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Volumn 326, Issue 5, 2003, Pages 1489-1501

On the interaction between gp41 and membranes: The immunodominant loop stabilizes gp41 helical hairpin conformation

Author keywords

Conformational change; HIV cell entry; Membrane fusion

Indexed keywords

GLYCOPROTEIN GP 41; RHODAMINE; TRYPTOPHAN; VIRUS PROTEIN;

EID: 0037424624     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00040-8     Document Type: Article
Times cited : (30)

References (40)
  • 2
    • 0030018156 scopus 로고    scopus 로고
    • CC CKR5: A RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1
    • Alkhatib G., Combadiere C., Broder C.C., Feng Y., Kennedy P.E., Murphy P.M., Berger E.A. CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1. Science. 272:1996;1955-1958.
    • (1996) Science , vol.272 , pp. 1955-1958
    • Alkhatib, G.1    Combadiere, C.2    Broder, C.C.3    Feng, Y.4    Kennedy, P.E.5    Murphy, P.M.6    Berger, E.A.7
  • 3
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng Y., Broder C.C., Kennedy P.E., Berger E.A. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science. 272:1996;872-877.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 5
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus
    • Gallaher W.R. Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell. 50:1987;327-328.
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 6
    • 0024564217 scopus 로고
    • Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide"
    • Harter C., James P., Bachi T., Semenza G., Brunner J. Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the "fusion peptide" J. Biol. Chem. 264:1989;6459-6464.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6459-6464
    • Harter, C.1    James, P.2    Bachi, T.3    Semenza, G.4    Brunner, J.5
  • 8
    • 0028864614 scopus 로고
    • A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein
    • Blacklow S.C., Lu M., Kim P.S. A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein. Biochemistry. 34:1995;14955-14962.
    • (1995) Biochemistry , vol.34 , pp. 14955-14962
    • Blacklow, S.C.1    Lu, M.2    Kim, P.S.3
  • 9
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M., Blacklow S.C., Kim P.S. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Struct. Biol. 2:1995;1075-1082.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 10
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan D.C., Fass D., Berger J.M., Kim P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell. 89:1997;263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 12
    • 0032541424 scopus 로고    scopus 로고
    • Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41
    • Caffrey M., Cai M., Kaufman J., Stahl S.J., Wingfield P.T., Covell D.G., et al. Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41. EMBO J. 17:1998;4572-4584.
    • (1998) EMBO J. , vol.17 , pp. 4572-4584
    • Caffrey, M.1    Cai, M.2    Kaufman, J.3    Stahl, S.J.4    Wingfield, P.T.5    Covell, D.G.6
  • 13
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild C.T., Shugars D.C., Greenwell T.K., McDanal C.B., Matthews T.J. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl Acad. Sci. USA. 91:1994;9770-9774.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 14
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough P.A., Hughson F.M., Skehel J.J., Wiley D.C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature. 371:1994;37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 15
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel J.J., Wiley D.C. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell. 95:1998;871-874.
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 16
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta R.A., Wild C.T., Weng Y., Weiss C.D. Capture of an early fusion-active conformation of HIV-1 gp41. Nature Struct. Biol. 5:1998;276-279.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 17
    • 0034714156 scopus 로고    scopus 로고
    • Membrane-induced conformational change during the activation of HIV-1 gp41
    • Kliger Y., Peisajovich S.G., Blumenthal R., Shai Y. Membrane-induced conformational change during the activation of HIV-1 gp41. J. Mol. Biol. 301:2000;905-914.
    • (2000) J. Mol. Biol. , vol.301 , pp. 905-914
    • Kliger, Y.1    Peisajovich, S.G.2    Blumenthal, R.3    Shai, Y.4
  • 18
    • 0035838975 scopus 로고    scopus 로고
    • SIV gp41 binds to membranes both in the monomeric and trimeric states: Consequences for the neuropathology and inhibition of HIV infection
    • Peisajovich S.G., Shai Y. SIV gp41 binds to membranes both in the monomeric and trimeric states: consequences for the neuropathology and inhibition of HIV infection. J. Mol. Biol. 311:2001;249-254.
    • (2001) J. Mol. Biol. , vol.311 , pp. 249-254
    • Peisajovich, S.G.1    Shai, Y.2
  • 19
    • 0033555680 scopus 로고    scopus 로고
    • Membrane-induced step in the activation of Sendai virus fusion protein
    • Ben-Efraim I., Kliger Y., Hermesh C., Shai Y. Membrane-induced step in the activation of Sendai virus fusion protein. J. Mol. Biol. 285:1999;609-625.
    • (1999) J. Mol. Biol. , vol.285 , pp. 609-625
    • Ben-Efraim, I.1    Kliger, Y.2    Hermesh, C.3    Shai, Y.4
  • 20
    • 0033582785 scopus 로고    scopus 로고
    • The ectodomain of HA2 of influenza virus promotes rapid pH dependent membrane fusion
    • Epand R.F., Macosko J.C., Russell C.J., Shin Y.K., Epand R.M. The ectodomain of HA2 of influenza virus promotes rapid pH dependent membrane fusion. J. Mol. Biol. 286:1999;489-503.
    • (1999) J. Mol. Biol. , vol.286 , pp. 489-503
    • Epand, R.F.1    Macosko, J.C.2    Russell, C.J.3    Shin, Y.K.4    Epand, R.M.5
  • 21
    • 0033600718 scopus 로고    scopus 로고
    • Direct evidence that the N-terminal heptad repeat of Sendai virus fusion protein participates in membrane fusion
    • Ghosh J.K., Shai Y. Direct evidence that the N-terminal heptad repeat of Sendai virus fusion protein participates in membrane fusion. J. Mol. Biol. 292:1999;531-546.
    • (1999) J. Mol. Biol. , vol.292 , pp. 531-546
    • Ghosh, J.K.1    Shai, Y.2
  • 22
    • 0034628898 scopus 로고    scopus 로고
    • The F1 protein of paramyxoviruses has two fusion peptides: Implications for the mechanism of membrane fusion
    • Peisajovich S.G., Samuel O., Shai Y. The F1 protein of paramyxoviruses has two fusion peptides: implications for the mechanism of membrane fusion. J. Mol. Biol. 296:2000;1353-1365.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1353-1365
    • Peisajovich, S.G.1    Samuel, O.2    Shai, Y.3
  • 23
    • 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
    • Suarez T., Gallaher W.R., Agirre A., Goni F.M., Nieva J.L. 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.
    • (2000) J. Virol. , vol.74 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 24
    • 0032843108 scopus 로고    scopus 로고
    • Monomer-trimer equilibrium of the ectodomain of SIV gp41: Insight into the mechanism of peptide inhibition of HIV infection
    • Caffrey M., Kaufman J., Stahl S., Wingfield P., Gronenborn A.M., Clore G.M. Monomer-trimer equilibrium of the ectodomain of SIV gp41: insight into the mechanism of peptide inhibition of HIV infection. Protein Sci. 8:1999;1904-1907.
    • (1999) Protein Sci. , vol.8 , pp. 1904-1907
    • Caffrey, M.1    Kaufman, J.2    Stahl, S.3    Wingfield, P.4    Gronenborn, A.M.5    Clore, G.M.6
  • 26
    • 0031554882 scopus 로고    scopus 로고
    • Determination of the secondary structure and global topology of the 44 kDa ectodomain of gp41 of the simian immunodeficiency virus by multidimensional nuclear magnetic resonance spectroscopy
    • Caffrey M., Cai M., Kaufman J., Stahl S.J., Wingfield P.T., Gronenborn A.M., Clore G.M. Determination of the secondary structure and global topology of the 44 kDa ectodomain of gp41 of the simian immunodeficiency virus by multidimensional nuclear magnetic resonance spectroscopy. J. Mol. Biol. 271:1997;819-826.
    • (1997) J. Mol. Biol. , vol.271 , pp. 819-826
    • Caffrey, M.1    Cai, M.2    Kaufman, J.3    Stahl, S.J.4    Wingfield, P.T.5    Gronenborn, A.M.6    Clore, G.M.7
  • 27
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson M., Mantsch H.H. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30:1995;95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 28
    • 0034975305 scopus 로고    scopus 로고
    • Ligand-modulation of the stability of the glucose transporter GLUT 1
    • Epand R.F., Epand R.M., Jung C.Y. Ligand-modulation of the stability of the glucose transporter GLUT 1. Protein Sci. 10:2001;1363-1369.
    • (2001) Protein Sci. , vol.10 , pp. 1363-1369
    • Epand, R.F.1    Epand, R.M.2    Jung, C.Y.3
  • 30
    • 0242282490 scopus 로고    scopus 로고
    • HIV-1 entry into T-cells is not dependent on CD4 and CCR5 localization to sphingolipid-enriched, detergent-resistant, raft membrane domains
    • epub ahead of printing on Nov. 12 as Manuscript M207371200
    • Percherancier Y., Lagane B., Planchenault T., Staropoli I., Altmeyer R., Virelizier J.L., et al. HIV-1 entry into T-cells is not dependent on CD4 and CCR5 localization to sphingolipid-enriched, detergent-resistant, raft membrane domains. J. Biol. Chem. 12:2002;00. epub ahead of printing on Nov. 12 as Manuscript M207371200.
    • (2002) J. Biol. Chem. , vol.12 , pp. 00
    • Percherancier, Y.1    Lagane, B.2    Planchenault, T.3    Staropoli, I.4    Altmeyer, R.5    Virelizier, J.L.6
  • 31
    • 0036148171 scopus 로고    scopus 로고
    • Segregation of CD4 and CXCR4 into distinct lipid microdomains in T lymphocytes suggests a mechanism for membrane destabilization by human immunodeficiency virus
    • Kozak S.L., Heard J.M., Kabat D. Segregation of CD4 and CXCR4 into distinct lipid microdomains in T lymphocytes suggests a mechanism for membrane destabilization by human immunodeficiency virus. J. Virol. 76:2002;1802-1815.
    • (2002) J. Virol. , vol.76 , pp. 1802-1815
    • Kozak, S.L.1    Heard, J.M.2    Kabat, D.3
  • 32
    • 0035978480 scopus 로고    scopus 로고
    • Model for the structure of the HIV gp41 ectodomain: Insight into the intermolecular interactions of the gp41 loop
    • Caffrey M. Model for the structure of the HIV gp41 ectodomain: insight into the intermolecular interactions of the gp41 loop. Biochim. Biophys. Acta. 1536:2001;116-122.
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 116-122
    • Caffrey, M.1
  • 33
    • 0030762020 scopus 로고    scopus 로고
    • The extracellular domain of immunodeficiency virus gp41 protein: Expression in Escherichia coli, purification, and crystallization
    • Wingfield P.T., Stahl S.J., Kaufman J., Zlotnick A., Hyde C.C., Gronenborn A.M., Clore G.M. The extracellular domain of immunodeficiency virus gp41 protein: expression in Escherichia coli, purification, and crystallization. Protein Sci. 6:1997;1653-1660.
    • (1997) Protein Sci. , vol.6 , pp. 1653-1660
    • Wingfield, P.T.1    Stahl, S.J.2    Kaufman, J.3    Zlotnick, A.4    Hyde, C.C.5    Gronenborn, A.M.6    Clore, G.M.7
  • 34
    • 0034142250 scopus 로고    scopus 로고
    • Buried polar interactions and conformational stability in the simian immunodeficiency virus (SIV) gp41 core
    • Ji H., Bracken C., Lu M. Buried polar interactions and conformational stability in the simian immunodeficiency virus (SIV) gp41 core. Biochemistry. 39:2000;676-685.
    • (2000) Biochemistry , vol.39 , pp. 676-685
    • Ji, H.1    Bracken, C.2    Lu, M.3
  • 35
    • 0035814911 scopus 로고    scopus 로고
    • Structural and functional analysis of the HIV gp41 core containing an Ile573 to Thr substitution: Implications for membrane fusion
    • Liu J., Shu W., Fagan M.B., Nunberg J.H., Lu M. Structural and functional analysis of the HIV gp41 core containing an Ile573 to Thr substitution: implications for membrane fusion. Biochemistry. 40:2001;2797-2807.
    • (2001) Biochemistry , vol.40 , pp. 2797-2807
    • Liu, J.1    Shu, W.2    Fagan, M.B.3    Nunberg, J.H.4    Lu, M.5
  • 36
    • 0034695596 scopus 로고    scopus 로고
    • Interactions between HIV-1 gp41 core and detergents and their implications for membrane fusion
    • Shu W., Ji H., Lu M. Interactions between HIV-1 gp41 core and detergents and their implications for membrane fusion. J. Biol. Chem. 275:2000;1839-1845.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1839-1845
    • Shu, W.1    Ji, H.2    Lu, M.3
  • 37
    • 0036889127 scopus 로고    scopus 로고
    • Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion
    • Finnegan C.M., Berg W., Lewis G.K., DeVico A.L. Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion. J. Virol. 76:2002;12123-12134.
    • (2002) J. Virol. , vol.76 , pp. 12123-12134
    • Finnegan, C.M.1    Berg, W.2    Lewis, G.K.3    DeVico, A.L.4
  • 38
    • 0034733546 scopus 로고    scopus 로고
    • Biophysical characterization of gp41 aggregates suggests a model for the molecular mechanism of HIV-associated neurological damage and dementia
    • Caffrey M., Braddock D.T., Louis J.M., Abu-Asab M.A., Kingma D., Liotta L., et al. Biophysical characterization of gp41 aggregates suggests a model for the molecular mechanism of HIV-associated neurological damage and dementia. J. Biol. Chem. 275:2000;19877-19882.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19877-19882
    • Caffrey, M.1    Braddock, D.T.2    Louis, J.M.3    Abu-Asab, M.A.4    Kingma, D.5    Liotta, L.6
  • 39
    • 0029873933 scopus 로고    scopus 로고
    • Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes
    • Gazit E., Miller I.R., Biggin P.C., Sansom M.S., Shai Y. Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes. J. Mol. Biol. 258:1996;860-870.
    • (1996) J. Mol. Biol. , vol.258 , pp. 860-870
    • Gazit, E.1    Miller, I.R.2    Biggin, P.C.3    Sansom, M.S.4    Shai, Y.5
  • 40
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • Surewicz W.K., Mantsch H.H., Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry. 32:1993;389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3


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