
    • Z. Liao, D.R. Graham, and J.E. Hildreth Lipid rafts and HIV pathogenesis: virion-associated cholesterol is required for fusion and infection of susceptible cells AIDS Res. Hum. Retroviruses 19 2003 675 687 (Pubitemid 37047093)
    • (2003) AIDS Research and Human Retroviruses , vol.19 , Issue.8 , pp. 675-687
    • Liao, Z.1    Graham, D.R.2    Hildreth, J.E.K.3
  • 35
    • 33745041479 scopus 로고    scopus 로고
    • Roles of bilayer material properties in function and distribution of membrane proteins
    • DOI 10.1146/annurev.biophys.35.040405.102022
    • T.J. McIntosh, and S.A. Simon Roles of bilayer material properties in function and distribution of membrane proteins Annu. Rev. Biophys. Biomol. Struct. 35 2006 177 198 (Pubitemid 43877375)
    • (2006) Annual Review of Biophysics and Biomolecular Structure , vol.35 , pp. 177-198
    • McIntosh, T.J.1    Simon, S.A.2
  • 37
    • 77649241031 scopus 로고    scopus 로고
    • A comparative study on the interactions of SMAP-29 with lipid monolayers
    • F. Neville, A. Ivankin, O. Konovalov, and D. Gidalevitz A comparative study on the interactions of SMAP-29 with lipid monolayers Biochim. Biophys. Acta 1798 2010 851 860
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 851-860
    • Neville, F.1    Ivankin, A.2    Konovalov, O.3    Gidalevitz, D.4
  • 38
    • 50949104097 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5
    • N. Huarte, M. Lorizate, R. Maeso, R. Kunert, R. Arranz, J.M. Valpuesta, and J.L. Nieva The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5 J. Virol. 82 2008 8986 8996
    • (2008) J. Virol. , vol.82 , pp. 8986-8996
    • Huarte, N.1    Lorizate, M.2    Maeso, R.3    Kunert, R.4    Arranz, R.5    Valpuesta, J.M.6    Nieva, J.L.7
  • 39
    • 0037077229 scopus 로고    scopus 로고
    • Sphingomyelin and cholesterol promote HIV-1 gp41 pretransmembrane sequence surface aggregation and membrane restructuring
    • DOI 10.1074/jbc.M202255200
    • A. Saez-Cirion, S. Nir, M. Lorizate, A. Agirre, A. Cruz, J. Perez-Gil, and J.L. Nieva Sphingomyelin and cholesterol promote HIV-1 gp41 pretransmembrane sequence surface aggregation and membrane restructuring J. Biol. Chem. 277 2002 21776 21785 (Pubitemid 34952329)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21776-21785
    • Saez-Cirion, A.1    Nir, S.2    Lorizate, M.3    Agirre, A.4    Cruz, A.5    Perez-Gil, J.6    Nieva, J.L.7
  • 40
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • DOI 10.1146/annurev.biochem.72.121801.161504
    • L.V. Chernomordik, and M.M. Kozlov Protein-lipid interplay in fusion and fission of biological membranes Annu. Rev. Biochem. 72 2003 175 207 (Pubitemid 36930445)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 41
    • 78649761049 scopus 로고    scopus 로고
    • All-or-none versus graded: Single-vesicle analysis reveals lipid composition effects on membrane permeabilization
    • B. Apellaniz, J.L. Nieva, P. Schwille, and A.J. Garcia-Saez All-or-none versus graded: single-vesicle analysis reveals lipid composition effects on membrane permeabilization Biophys. J. 99 2010 3619 3628
    • (2010) Biophys. J. , vol.99 , pp. 3619-3628
    • Apellaniz, B.1    Nieva, J.L.2    Schwille, P.3    Garcia-Saez, A.J.4
  • 42
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • W.C. Wimley Describing the mechanism of antimicrobial peptide action with the interfacial activity model ACS Chem. Biol. 5 2010 905 917
    • (2010) ACS Chem. Biol. , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 43
    • 2942754299 scopus 로고    scopus 로고
    • Molecular mechanisms of peptide-induced pores in membranes
    • H.W. Huang Molecular mechanisms of peptide-induced pores in membranes Phys. Rev. Lett. 92 2004 198304
    • (2004) Phys. Rev. Lett. , vol.92 , pp. 198304
    • Huang, H.W.1
  • 44
    • 2942692314 scopus 로고    scopus 로고
    • Membrane perturbation induced by interfacially adsorbed peptides
    • DOI 10.1529/biophysj.103.033605
    • A. Zemel, A. Ben-Shaul, and S. May Membrane perturbation induced by interfacially adsorbed peptides Biophys. J. 86 2004 3607 3619 (Pubitemid 38780240)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3607-3619
    • Zemel, A.1    Ben-Shaul, A.2    May, S.3
  • 45
    • 46449135255 scopus 로고    scopus 로고
    • The hydrophobic insertion mechanism of membrane curvature generation by proteins
    • F. Campelo, H.T. McMahon, and M.M. Kozlov The hydrophobic insertion mechanism of membrane curvature generation by proteins Biophys. J. 95 2008 2325 2339
    • (2008) Biophys. J. , vol.95 , pp. 2325-2339
    • Campelo, F.1    McMahon, H.T.2    Kozlov, M.M.3
  • 48
    • 57149107577 scopus 로고    scopus 로고
    • Cryoelectron tomography of HIV-1 envelope spikes: Further evidence for tripod-like legs
    • P. Zhu, H. Winkler, E. Chertova, K.A. Taylor, and K.H. Roux Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs PLoS Pathog. 4 2008 e1000203
    • (2008) PLoS Pathog. , vol.4 , pp. 1000203
    • Zhu, P.1    Winkler, H.2    Chertova, E.3    Taylor, K.A.4    Roux, K.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.