메뉴 건너뛰기




Volumn 24, Issue 11, 2010, Pages 4196-4202

Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain

Author keywords

HIV 1 entry inhibitor; Membrane fusion; Peptide membrane interaction; Viral envelope protein

Indexed keywords

ENVELOPE PROTEIN; FATTY ACID; GLYCOPROTEIN GP 41; LIPOPEPTIDE;

EID: 78649829342     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.09-151704     Document Type: Article
Times cited : (28)

References (37)
  • 1
    • 0036317971 scopus 로고    scopus 로고
    • Oligomeric structure of the human immunodeficiency virus type 1 envelope protein on the virion surface
    • DOI 10.1128/JVI.76.15.7863-7867.2002
    • Center, R. J., Leapman, R. D., Lebowitz, J., Arthur, L. O., Earl, P. L., and Moss, B. (2002) Oligomeric structure of the human immunodeficiency virus type 1 envelope protein on the virion surface. J. Virol. 76, 7863-7867 (Pubitemid 34761009)
    • (2002) Journal of Virology , vol.76 , Issue.15 , pp. 7863-7867
    • Center, R.J.1    Leapman, R.D.2    Lebowitz, J.3    Arthur, L.O.4    Earl, P.L.5    Moss, B.6
  • 2
    • 0035955695 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant HIV gp140: The gp41 ectodomain of HIV or simian immunodeficiency virus is sufficient to maintain the retroviral envelope glycoprotein as a trimer
    • Zhang, C. W., Chishti, Y., Hussey, R. E., and Reinherz, E. L. (2001) Expression, purification, and characterization of recombinant HIV gp140: the gp41 ectodomain of HIV or simian immunodeficiency virus is sufficient to maintain the retroviral envelope glycoprotein as a trimer. J. Biol. Chem. 276, 39577-39585
    • (2001) J. Biol. Chem. , vol.276 , pp. 39577-39585
    • Zhang, C.W.1    Chishti, Y.2    Hussey, R.E.3    Reinherz, E.L.4
  • 4
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • DOI 10.1080/10409230802058320, PII 794225034
    • White, J. M., Delos, S. E., Brecher, M., and Schornberg, K. (2008) Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43, 189-219 (Pubitemid 351883153)
    • (2008) Critical Reviews in Biochemistry and Molecular Biology , vol.43 , Issue.3 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 5
    • 1842612607 scopus 로고    scopus 로고
    • Virus entry: Molecular mechanisms and biomedical applications
    • DOI 10.1038/nrmicro817
    • Dimitrov, D. S. (2004) Virus entry: molecular mechanisms and biomedical applications. Nat. Rev. Microbiol. 2, 109-122 (Pubitemid 39490065)
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.2 , pp. 109-122
    • Dimitrov, D.S.1
  • 7
    • 0036329849 scopus 로고    scopus 로고
    • Cell surface receptors, virus entry and tropism of primate lentiviruses
    • Clapham, P. R., and McKnight, A. (2002) Cell surface receptors, virus entry and tropism of primate lentiviruses. J. Gen. Virol. 83, 1809-1829
    • (2002) J. Gen. Virol. , vol.83 , pp. 1809-1829
    • Clapham, P.R.1    McKnight, A.2
  • 8
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan, D. C., and Kim, P. S. (1998) HIV entry and its inhibition. Cell 93, 681-684
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 9
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman, P. M., and Lawrence, M. C. (2003) The structural biology of type I viral membrane fusion. Nat. Rev. Mol. Cell. Biol. 4, 309-319
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 10
    • 0028218423 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage
    • Nieva, J. L., Nir, S., Muga, A., Goni, F. M., and Wilschut, J. (1994) Interaction of the HIV-1 fusion peptide with phospholipid vesicles: different structural requirements for fusion and leakage. Biochemistry 33, 3201-3209 (Pubitemid 24112630)
    • (1994) Biochemistry , vol.33 , Issue.11 , pp. 3201-3209
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goni, F.M.4    Wilschut, J.5
  • 11
    • 0345060499 scopus 로고    scopus 로고
    • Role of the fusion peptide and membrane-proximal domain in HIV-1 envelope glycoprotein-mediated membrane fusion
    • Dimitrov, A. S., Rawat, S. S., Jiang, S., and Blumenthal, R. (2003) Role of the fusion peptide and membrane-proximal domain in HIV-1 envelope glycoprotein-mediated membrane fusion. Biochemistry 42, 14150-14158
    • (2003) Biochemistry , vol.42 , pp. 14150-14158
    • Dimitrov, A.S.1    Rawat, S.S.2    Jiang, S.3    Blumenthal, R.4
  • 12
    • 33645230933 scopus 로고    scopus 로고
    • Membrane-anchored inhibitory peptides capture human immunodeficiency virus type 1 gp41 conformations that engage the target membrane prior to fusion
    • Melikyan, G. B., Egelhofer, M., and von Laer, D. (2006) Membrane-anchored inhibitory peptides capture human immunodeficiency virus type 1 gp41 conformations that engage the target membrane prior to fusion. J. Virol. 80, 3249-3258
    • (2006) J. Virol. , vol.80 , pp. 3249-3258
    • Melikyan, G.B.1    Egelhofer, M.2    Von Laer, D.3
  • 13
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., Fass, D., Berger, J. M., and Kim, P. S. (1997) Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263-273
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 14
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel, J. J., and Wiley, D. C. (1998) Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 95, 871-874
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 15
    • 3142510881 scopus 로고    scopus 로고
    • Intracellular and viral membrane fusion: A uniting mechanism
    • Sollner, T. H. (2004) Intracellular and viral membrane fusion: a uniting mechanism. Curr. Opin. Cell Biol. 16, 429-435
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 429-435
    • Sollner, T.H.1
  • 16
    • 21244478580 scopus 로고    scopus 로고
    • The fusion activity of HIV-1 gp41 depends on interhelical interactions
    • Suntoke, T. R., and Chan, D. C. (2005) The fusion activity of HIV-1 gp41 depends on interhelical interactions. J. Biol. Chem. 280, 19852-19857
    • (2005) J. Biol. Chem. , vol.280 , pp. 19852-19857
    • Suntoke, T.R.1    Chan, D.C.2
  • 18
    • 0038467539 scopus 로고    scopus 로고
    • Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope
    • Kilgore, N. R., Salzwedel, K., Reddick, M., Allaway, G. P., and Wild, C. T. (2003) Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope. J. Virol. 77, 7669-7672
    • (2003) J. Virol. , vol.77 , pp. 7669-7672
    • Kilgore, N.R.1    Salzwedel, K.2    Reddick, M.3    Allaway, G.P.4    Wild, C.T.5
  • 19
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root, M. J., Kay, M. S., and Kim, P. S. (2001) Protein design of an HIV-1 entry inhibitor. Science 291, 884-888
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 20
    • 15744393651 scopus 로고    scopus 로고
    • Different from the HIV fusion inhibitor C34, the anti-HIV drug Fuzeon (T-20) inhibits HIV-1 entry by targeting multiple sites in gp41 and gp120
    • Liu, S., Lu, H., Niu, J., Xu, Y., Wu, S., and Jiang, S. (2005) Different from the HIV fusion inhibitor C34, the anti-HIV drug Fuzeon (T-20) inhibits HIV-1 entry by targeting multiple sites in gp41 and gp120. J. Biol. Chem. 280, 11259-11273
    • (2005) J. Biol. Chem. , vol.280 , pp. 11259-11273
    • Liu, S.1    Lu, H.2    Niu, J.3    Xu, Y.4    Wu, S.5    Jiang, S.6
  • 21
    • 0035949493 scopus 로고    scopus 로고
    • Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
    • Eckert, D. M., and Kim, P. S. (2001) Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. Proc. Natl. Acad. Sci. U. S. A. 98, 11187-11192
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11187-11192
    • Eckert, D.M.1    Kim, P.S.2
  • 22
    • 0038047695 scopus 로고    scopus 로고
    • Enfuvirtide approved for defusing HIV
    • Burton, A. (2003) Enfuvirtide approved for defusing HIV. Lancet Infect. Dis. 3, 260-269
    • (2003) Lancet Infect. Dis. , vol.3 , pp. 260-269
    • Burton, A.1
  • 23
    • 0021245601 scopus 로고
    • The role of T3 surface molecules in the activation of human T cells: A twostimulus requirement for IL 2 production reflects events occurring at a pre-translational level
    • Weiss, A., Wiskocil, R. L., and Stobo, J. D. (1984) The role of T3 surface molecules in the activation of human T cells: a twostimulus requirement for IL 2 production reflects events occurring at a pre-translational level. J. Immunol. 133, 123-128
    • (1984) J. Immunol. , vol.133 , pp. 123-128
    • Weiss, A.1    Wiskocil, R.L.2    Stobo, J.D.3
  • 24
    • 0030053308 scopus 로고    scopus 로고
    • Molecular determinants of acute single-cell lysis by human immunodeficiency virus type 1
    • Cao, J., Park, I. W., Cooper, A., and Sodroski, J. (1996) Molecular determinants of acute single-cell lysis by human immunodeficiency virus type 1. J. Virol. 70, 1340-1354
    • (1996) J. Virol. , vol.70 , pp. 1340-1354
    • Cao, J.1    Park, I.W.2    Cooper, A.3    Sodroski, J.4
  • 25
    • 0020395778 scopus 로고
    • Synthesis of the antibacterial peptide cecropin A (1-33)
    • Merrifield, R. B., Vizioli, L. D., and Boman, H. G. (1982) Synthesis of the antibacterial peptide cecropin A (1-33). Biochemistry 21, 5020-5031
    • (1982) Biochemistry , vol.21 , pp. 5020-5031
    • Merrifield, R.B.1    Vizioli, L.D.2    Boman, H.G.3
  • 26
    • 70049117718 scopus 로고    scopus 로고
    • Membrane-anchored HIV-1 N-heptad repeat peptides are highly potent cell fusion inhibitors via an altered mode of action
    • Wexler-Cohen, Y., and Shai, Y. (2009) Membrane-anchored HIV-1 N-heptad repeat peptides are highly potent cell fusion inhibitors via an altered mode of action. PLoS Pathog. 5, e1000509
    • (2009) PLoS Pathog. , vol.5
    • Wexler-Cohen, Y.1    Shai, Y.2
  • 27
    • 35948978102 scopus 로고    scopus 로고
    • Demonstrating the C-terminal boundary of the HIV 1 fusion conformation in a dynamic ongoing fusion process and implication for fusion inhibition
    • Wexler-Cohen, Y., and Shai, Y. (2007) Demonstrating the C-terminal boundary of the HIV 1 fusion conformation in a dynamic ongoing fusion process and implication for fusion inhibition. FASEB J. 21, 3677-3684
    • (2007) FASEB J. , vol.21 , pp. 3677-3684
    • Wexler-Cohen, Y.1    Shai, Y.2
  • 28
    • 0037134497 scopus 로고    scopus 로고
    • Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41
    • Bewley, C. A., Louis, J. M., Ghirlando, R., and Clore, G. M. (2002) Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. J. Biol. Chem. 277, 14238-14245
    • (2002) J. Biol. Chem. , vol.277 , pp. 14238-14245
    • Bewley, C.A.1    Louis, J.M.2    Ghirlando, R.3    Clore, G.M.4
  • 29
    • 56849129238 scopus 로고    scopus 로고
    • Peptide P5 (residues 628-683), comprising the entire membrane proximal region of HIV-1 gp41 and its calcium-binding site, is a potent inhibitor of HIV-1 infection
    • Yu, H., Tudor, D., Alfsen, A., Labrosse, B., Clavel, F., and Bomsel, M. (2008) Peptide P5 (residues 628-683), comprising the entire membrane proximal region of HIV-1 gp41 and its calcium-binding site, is a potent inhibitor of HIV-1 infection. Retrovirology 5, 93-105
    • (2008) Retrovirology , vol.5 , pp. 93-105
    • Yu, H.1    Tudor, D.2    Alfsen, A.3    Labrosse, B.4    Clavel, F.5    Bomsel, M.6
  • 30
    • 45749112585 scopus 로고    scopus 로고
    • Identification of a critical motif for the human immunodeficiency virus type 1 (HIV-1) gp41 core structure: Implications for designing novel anti-HIV fusion inhibitors
    • He, Y., Cheng, J., Li, J., Qi, Z., Lu, H., Dong, M., Jiang, S., and Dai, Q. (2008) Identification of a critical motif for the human immunodeficiency virus type 1 (HIV-1) gp41 core structure: implications for designing novel anti-HIV fusion inhibitors. J. Virol. 82, 6349-6358
    • (2008) J. Virol. , vol.82 , pp. 6349-6358
    • He, Y.1    Cheng, J.2    Li, J.3    Qi, Z.4    Lu, H.5    Dong, M.6    Jiang, S.7    Dai, Q.8
  • 31
    • 46049107703 scopus 로고    scopus 로고
    • The membrane proximal external region of the HIV-1 envelope glycoprotein gp41 contributes to the stabilization of the six-helix bundle formed with a matching N′ peptide
    • Noah, E., Biron, Z., Naider, F., Arshava, B., and Anglister, J. (2008) The membrane proximal external region of the HIV-1 envelope glycoprotein gp41 contributes to the stabilization of the six-helix bundle formed with a matching N′ peptide. Biochemistry 47, 6782-6792
    • (2008) Biochemistry , vol.47 , pp. 6782-6792
    • Noah, E.1    Biron, Z.2    Naider, F.3    Arshava, B.4    Anglister, J.5
  • 33
    • 33646185493 scopus 로고    scopus 로고
    • Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells
    • Yang, X., Kurteva, S., Ren, X., Lee, S., and Sodroski, J. (2006) Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells. J. Virol. 80, 4388-4395
    • (2006) J. Virol. , vol.80 , pp. 4388-4395
    • Yang, X.1    Kurteva, S.2    Ren, X.3    Lee, S.4    Sodroski, J.5
  • 35
    • 24344437154 scopus 로고    scopus 로고
    • HIV-1-infected blood mononuclear cells form an integrin- and agrin-dependent viral synapse to induce efficient HIV-1 transcytosis across epithelial cell monolayer
    • Alfsen, A., Yu, H., Magerus-Chatinet, A., Schmitt, A., and Bomsel, M. (2005) HIV-1-infected blood mononuclear cells form an integrin- and agrin-dependent viral synapse to induce efficient HIV-1 transcytosis across epithelial cell monolayer. Mol. Biol. Cell 16, 4267-4279
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4267-4279
    • Alfsen, A.1    Yu, H.2    Magerus-Chatinet, A.3    Schmitt, A.4    Bomsel, M.5
  • 36
    • 0037490139 scopus 로고    scopus 로고
    • Covalent trimers of the internal N-terminal trimeric coiled-coil of gp41 and antibodies directed against them are potent inhibitors of HIV envelope-mediated cell fusion
    • Louis, J. M., Nesheiwat, I., Chang, L., Clore, G. M., and Bewley, C. A. (2003) Covalent trimers of the internal N-terminal trimeric coiled-coil of gp41 and antibodies directed against them are potent inhibitors of HIV envelope-mediated cell fusion. J. Biol. Chem. 278, 20278-20285
    • (2003) J. Biol. Chem. , vol.278 , pp. 20278-20285
    • Louis, J.M.1    Nesheiwat, I.2    Chang, L.3    Clore, G.M.4    Bewley, C.A.5
  • 37
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild, C., Oas, T., McDanal, C., Bolognesi, D., and Matthews, T. (1992) A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. U. S. A. 89, 10537-10541
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.