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Volumn 3, Issue , 2006, Pages

Antiviral properties of two trimeric recombinant gp41 proteins

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; GLYCOPROTEIN GP 120; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; MEMBRANE PROTEIN; RECOMBINANT GLYCOPROTEIN GP 41A; RECOMBINANT GLYCOPROTEIN GP 41B; UNCLASSIFIED DRUG; VIRUS RECEPTOR; GAG PROTEIN; GLYCOPROTEIN GP 41; RECOMBINANT PROTEIN; VIRUS ENVELOPE PROTEIN;

EID: 33645774712     PISSN: 17424690     EISSN: 17424690     Source Type: Journal    
DOI: 10.1186/1742-4690-3-16     Document Type: Article
Times cited : (6)

References (49)
  • 1
    • 0034304841 scopus 로고    scopus 로고
    • New targets for inhibitors of HIV-1 replication
    • Moore JP, Stevenson M: New targets for inhibitors of HIV-1 replication. Nat Rev Mol Cell Biol 2000, 1(1):40-49.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , Issue.1 , pp. 40-49
    • Moore, J.P.1    Stevenson, M.2
  • 2
    • 0038639554 scopus 로고    scopus 로고
    • HIV and AIDS: 20 years of science
    • Fauci AS: HIV and AIDS: 20 years of science. Nat Med 2003, 9(7):839-843.
    • (2003) Nat Med , vol.9 , Issue.7 , pp. 839-843
    • Fauci, A.S.1
  • 5
    • 0036707268 scopus 로고    scopus 로고
    • Eliminating HIV-1 reservoirs
    • Pomerantz RJ: Eliminating HIV-1 reservoirs. Curr Opin Investig Drugs 2002, 3(8):1133-1137.
    • (2002) Curr Opin Investig Drugs , vol.3 , Issue.8 , pp. 1133-1137
    • Pomerantz, R.J.1
  • 6
    • 3042719556 scopus 로고    scopus 로고
    • Can HIV be cured? Mechanisms of HIV persistence and strategies to combat it
    • Hamer DH: Can HIV be cured? Mechanisms of HIV persistence and strategies to combat it. Curr HIV Res 2004, 2(2):99-111.
    • (2004) Curr HIV Res , vol.2 , Issue.2 , pp. 99-111
    • Hamer, D.H.1
  • 7
    • 0033613070 scopus 로고    scopus 로고
    • Latent reservoirs of HIV: Obstacles to the eradication of virus
    • Chun TW, Fauci AS: Latent reservoirs of HIV: obstacles to the eradication of virus. Proc Natl Acad Sci U S A 1999, 96(20):10958-10961.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.20 , pp. 10958-10961
    • Chun, T.W.1    Fauci, A.S.2
  • 9
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • Wyatt R, Sodroski J: The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 1998, 280(5371):1884-1888.
    • (1998) Science , vol.280 , Issue.5371 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 10
    • 6944223883 scopus 로고    scopus 로고
    • Virus attachment and entry offer numerous targets for antiviral therapy
    • Altmeyer R: Virus attachment and entry offer numerous targets for antiviral therapy. Curr Pharm Des 2004, 10(30)3701-3712.
    • (2004) Curr Pharm Des , vol.10 , Issue.30 , pp. 3701-3712
    • Altmeyer, R.1
  • 11
    • 0036329849 scopus 로고    scopus 로고
    • Cell surface receptors, virus entry and tropism of primate lentiviruses
    • Clapham PR, McKnight A: Cell surface receptors, virus entry and tropism of primate lentiviruses. J Gen Virol 2002, 83(Pt 8):1809-1829.
    • (2002) J Gen Virol , vol.83 , Issue.PART 8 , pp. 1809-1829
    • Clapham, P.R.1    McKnight, A.2
  • 12
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus
    • Gallaher WR: Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell 1987, 50(3):327-328.
    • (1987) Cell , vol.50 , Issue.3 , pp. 327-328
    • Gallaher, W.R.1
  • 13
    • 0025010813 scopus 로고
    • Retroviral envelope glycoproteins contain a 'leucine zipper'-like repeat
    • Delwart EL, Mosialos G, Gilmore T: Retroviral envelope glycoproteins contain a 'leucine zipper'-like repeat. AIDS Res Hum Retroviruses 1990, 6(6):703-706.
    • (1990) AIDS Res Hum Retroviruses , vol.6 , Issue.6 , pp. 703-706
    • Delwart, E.L.1    Mosialos, G.2    Gilmore, T.3
  • 14
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers P, Pringle CR, Easton AJ: Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J Gen Virol 1990, 71 (Pt 12):3075-3080.
    • (1990) J Gen Virol , vol.71 , Issue.PART 12 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 15
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS: Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997, 89(2):263-273.
    • (1997) Cell , vol.89 , Issue.2 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 16
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M, Blacklow SC, Kim PS: A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat Struct Biol 1995, 2(12):1075-1082.
    • (1995) Nat Struct Biol , vol.2 , Issue.12 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 17
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan K, Liu J, Wang J, Shen S, Lu M: Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc Natl Acad Sci U S A 1997, 94(23):12303-12308.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , Issue.23 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 19
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert DM, Kim PS: Mechanisms of viral membrane fusion and its inhibition. Annu Rev Biochem 2001, 70:777-810.
    • (2001) Annu Rev Biochem , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 21
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan DC, Kim PS: HIV entry and its inhibition. Cell 1998, 93(5):681-684.
    • (1998) Cell , vol.93 , Issue.5 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 22
    • 0037301373 scopus 로고    scopus 로고
    • Peptides trap the human immunodeficiency virus type 1 envelope glycoprotein fusion intermediate at two sites
    • He Y, Vassell R, Zaitseva M, Nguyen N, Yang Z, Weng Y, Weiss CD: Peptides trap the human immunodeficiency virus type 1 envelope glycoprotein fusion intermediate at two sites. J Virol 2003, 77(3):1666-1671.
    • (2003) J Virol , vol.77 , Issue.3 , pp. 1666-1671
    • He, Y.1    Vassell, R.2    Zaitseva, M.3    Nguyen, N.4    Yang, Z.5    Weng, Y.6    Weiss, C.D.7
  • 23
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky LT, Shugars DC, Matthews TJ: Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J Virol 1998, 72(2):986-993.
    • (1998) J Virol , vol.72 , Issue.2 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 24
    • 0035949493 scopus 로고    scopus 로고
    • Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
    • Eckert DM, Kim PS: Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. Proc Natl Acad Sci U S A 2001, 98(20):11187-11192.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.20 , pp. 11187-11192
    • Eckert, D.M.1    Kim, P.S.2
  • 25
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root MJ, Kay MS, Kim PS: Protein design of an HIV-1 entry inhibitor. Science 2001, 291(5505):884-888.
    • (2001) Science , vol.291 , Issue.5505 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 27
    • 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 CT, Shugars DC, Greenwell TK, McDanal CB, Matthews TJ: 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 U S A 1994, 91(21):9770-9774.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , Issue.21 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 29
    • 0034645796 scopus 로고    scopus 로고
    • Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation
    • Kliger Y, Shai Y: Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation. J Mol Biol 2000, 295(2):163-168.
    • (2000) J Mol Biol , vol.295 , Issue.2 , pp. 163-168
    • Kliger, Y.1    Shai, Y.2
  • 31
    • 0033856458 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120
    • Derdeyn CA, Decker JM, Sfakianos JN, Wu X, O'Brien WA, Ratner L, Kappes JC, Shaw GM, Hunter E: Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120. J Virol 2000, 74(18):8358-8367.
    • (2000) J Virol , vol.74 , Issue.18 , pp. 8358-8367
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3    Wu, X.4    O'Brien, W.A.5    Ratner, L.6    Kappes, J.C.7    Shaw, G.M.8    Hunter, E.9
  • 32
    • 0034890660 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor
    • Derdeyn CA, Decker JM, Sfakianos JN, Zhang Z, O'Brien WA, Ratner L, Shaw GM, Hunter E: Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor. J Virol 2001, 75(18):8605-8614.
    • (2001) J Virol , vol.75 , Issue.18 , pp. 8605-8614
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3    Zhang, Z.4    O'Brien, W.A.5    Ratner, L.6    Shaw, G.M.7    Hunter, E.8
  • 33
    • 2342466810 scopus 로고    scopus 로고
    • CD4-induced T-20 binding to human immunodeficiency virus type 1 gp120 blocks interaction with the CXCR4 coreceptor
    • Yuan W, Craig S, Si Z, Farzan M, Sodroski J: CD4-induced T-20 binding to human immunodeficiency virus type 1 gp120 blocks interaction with the CXCR4 coreceptor. J Virol 2004, 78(10):5448-5457.
    • (2004) J Virol , vol.78 , Issue.10 , pp. 5448-5457
    • Yuan, W.1    Craig, S.2    Si, Z.3    Farzan, M.4    Sodroski, J.5
  • 34
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 virions induced by soluble CD4
    • Moore JP, McKeating JA, Weiss RA, Sattentau QJ: Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 1990, 250(4984):1139-1142.
    • (1990) Science , vol.250 , Issue.4984 , pp. 1139-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 35
    • 0026011315 scopus 로고
    • Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120
    • Hart TK, Kirsh R, Ellens H, Sweet RW, Lambert DM, Petteway SRJ, Leary J, Bugelski PJ: Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120. Proc Natl Acad Sci U S A 1991, 88(6):2189-2193.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , Issue.6 , pp. 2189-2193
    • Hart, T.K.1    Kirsh, R.2    Ellens, H.3    Sweet, R.W.4    Lambert, D.M.5    Petteway, S.R.J.6    Leary, J.7    Bugelski, P.J.8
  • 36
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau QJ, Moore JP: Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. J Exp Med 1991, 174(2):407-415.
    • (1991) J Exp Med , vol.174 , Issue.2 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 37
    • 0346688617 scopus 로고    scopus 로고
    • Role of the ectodomain of the gp41 transmembrane envelope protein of human immunodeficiency virus type 1 in late steps of the membrane fusion process
    • Bar S, Alizon M: Role of the ectodomain of the gp41 transmembrane envelope protein of human immunodeficiency virus type 1 in late steps of the membrane fusion process. J Virol 2004, 78(2):811-820.
    • (2004) J Virol , vol.78 , Issue.2 , pp. 811-820
    • Bar, S.1    Alizon, M.2
  • 38
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta RA, Wild CT, Weng Y, Weiss CD: Capture of an early fusion-active conformation of HIV-1 gp41. Nat Struct Biol 1998, 5(4):276-279.
    • (1998) Nat Struct Biol , vol.5 , Issue.4 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 39
    • 0032899254 scopus 로고    scopus 로고
    • Subdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: Implications for viral membrane fusion
    • Lu M, Ji H, Shen S: Subdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: implications for viral membrane fusion. J Virol 1999, 73(5):4433-4438.
    • (1999) J Virol , vol.73 , Issue.5 , pp. 4433-4438
    • Lu, M.1    Ji, H.2    Shen, S.3
  • 40
    • 0032850583 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: Role of a conserved hydrophobic cavity in membrane fusion
    • Ji H, Shu W, Burling FT, Jiang S, Lu M: Inhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: role of a conserved hydrophobic cavity in membrane fusion. J Virol 1999, 73(10):8578-8586.
    • (1999) J Virol , vol.73 , Issue.10 , pp. 8578-8586
    • Ji, H.1    Shu, W.2    Burling, F.T.3    Jiang, S.4    Lu, M.5
  • 42
    • 0033600836 scopus 로고    scopus 로고
    • The anti-HIV pseudopeptide HB-19 forms a complex with the cell-surface-expressed nucleolin independent of heparan sulfate proteoglycans
    • Nisole S, Krust B, Callebaut C, Guichard G, Muller S, Briand JP, Hovanessian AG: The anti-HIV pseudopeptide HB-19 forms a complex with the cell-surface-expressed nucleolin independent of heparan sulfate proteoglycans. J Biol Chem 1999, 274(39):27875-27884.
    • (1999) J Biol Chem , vol.274 , Issue.39 , pp. 27875-27884
    • Nisole, S.1    Krust, B.2    Callebaut, C.3    Guichard, G.4    Muller, S.5    Briand, J.P.6    Hovanessian, A.G.7
  • 43
    • 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, Jiang S: 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 2005, 280(12):11259-11273.
    • (2005) J Biol Chem , vol.280 , Issue.12 , pp. 11259-11273
    • Liu, S.1    Lu, H.2    Niu, J.3    Xu, Y.4    Wu, S.5    Jiang, S.6
  • 45
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Munoz-Barroso I, Durell S, Sakaguchi K, Appella E, Blumenthal R: Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41. J Cell Biol 1998, 140(2):315-323.
    • (1998) J Cell Biol , vol.140 , Issue.2 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 46
    • 0037340005 scopus 로고    scopus 로고
    • HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation
    • Markosyan RM, Cohen FS, Melikyan GB: HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation. Mol Biol Cell 2003, 14(3):926-938.
    • (2003) Mol Biol Cell , vol.14 , Issue.3 , pp. 926-938
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 47
    • 0035800816 scopus 로고    scopus 로고
    • Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity
    • Louis JM, Bewley CA, Clore GM: Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity. J Biol Chem 2001, 276(31):29485-29489.
    • (2001) J Biol Chem , vol.276 , Issue.31 , pp. 29485-29489
    • Louis, J.M.1    Bewley, C.A.2    Clore, G.M.3
  • 48
    • 0031575431 scopus 로고    scopus 로고
    • Change in coreceptor use correlates with disease progression in HIV-1-infected individuals
    • 1114 First Ave, 4TH Fl, New York, NY 10021, Rockefeller Univ Press
    • Connor RI, Sheridan KE, Ceradini D, Choe S, Landau NR: Change in coreceptor use correlates with disease progression in HIV-1-infected individuals. In J Exp Med Volume 185. Issue 4 1114 First Ave, 4TH Fl, New York, NY 10021, Rockefeller Univ Press; 1997:621-628.
    • (1997) J Exp Med , vol.185 , Issue.4 , pp. 621-628
    • Connor, R.I.1    Sheridan, K.E.2    Ceradini, D.3    Choe, S.4    Landau, N.R.5
  • 49
    • 0031985314 scopus 로고    scopus 로고
    • Spontaneous mutations in the env gene of the human immunodeficiency virus type 1 NDK isolate are associated with a CD4-independent entry phenotype
    • Dumonceaux J, Nisole S, Chanel C, Quivet L, Amara A, Baleux F, Briand P, Hazan U: Spontaneous mutations in the env gene of the human immunodeficiency virus type 1 NDK isolate are associated with a CD4-independent entry phenotype. J Virol 1998, 72(1):512-519.
    • (1998) J Virol , vol.72 , Issue.1 , pp. 512-519
    • Dumonceaux, J.1    Nisole, S.2    Chanel, C.3    Quivet, L.4    Amara, A.5    Baleux, F.6    Briand, P.7    Hazan, U.8


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