메뉴 건너뛰기




Volumn 47, Issue 25, 2008, Pages 6662-6670

Impact of the enfuvirtide resistance mutation N43D and the associated baseline polymorphism E137K on peptide sensitivity and six-helix bundle structure

Author keywords

[No Author keywords available]

Indexed keywords

AMERICAN CHEMICAL SOCIETY (ACS); ANTIVIRAL ACTIVITIES; CIRCULAR DICHROISM (DC); CLINICAL USES; HELICITY; HELIX BUNDLES; HUMAN IMMUNODEFICIENCY VIRUS TYPE-1 (HIV-1); IN-VITRO ASSAYS; ION PAIRS; LOSS OF STABILITY; MUTATION RESULTS; PEPTIDE MODELS; THERMAL STABILITY; VIRAL FITNESS; X RAY CRYSTALLOGRAPHY;

EID: 45749147766     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702509d     Document Type: Article
Times cited : (30)

References (36)
  • 1
    • 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
  • 2
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive α-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., and Matthews, T. J. (1994) Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. U.S.A. 91, 9770-9774.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , 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
  • 3
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky, L. T., Shugars, D. C., and Matthews, T. J. (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
  • 4
    • 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., Decker, J. M., Sfakianos, J. N., Zhang, Z., O'Brien, W. A., Ratner, L., Shaw, G. M., and Hunter, E. (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
  • 5
    • 4444375658 scopus 로고    scopus 로고
    • Resistance to enfuvirtide, the first HIV fusion inhibitor
    • Greenberg, M. L., and Cammack, N. (2004) Resistance to enfuvirtide, the first HIV fusion inhibitor. J. Antimicrob. Chemother. 54, 333-340.
    • (2004) J. Antimicrob. Chemother , vol.54 , pp. 333-340
    • Greenberg, M.L.1    Cammack, N.2
  • 8
    • 33646868062 scopus 로고    scopus 로고
    • Characterization of envelope glycoprotein gp41 genotype and phenotypic susceptibility to enfuvirtide at baseline and on treatment in the phase III clinical trials TORO-1 and TORO-2
    • Melby, T., Sista, P., DeMasi, R., Kirkland, T., Roberts, N., Salgo, M., Heilek-Snyder, G., Cammack, N., Matthews, T. J., and Greenberg, M. L. (2006) Characterization of envelope glycoprotein gp41 genotype and phenotypic susceptibility to enfuvirtide at baseline and on treatment in the phase III clinical trials TORO-1 and TORO-2. AIDS Res. Hum. Retroviruses 22, 375-385.
    • (2006) AIDS Res. Hum. Retroviruses , vol.22 , pp. 375-385
    • Melby, T.1    Sista, P.2    DeMasi, R.3    Kirkland, T.4    Roberts, N.5    Salgo, M.6    Heilek-Snyder, G.7    Cammack, N.8    Matthews, T.J.9    Greenberg, M.L.10
  • 11
    • 3042799046 scopus 로고    scopus 로고
    • Relative replicative fitness of human immunodeficiency virus type 1 mutants resistant to enfuvirtide (T-20)
    • Lu, J., Sista, P., Giguel, F., Greenberg, M., and Kuritzkes, D. R. (2004) Relative replicative fitness of human immunodeficiency virus type 1 mutants resistant to enfuvirtide (T-20). J. Virol. 78, 4628-4637.
    • (2004) J. Virol , vol.78 , pp. 4628-4637
    • Lu, J.1    Sista, P.2    Giguel, F.3    Greenberg, M.4    Kuritzkes, D.R.5
  • 12
    • 16244380203 scopus 로고    scopus 로고
    • Enfuvirtide resistance mutations: Impact on human immunodeficiency virus envelope function, entry inhibitor sensitivity, and virus neutralization
    • Reeves, J. D., Lee, F.-H., Miamidian, J. L., Jabara, C. B., Juntilla, M. M., and Doms, R. W. (2005) Enfuvirtide resistance mutations: Impact on human immunodeficiency virus envelope function, entry inhibitor sensitivity, and virus neutralization. J. Virol. 79, 4991-4999.
    • (2005) J. Virol , vol.79 , pp. 4991-4999
    • Reeves, J.D.1    Lee, F.-H.2    Miamidian, J.L.3    Jabara, C.B.4    Juntilla, M.M.5    Doms, R.W.6
  • 14
    • 36348936125 scopus 로고    scopus 로고
    • Association between specific enfuvirtide resistance mutations and CD4 cell response during enfuvirtide-based therapy
    • Melby, T., DeSpirito, M., DeMasi, R., Heilek, G., Thommes, J. A., Greenberg, M. L., and Graham, N. (2007) Association between specific enfuvirtide resistance mutations and CD4 cell response during enfuvirtide-based therapy. AIDS 21, 2537-2539.
    • (2007) AIDS 21 , pp. 2537-2539
    • Melby, T.1    DeSpirito, M.2    DeMasi, R.3    Heilek, G.4    Thommes, J.A.5    Greenberg, M.L.6    Graham, N.7
  • 16
    • 33750252336 scopus 로고    scopus 로고
    • Genetic evolution of gp41 reveals a highly exclusive relationship between codons 36, 38 and 43 in gp41 under long-term enfuvirtide-containing salvage regimen
    • Cabrera, C., Marfil, S., Garcia, E., Martinez-Picado, J., Bonjoch, A., Bofill, M., Moreno, S., Ribera, E., Domingo, P., Clotet, B., and Ruiz, L. (2006) Genetic evolution of gp41 reveals a highly exclusive relationship between codons 36, 38 and 43 in gp41 under long-term enfuvirtide-containing salvage regimen. AIDS 20, 2075-2080.
    • (2006) AIDS 20 , pp. 2075-2080
    • Cabrera, C.1    Marfil, S.2    Garcia, E.3    Martinez-Picado, J.4    Bonjoch, A.5    Bofill, M.6    Moreno, S.7    Ribera, E.8    Domingo, P.9    Clotet, B.10    Ruiz, L.11
  • 17
    • 10744229122 scopus 로고    scopus 로고
    • Lalezari, J. P., DeJesus, E., Northfelt, D. W., Richmond, G., Wolfe, P., Haubrich, R., Henry, D., Powderly, W., Becker, S., Thompson, M., Valentine, F., Wright, D., Carlson, M., Riddler, S., Haas, F. F., DeMasi, R., Sista, P. R., Salgo, M., and Delehanty, J. (2003) A controlled Phase II trial assessing three doses of enfuvirtide (T-20) in combination with abacavir, amprenavir, ritonavir and efavirenz in non-nucleoside reverse transcriptase inhibitor-naive HIV-infected adults. Antiviral Ther. 8, 279-287.
    • Lalezari, J. P., DeJesus, E., Northfelt, D. W., Richmond, G., Wolfe, P., Haubrich, R., Henry, D., Powderly, W., Becker, S., Thompson, M., Valentine, F., Wright, D., Carlson, M., Riddler, S., Haas, F. F., DeMasi, R., Sista, P. R., Salgo, M., and Delehanty, J. (2003) A controlled Phase II trial assessing three doses of enfuvirtide (T-20) in combination with abacavir, amprenavir, ritonavir and efavirenz in non-nucleoside reverse transcriptase inhibitor-naive HIV-infected adults. Antiviral Ther. 8, 279-287.
  • 18
    • 33847020059 scopus 로고    scopus 로고
    • Full fusion competence rescue of the enfuvirtide resistant HIV-1 gp41 genotype (43D) by a prevalent polymorphism (137K)
    • Tolstrup, M., Selzer-Plon, J., Laursen, A. L., Bertelsen, L., Gerstoft, J., Duch, M., Pedersen, F., and Ostergaard, L. (2007) Full fusion competence rescue of the enfuvirtide resistant HIV-1 gp41 genotype (43D) by a prevalent polymorphism (137K). AIDS 21, 519-521.
    • (2007) AIDS 21 , pp. 519-521
    • Tolstrup, M.1    Selzer-Plon, J.2    Laursen, A.L.3    Bertelsen, L.4    Gerstoft, J.5    Duch, M.6    Pedersen, F.7    Ostergaard, L.8
  • 19
    • 0027499917 scopus 로고
    • Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein
    • Cao, J., Bergeron, L., Helseth, E., Thali, M., Repke, H., and Sodroski, J. (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
  • 20
    • 0034759947 scopus 로고    scopus 로고
    • Structural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis
    • Lu, M., Stoller, M. O., Wang, S., Liu, J., Fagan, M. B., and Nunberg, J. H. (2001) Structural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis. J. Virol. 75, 11146-11156.
    • (2001) J. Virol , vol.75 , pp. 11146-11156
    • Lu, M.1    Stoller, M.O.2    Wang, S.3    Liu, J.4    Fagan, M.B.5    Nunberg, J.H.6
  • 21
    • 0031798443 scopus 로고    scopus 로고
    • Mutational analysis of residues in the coiled-coil domain of human immunodeficiency virus type 1 transmembrane protein gp41
    • Weng, Y., and Weiss, C. D. (1998) Mutational analysis of residues in the coiled-coil domain of human immunodeficiency virus type 1 transmembrane protein gp41. J. Virol. 72, 9676-9682.
    • (1998) J. Virol , vol.72 , pp. 9676-9682
    • Weng, Y.1    Weiss, C.D.2
  • 22
    • 0036633932 scopus 로고    scopus 로고
    • Genetic evidence that interhelical packing interactions in the gp41 core are critical for transition of the human immunodeficiency virus type 1 envelope glycoprotein to the fusion-active state
    • Follis, K. E., Larson, S. J., Lu, M., and Nunberg, J. H. (2002) Genetic evidence that interhelical packing interactions in the gp41 core are critical for transition of the human immunodeficiency virus type 1 envelope glycoprotein to the fusion-active state. J. Virol. 76, 7356-7362.
    • (2002) J. Virol , vol.76 , pp. 7356-7362
    • Follis, K.E.1    Larson, S.J.2    Lu, M.3    Nunberg, J.H.4
  • 23
    • 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
  • 24
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan, K., Liu, J., Wang, J., Shen, S., and Lu, M. (1997) Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. U.S.A. 94, 12303-12308.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 25
    • 0032483021 scopus 로고    scopus 로고
    • Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: Conserved helical interactions underlie the broad inhibitory activity of gp41 peptides
    • Malashkevich, V. N., Chan, D. C., Chutkowski, C. T., and Kim, P. S. (1998) Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: Conserved helical interactions underlie the broad inhibitory activity of gp41 peptides. Proc. Natl. Acad. Sci. U.S.A. 95, 9134-9139.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 9134-9139
    • Malashkevich, V.N.1    Chan, D.C.2    Chutkowski, C.T.3    Kim, P.S.4
  • 27
    • 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., Barry, A. P., Wang, Z. X., Connolly, S. M., Peiper, S. C., and Greenberg, M. L. (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
  • 28
    • 0026562720 scopus 로고
    • Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated β-galactosidase gene
    • Kimpton, J., and Emerman, M. (1992) Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated β-galactosidase gene. J. Virol. 66, 2232-2239.
    • (1992) J. Virol , vol.66 , pp. 2232-2239
    • Kimpton, J.1    Emerman, M.2
  • 29
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 30
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W. C. (1990) Protein secondary structure and circular dichroism: A practical guide. Proteins: Struct., Funct., Genet. 7, 205-214.
    • (1990) Proteins: Struct., Funct., Genet , vol.7 , pp. 205-214
    • Johnson, W.C.1
  • 31
    • 0038671938 scopus 로고    scopus 로고
    • The hydrophobic pocket contributes to the structural stability of the N-terminal coiled coil of HIV gp41 but is not required for six-helix bundle formation
    • Dwyer, J. J., Hasan, A., Wilson, K. L., White, J. M., Matthews, T. J., and Delmedico, M. K. (2003) The hydrophobic pocket contributes to the structural stability of the N-terminal coiled coil of HIV gp41 but is not required for six-helix bundle formation. Biochemistry 42, 4945-4953.
    • (2003) Biochemistry , vol.42 , pp. 4945-4953
    • Dwyer, J.J.1    Hasan, A.2    Wilson, K.L.3    White, J.M.4    Matthews, T.J.5    Delmedico, M.K.6
  • 33
    • 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
  • 35
    • 45749112665 scopus 로고    scopus 로고
    • DeLano, W. L, 2002 The PyMOL Molecular Graphics System, version 0.92, DeLano Scientific, San Carlos, CA
    • DeLano, W. L. (2002) The PyMOL Molecular Graphics System, version 0.92, DeLano Scientific, San Carlos, CA.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.