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Volumn 49, Issue 3, 2005, Pages 1113-1119

Emergence and evolution of enfuvirtide resistance following long-term therapy involves heptad repeat 2 mutations within gp41

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; ANTIRETROVIRUS AGENT; ENFUVIRTIDE; GLUTAMINE; GLYCOPROTEIN GP 41; HISTIDINE; SERINE;

EID: 20044371998     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.49.3.1113-1119.2005     Document Type: Article
Times cited : (159)

References (38)
  • 1
    • 0027499917 scopus 로고
    • Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein
    • Cao, J., L. Bergeron, E. Helseth, M. Thali, H. Repke, and J. Sodroski. 1993. Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein. J. Virol. 67:2747-2755.
    • (1993) J. Virol. , vol.67 , pp. 2747-2755
    • Cao, J.1    Bergeron, L.2    Helseth, E.3    Thali, M.4    Repke, H.5    Sodroski, J.6
  • 2
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers, P., C. R. Pringle, and A. J. Easton. 1990. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 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
  • 3
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan, D. C., D. Fass, J. M. Berger, and P. S. Kim. 1998. HIV entry and its inhibition. Cell 93:681-684.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 4
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., D. Fass, J. M. Berger, and P. S. Kim. 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
  • 5
    • 0029072191 scopus 로고
    • A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: Implication for viral fusion
    • Chen, C. H., T. J. Matthews, C. B. McDanal, D. P. Bolognesi, and M. L. Greenberg. 1995. A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion. J. Virol. 69:3771-3777.
    • (1995) J. Virol. , vol.69 , pp. 3771-3777
    • Chen, C.H.1    Matthews, T.J.2    McDanal, C.B.3    Bolognesi, D.P.4    Greenberg, M.L.5
  • 6
    • 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, C. A., J. M. Decker, J. N. Sfakianos, Z. Zhang, W. A. O'Brien, L. Ratner, G. M. Shaw, and E. Hunter. 2001. 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. 75:8605-8614.
    • (2001) J. Virol. , vol.75 , 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
  • 7
    • 17044442276 scopus 로고    scopus 로고
    • Analysis of genetic variability within the immunodominant epitopes of envelope gp41 from human immunodeficiency virus type 1 (HIV-1) group M and its impact on HIV-1 antibody detection
    • Dorn, J., S. Masciotra, C. Yang, R. Downing, B. Biryahwaho, T. D. Mastro, J. Nkengasong, D. Pieniazek, M. A. Rayfield, D. J. Hu, and R. B. Lal. 2000. Analysis of genetic variability within the immunodominant epitopes of envelope gp41 from human immunodeficiency virus type 1 (HIV-1) group M and its impact on HIV-1 antibody detection. J. Clin. Microbiol. 38:773-780.
    • (2000) J. Clin. Microbiol. , vol.38 , pp. 773-780
    • Dorn, J.1    Masciotra, S.2    Yang, C.3    Downing, R.4    Biryahwaho, B.5    Mastro, T.D.6    Nkengasong, J.7    Pieniazek, D.8    Rayfield, M.A.9    Hu, D.J.10    Lal, R.B.11
  • 10
    • 0037119035 scopus 로고    scopus 로고
    • Resistance mutation in HIV entry inhibitors
    • Hanna, S. L., C. Yang, S. M. Owen, and R. B. Lai. 2002. Resistance mutation in HIV entry inhibitors. AIDS 16:1603-1608.
    • (2002) AIDS , vol.16 , pp. 1603-1608
    • Hanna, S.L.1    Yang, C.2    Owen, S.M.3    Lai, R.B.4
  • 11
    • 0026069632 scopus 로고
    • Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein
    • Helseth, E., U. Olshevsky, C. Furman, and J. Sodroski. 1991. Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein. J. Virol. 65:2119-2123.
    • (1991) J. Virol. , vol.65 , pp. 2119-2123
    • Helseth, E.1    Olshevsky, U.2    Furman, C.3    Sodroski, J.4
  • 13
    • 0034466833 scopus 로고    scopus 로고
    • Evolution of the human immunodeficiency virus type 1 envelope during infection reveals molecular corollaries of specificity for coreceptor utilization and AIDS pathogenesis
    • Hu, Q. X., A. P. Barry, Z. X. Wang, S. M. Connolly, S. C. Peiper, and M. L. Greenberg. 2000. Evolution of the human immunodeficiency virus type 1 envelope during infection reveals molecular corollaries of specificity for coreceptor utilization and AIDS pathogenesis. J. Virol. 74:11858-11872.
    • (2000) J. Virol. , vol.74 , pp. 11858-11872
    • Hu, Q.X.1    Barry, A.P.2    Wang, Z.X.3    Connolly, S.M.4    Peiper, S.C.5    Greenberg, M.L.6
  • 15
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones, S., and J. M. Thornton. 1996. Principles of protein-protein interactions. Proc. Natl. Acad. Sci. USA 93:13-20.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 21
    • 0035800816 scopus 로고    scopus 로고
    • Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity
    • Louis, J. M., C. A. Bewley, and G. M. Clore. 2001. Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity. J. Biol. Chem. 276:29485-29489.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29485-29489
    • Louis, J.M.1    Bewley, C.A.2    Clore, G.M.3
  • 22
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan, A. D., and M. Stewart. 1975. Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98:293-304.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 23
    • 0037183892 scopus 로고    scopus 로고
    • Evolution of the gp41 env region in HIV-infected patients receiving T-20, a fusion inhibitor
    • Poveda, E., B. Rodes, C. Toro, L. Martin-Carbonero, J. Gonzalez-Lahoz, and V. Soriano. 2002. Evolution of the gp41 env region in HIV-infected patients receiving T-20, a fusion inhibitor. AIDS 27:1959-1961.
    • (2002) AIDS , vol.27 , pp. 1959-1961
    • Poveda, E.1    Rodes, B.2    Toro, C.3    Martin-Carbonero, L.4    Gonzalez-Lahoz, J.5    Soriano, V.6
  • 24
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky, L. T., D. C. Shugars, and T. J. Matthews. 1998. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 72:986-993.
    • (1998) J. Virol. , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 26
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root, M. J., M. S. Kay, and P. S. Kim. 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
  • 27
    • 0012885271 scopus 로고    scopus 로고
    • Characterization of baseline and treatment-emergent resistance to T-20 (enfuvirtide) observed in phase II clinical trials: Substitutions in gp41 amino acids 36-45 and enfuvirtide susceptibility of virus isolates
    • Sista, P., T. Melby, M. L. Greenberg, D. Davison, L. Jin, S. Mosier, et al. 2002. Characterization of baseline and treatment-emergent resistance to T-20 (enfuvirtide) observed in phase II clinical trials: substitutions in gp41 amino acids 36-45 and enfuvirtide susceptibility of virus isolates. Antivir. Ther. 7:S16.
    • (2002) Antivir. Ther. , vol.7
    • Sista, P.1    Melby, T.2    Greenberg, M.L.3    Davison, D.4    Jin, L.5    Mosier, S.6
  • 33
    • 0027692502 scopus 로고
    • A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion
    • Wild, C., T. Greenwell, and T. Matthews. 1993. A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion. AIDS Res. Hum. Retrovir. 9:1051-1053.
    • (1993) AIDS Res. Hum. Retrovir. , vol.9 , pp. 1051-1053
    • Wild, C.1    Greenwell, T.2    Matthews, T.3
  • 34
    • 0028953212 scopus 로고
    • The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure
    • Wild, C., T. Greenwell, D. Shugars, L. Rimsky-Clarke, and T. Matthews. 1995. The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure. AIDS Res. Hum. Retrovir. 11:323-325.
    • (1995) AIDS Res. Hum. Retrovir. , vol.11 , pp. 323-325
    • Wild, C.1    Greenwell, T.2    Shugars, D.3    Rimsky-Clarke, L.4    Matthews, T.5
  • 35
    • 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., D. C. Shugars, T. K. Greenwell, C. B. McDanal, and T. J. Matthews. 1994. 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 91:9770-9774.
    • (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
  • 36
    • 0037119027 scopus 로고    scopus 로고
    • Minimal variation in T-20 binding domain of different HIV-1 subtypes from antiretroviral-naive and -experienced patients
    • Xu, L., S. Hue, S. Taylor, D. Ratcliffe, J. A. Workman, S. Jackson, P. A. Cane, and D. Pillay. 2002. Minimal variation in T-20 binding domain of different HIV-1 subtypes from antiretroviral-naive and -experienced patients. AIDS 16:1684-1686.
    • (2002) AIDS , vol.16 , pp. 1684-1686
    • Xu, L.1    Hue, S.2    Taylor, S.3    Ratcliffe, D.4    Workman, J.A.5    Jackson, S.6    Cane, P.A.7    Pillay, D.8
  • 37
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young, L., R. L. Jernigan, and D. G. Covell. 1994. A role for surface hydrophobicity in protein-protein recognition. Protein Sci. 3:717-729.
    • (1994) Protein Sci. , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 38
    • 0035805185 scopus 로고    scopus 로고
    • Primary genotypic resistance of HIV-1 to the fusion inhibitor T-20 in long-term infected patients
    • Zollner, B., H. H. Feucht, M. Schroter, P. Schafer, A. Plettenberg, A. Stoehr, and R. Laufs. 2001. Primary genotypic resistance of HIV-1 to the fusion inhibitor T-20 in long-term infected patients. AIDS 15:935-936.
    • (2001) AIDS , vol.15 , pp. 935-936
    • Zollner, B.1    Feucht, H.H.2    Schroter, M.3    Schafer, P.4    Plettenberg, A.5    Stoehr, A.6    Laufs, R.7


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