메뉴 건너뛰기




Volumn 287, Issue 11, 2012, Pages 8297-8309

Trimeric, coiled-coil extension on peptide fusion inhibitor of HIV-1 influences selection of resistance pathways

Author keywords

[No Author keywords available]

Indexed keywords

COILED COIL; DOMINANT NEGATIVE; EQUAL PROBABILITY; FUSION PROTEINS; GAIN INSIGHT; GENETIC PATHWAYS; HEPTAD REPEAT REGIONS; INHIBITOR DESIGN; PEPTIDE FUSION; PEPTIDE INHIBITORS; REFOLDING; TRIMERIZATION; VIRUS ENTRY;

EID: 84863270623     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.324483     Document Type: Article
Times cited : (21)

References (45)
  • 1
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • DOI 10.1146/annurev.biochem.70.1.777
    • Eckert, D. M., and Kim, P. S. (2001) Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70, 777-810 (Pubitemid 32662225)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 2
    • 79960435702 scopus 로고    scopus 로고
    • Membrane fusion mediated by human Immunodeficiency virus envelope glycoprotein
    • Melikyan, G. B. (2011) Membrane fusion mediated by human Immunodeficiency virus envelope glycoprotein. Curr. Top. Membr. 86, 81-106
    • (2011) Curr. Top. Membr. , vol.86 , pp. 81-106
    • Melikyan, G.B.1
  • 3
    • 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 (Pubitemid 27199898)
    • (1997) Cell , vol.89 , Issue.2 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 4
    • 0030962291 scopus 로고    scopus 로고
    • Atomic structure of the ectodomain from HIV-1 gp41
    • DOI 10.1038/387426a0
    • Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J., and Wiley, D. C. (1997) Atomic structure of the ectodomain from HIV-1 gp41. Nature 387, 426-430 (Pubitemid 27227210)
    • (1997) Nature , vol.387 , Issue.6631 , pp. 426-430
    • Weissenhorn, W.1    Dessen, A.2    Harrison, S.C.3    Skehel, J.J.4    Wiley, D.C.5
  • 8
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • DOI 10.1038/nsb0498-276
    • Furuta, R. A., Wild, C. T., Weng, Y., and Weiss, C. D. (1998) Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 5, 276-279 (Pubitemid 28164878)
    • (1998) Nature Structural Biology , vol.5 , Issue.4 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 9
    • 0037301373 scopus 로고    scopus 로고
    • Peptides trap the human immunodeficiency virus type 1 envelope glycoprotein fusion intermediate at two sites
    • DOI 10.1128/JVI.77.3.1666-1671.2003
    • He, Y., Vassell, R., Zaitseva, M., Nguyen, N., Yang, Z., Weng, Y., and Weiss, C. D. (2003) Peptides trap the human immunodeficiency virus type 1 envelope glycoprotein fusion intermediate at two sites. J. Virol. 77, 1666-1671 (Pubitemid 36113245)
    • (2003) Journal of Virology , 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
  • 10
    • 0037470227 scopus 로고    scopus 로고
    • The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions
    • DOI 10.1074/jbc.M211154200
    • Koshiba, T., and Chan, D. C. (2003) The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions. J. Biol. Chem. 278, 7573-7579 (Pubitemid 36800765)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 7573-7579
    • Koshiba, T.1    Chan, D.C.2
  • 11
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • DOI 10.1016/S0092-8674(00)81430-0
    • Chan, D. C., and Kim, P. S. (1998) HIV entry and its inhibition. Cell 93, 681-684 (Pubitemid 28257575)
    • (1998) Cell , vol.93 , Issue.5 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 12
    • 0042924167 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry with fusion inhibitors
    • DOI 10.2174/0929867033457124
    • Baldwin, C. E., Sanders, R. W., and Berkhout, B. (2003) Inhibiting HIV-1 entry with fusion inhibitors. Curr. Med. Chem. 10, 1633-1642 (Pubitemid 37038590)
    • (2003) Current Medicinal Chemistry , vol.10 , Issue.17 , pp. 1633-1642
    • Baldwin, C.E.1    Sanders, R.W.2    Berkhout, B.3
  • 13
    • 34248155890 scopus 로고    scopus 로고
    • HIV gp41 C-terminal heptad repeat contains multifunctional domains: Relation to mechanisms of action of anti-HIV peptides
    • DOI 10.1074/jbc.M609148200
    • Liu, S., Jing, W., Cheung, B., Lu, H., Sun, J., Yan, X., Niu, J., Farmar, J., Wu, S., and Jiang, S. (2007) HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides. J. Biol. Chem. 282, 9612-9620 (Pubitemid 47104580)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.13 , pp. 9612-9620
    • Liu, S.1    Jing, W.2    Cheung, B.3    Lu, H.4    Sun, J.5    Yan, X.6    Niu, J.7    Farmar, J.8    Wu, S.9    Jiang, S.10
  • 14
    • 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
    • DOI 10.1128/JVI.77.13.7669-7672.2003
    • 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 (Pubitemid 36734537)
    • (2003) Journal of Virology , vol.77 , Issue.13 , pp. 7669-7672
    • Kilgore, N.R.1    Salzwedel, K.2    Reddick, M.3    Allaway, G.P.4    Wild, C.T.5
  • 15
    • 0036090585 scopus 로고    scopus 로고
    • Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy
    • DOI 10.1128/AAC.46.6.1896-1905.2002
    • Wei, X., Decker, J. M., Liu, H., Zhang, Z., Arani, R. B., Kilby, J. M., Saag, M. S., Wu, X., Shaw, G. M., and Kappes, J. C. (2002) Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy. Antimicrob. Agents. Chemother. 46, 1896-1905 (Pubitemid 34535213)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.6 , pp. 1896-1905
    • Wei, X.1    Decker, J.M.2    Liu, H.3    Zhang, Z.4    Arani, R.B.5    Kilby, J.M.6    Saag, M.S.7    Wu, X.8    Shaw, G.M.9    Kappes, J.C.10
  • 16
    • 0037183892 scopus 로고    scopus 로고
    • Evolution of the gp41 env region in HIV-infected patients receiving T-20, a fusion inhibitor
    • Poveda, E., Rodés, B., Toro, C., Martín-Carbonero, L., Gonzalez-Lahoz, J., and Soriano, V. (2002) Evolution of the gp41 env region in HIV-infected patients receiving T-20, a fusion inhibitor. Aids 16, 1959-1961
    • (2002) Aids , vol.16 , pp. 1959-1961
    • Poveda, E.1    Rodés, B.2    Toro, C.3    Martín-Carbonero, L.4    Gonzalez-Lahoz, J.5    Soriano, V.6
  • 17
    • 4444375658 scopus 로고    scopus 로고
    • Resistance to enfuvirtide, the first HIV fusion inhibitor
    • DOI 10.1093/jac/dkh330
    • Greenberg, M. L., and Cammack, N. (2004) Resistance to enfuvirtide, the first HIV fusion inhibitor. J. Antimicrob. Chemother. 54, 333-340 (Pubitemid 39177450)
    • (2004) Journal of Antimicrobial Chemotherapy , vol.54 , Issue.2 , pp. 333-340
    • Greenberg, M.L.1    Cammack, N.2
  • 19
    • 34249935492 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 variants resistant to first- and second-version fusion inhibitors and cytopathic in ex vivo human lymphoid tissue
    • DOI 10.1128/JVI.02546-06
    • Chinnadurai, R., Rajan, D., Münch, J., and Kirchhoff, F. (2007) Human immunodeficiency virus type 1 variants resistant to first- and second-version fusion inhibitors and cytopathic in ex vivo human lymphoid tissue. J. Virol. 81, 6563-6572 (Pubitemid 46878060)
    • (2007) Journal of Virology , vol.81 , Issue.12 , pp. 6563-6572
    • Chinnadurai, R.1    Rajan, D.2    Munch, J.3    Kirchhoff, F.4
  • 21
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • DOI 10.1126/science.1057453
    • Root, M. J., Kay, M. S., and Kim, P. S. (2001) Protein design of an HIV-1 entry inhibitor. Science 291, 884-888 (Pubitemid 32120761)
    • (2001) Science , vol.291 , Issue.5505 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 22
    • 0031441562 scopus 로고    scopus 로고
    • A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein
    • Lu, M., and Kim, P. S. (1997)Atrimeric structural subdomain of the HIV-1 transmembrane glycoprotein. J. Biomol. Struct. Dyn. 15, 465-471 (Pubitemid 28035859)
    • (1997) Journal of Biomolecular Structure and Dynamics , vol.15 , Issue.3 , pp. 465-471
    • Lu, M.1    Kim, P.S.2
  • 23
    • 0029926552 scopus 로고    scopus 로고
    • HIV-1 membrane fusion mechanism: Structural studies of the interactions between biologically-active peptides from gp41
    • DOI 10.1021/bi9606962
    • Lawless, M. K., Barney, S., Guthrie, K. I., Bucy, T. B., Petteway, S. R., Jr., and Merutka, G. (1996) HIV-1 membrane fusion mechanism. Structural studies of the interactions between biologically active peptides from gp41. Biochemistry 35, 13697-13708 (Pubitemid 26359183)
    • (1996) Biochemistry , vol.35 , Issue.42 , pp. 13697-13708
    • Lawless, M.K.1    Barney, S.2    Guthrie, K.I.3    Bucy, T.B.4    Petteway Jr., S.R.5    Merutka, G.6
  • 24
    • 0037134497 scopus 로고    scopus 로고
    • Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41
    • DOI 10.1074/jbc.M201453200
    • 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 (Pubitemid 34968038)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.16 , pp. 14238-14245
    • Bewley, C.A.1    Louis, J.M.2    Ghirlando, R.3    Marius, C.G.4
  • 25
    • 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., and Clore, G. M. (1999) Monomer-trimer equilibrium of the ectodomain of SIV gp41. Insight into the mechanism of peptide inhibition of HIV infection. Protein Sci. 8, 1904-1907 (Pubitemid 29430491)
    • (1999) Protein Science , vol.8 , Issue.9 , pp. 1904-1907
    • Caffrey, M.1    Kaufman, J.2    Stahl, S.3    Wingfield, P.4    Gronenborn, A.M.5    Clore, G.M.6
  • 26
    • 16244367157 scopus 로고    scopus 로고
    • Human immunodeficiency virus (HIV) gp41 escape mutants: Cross-resistance to peptide inhibitors of HIV fusion and altered receptor activation of gp120
    • DOI 10.1128/JVI.79.8.4774-4781.2005
    • Desmezieres, E., Gupta, N., Vassell, R., He, Y., Peden, K., Sirota, L., Yang, Z., Wingfield, P., and Weiss, C. D. (2005) Human immunodeficiency virus (HIV) gp41 escape mutants. Cross-resistance to peptide inhibitors of HIV fusion and altered receptor activation of gp120. J. Virol. 79, 4774-4781 (Pubitemid 40464228)
    • (2005) Journal of Virology , vol.79 , Issue.8 , pp. 4774-4781
    • Desmezieres, E.1    Gupta, N.2    Vassell, R.3    He, Y.4    Peden, K.5    Sirota, L.6    Yang, Z.7    Wingfield, P.8    Weiss, C.D.9
  • 27
    • 0025149054 scopus 로고
    • Mutational analysis of the human immunodeficiency virus type 1 Rev transactivator: Essential residues near the amino terminus
    • Hope, T. J., McDonald, D., Huang, X. J., Low, J., and Parslow, T. G. (1990) Mutational analysis of the human immunodeficiency virus type 1 Rev transactivator. Essential residues near the amino terminus. J. Virol. 64, 5360-5366 (Pubitemid 20364526)
    • (1990) Journal of Virology , vol.64 , Issue.11 , pp. 5360-5366
    • Hope, T.J.1    McDonald, D.2    Huang, X.3    Low, J.4    Parslow, T.G.5
  • 28
    • 0031954686 scopus 로고    scopus 로고
    • Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1
    • Platt, E. J., Wehrly, K., Kuhmann, S. E., Chesebro, B., and Kabat, D. (1998) Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1. J. Virol. 72, 2855-2864 (Pubitemid 28175522)
    • (1998) Journal of Virology , vol.72 , Issue.4 , pp. 2855-2864
    • Platt, E.J.1    Wehrly, K.2    Kuhmann, S.E.3    Chesebro, B.4    Kabat, D.5
  • 29
    • 0029045651 scopus 로고
    • CD26 expression correlates with entry, replication and cytopathicity of monocytotropic HIV-1 strains in a T-cell line
    • Oravecz, T., Roderiquez, G., Koffi, J., Wang, J., Ditto, M., Bou-Habib, D. C., Lusso, P., and Norcross, M. A. (1995) CD26 expression correlates with entry, replication and cytopathicity of monocytotropic HIV-1 strains in a T-cell line. Nat. Med. 1, 919-926
    • (1995) Nat. Med. , vol.1 , pp. 919-926
    • Oravecz, T.1    Roderiquez, G.2    Koffi, J.3    Wang, J.4    Ditto, M.5    Bou-Habib, D.C.6    Lusso, P.7    Norcross, M.A.8
  • 30
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent endpoints
    • Reed, L. J., and Muench, H. (1938) A simple method of estimating fifty percent endpoints. Am. J. Hygiene 27, 493-497
    • (1938) Am. J. Hygiene , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 31
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • Chen, Y. H., Yang, J. T., and Chau, K. H. (1974) Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 32
    • 0034701058 scopus 로고    scopus 로고
    • Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides
    • DOI 10.1021/bi9921687
    • Shu, W., Liu, J., Ji, H., Radigen, L., Jiang, S., and Lu, M. (2000) Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides. Biochemistry 39, 1634-1642 (Pubitemid 30108955)
    • (2000) Biochemistry , vol.39 , Issue.7 , pp. 1634-1642
    • Shu, W.1    Liu, J.2    Ji, H.3    Radigen, L.4    Jiang, S.5    Lu, M.6
  • 33
    • 0028947236 scopus 로고
    • Thermodynamics of denaturation of barstar. Evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride
    • Agashe, V. R., and Udgaonkar, J. B. (1995) Thermodynamics of denaturation of barstar. Evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride. Biochemistry 34, 3286-3299
    • (1995) Biochemistry , vol.34 , pp. 3286-3299
    • Agashe, V.R.1    Udgaonkar, J.B.2
  • 34
    • 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
    • DOI 10.1128/JVI.00319-08
    • 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 (Pubitemid 351875113)
    • (2008) Journal of Virology , vol.82 , Issue.13 , 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
  • 35
    • 84862909153 scopus 로고    scopus 로고
    • Selection with a peptide fusion inhibitor corresponding to the first heptad repeat of HIV-1 gp41 identifies two genetic pathways conferring cross-resistance to peptide fusion inhibitors corresponding to the first and second heptad repeats (HR1 and HR2) of gp41
    • Wang, W., De Feo, C. J., Zhuang, M., Vassell, R., and Weiss, C. D. (2011) Selection with a peptide fusion inhibitor corresponding to the first heptad repeat of HIV-1 gp41 identifies two genetic pathways conferring cross-resistance to peptide fusion inhibitors corresponding to the first and second heptad repeats (HR1 and HR2) of gp41. J. Virol. 85, 12929-12938
    • (2011) J. Virol. , vol.85 , pp. 12929-12938
    • Wang, W.1    De Feo, C.J.2    Zhuang, M.3    Vassell, R.4    Weiss, C.D.5
  • 36
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp 120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • DOI 10.1038/31405
    • Kwong, P. D., Wyatt, R., Robinson, J., Sweet, R. W., Sodroski, J., and Hendrickson, W. A. (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648-659 (Pubitemid 28289647)
    • (1998) Nature , vol.393 , Issue.6686 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 37
    • 1342300737 scopus 로고    scopus 로고
    • α-Complementation assay for HIV envelope glycoprotein-mediated fusion
    • DOI 10.1016/j.virol.2003.11.012
    • Holland, A. U., Munk, C., Lucero, G. R., Nguyen, L. D., and Landau, N. R. (2004) α-Complementation assay for HIV envelope glycoprotein-mediated fusion. Virology 319, 343-352 (Pubitemid 38251274)
    • (2004) Virology , vol.319 , Issue.2 , pp. 343-352
    • Holland, A.U.1    Munk, C.2    Lucero, G.R.3    Nguyen, L.D.4    Landau, N.R.5
  • 39
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., Blacklow, S. C., and Kim, P. S. (1995) A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2, 1075-1082
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 40
    • 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. (2001) Model for the structure of the HIV gp41 ectodomain. Insight into the intermolecular interactions of the gp41 loop. Biochim. Biophys. Acta 1536, 116-122
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 116-122
    • Caffrey, M.1
  • 41
    • 16844379486 scopus 로고    scopus 로고
    • Steric accessibility of the HIV-1 gp41 N-trimer region
    • Hamburger, A. E., Kim, S., Welch, B. D., and Kay, M. S. (2005) Steric accessibility of the HIV-1 gp41 N-trimer region. J. Biol. Chem. 280, 12567-12572
    • (2005) J. Biol. Chem. , vol.280 , pp. 12567-12572
    • Hamburger, A.E.1    Kim, S.2    Welch, B.D.3    Kay, M.S.4
  • 42
    • 33748741296 scopus 로고    scopus 로고
    • Kinetic dependence to HIV-1 entry inhibition
    • DOI 10.1074/jbc.M601457200
    • Steger, H. K., and Root, M. J. (2006) Kinetic dependence to HIV-1 entry inhibition. J. Biol. Chem. 281, 25813-25821 (Pubitemid 44401969)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.35 , pp. 25813-25821
    • Steger, H.K.1    Root, M.J.2
  • 44
    • 84863290011 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.