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Volumn 80, Issue 1, 2008, Pages 71-76

Novel screening systems for HIV-1 fusion mediated by two extra-virion heptad repeats of gp41

Author keywords

Alkaline phosphatase; ELISA; Fusion; Gp41; HIV 1; Screening

Indexed keywords

ALKALINE PHOSPHATASE; ANTIBODY CONJUGATE; ANTIVIRUS AGENT; DIMETHYL SULFOXIDE; ENFUVIRTIDE; GLYCOPROTEIN GP 41; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; VIRUS FUSION INHIBITOR;

EID: 50049102385     PISSN: 01663542     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.antiviral.2008.05.006     Document Type: Article
Times cited : (10)

References (43)
  • 3
    • 0000701207 scopus 로고
    • Mechanism of inhibitory effect of dextran sulfate and heparin on replication of human immunodeficiency virus in vitro
    • Baba M., Pauwels R., Balzarini J., Arnout J., Desmyter J., and De Clercq E. Mechanism of inhibitory effect of dextran sulfate and heparin on replication of human immunodeficiency virus in vitro. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 6132-6136
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 6132-6136
    • Baba, M.1    Pauwels, R.2    Balzarini, J.3    Arnout, J.4    Desmyter, J.5    De Clercq, E.6
  • 4
    • 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. Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. J. Biol. Chem. 277 (2002) 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
  • 6
    • 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., García E., Martinez-Picado J., Bonjoch A., Bofill M., Moreno S., Ribera E., Domingo P., Clotet B., and Ruiz L. 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 (2006) 2075-2080
    • (2006) AIDS , vol.20 , pp. 2075-2080
    • Cabrera, C.1    Marfil, S.2    García, 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
  • 7
    • 34447260888 scopus 로고    scopus 로고
    • A novel fluorescence intensity screening assay identifies new low-molecular-weight inhibitors of the gp41 coiled-coil domain of human immunodeficiency virus type 1
    • Cai L., and Gochin M. A novel fluorescence intensity screening assay identifies new low-molecular-weight inhibitors of the gp41 coiled-coil domain of human immunodeficiency virus type 1. Antimicrob. Agents Chemother. 51 (2007) 2388-2395
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 2388-2395
    • Cai, L.1    Gochin, M.2
  • 9
    • 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. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89 (1997) 263-273
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 11
    • 0022543853 scopus 로고
    • Expression, secretion and processing of hirudin in E. coli using the alkaline phosphatase signal sequence
    • Dodt J., Schmitz T., Schäfer T., and Bergmann C. Expression, secretion and processing of hirudin in E. coli using the alkaline phosphatase signal sequence. FEBS Lett. 202 (1986) 373-377
    • (1986) FEBS Lett. , vol.202 , pp. 373-377
    • Dodt, J.1    Schmitz, T.2    Schäfer, T.3    Bergmann, C.4
  • 12
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert D.M., and Kim P.S. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70 (2001) 777-810
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 16
    • 34147136222 scopus 로고    scopus 로고
    • Safety and efficacy of the HIV-1 integrase inhibitor raltegravir (MK-0518) in treatment-experienced patients with multidrug-resistant virus: a phase II randomised controlled trial
    • Grinsztejn B., Nguyen B.Y., Katlama C., Gatell J.M., Lazzarin A., Vittecoq D., Gonzalez C.J., Chen J., Harvey C.M., and Isaacs R.D. Safety and efficacy of the HIV-1 integrase inhibitor raltegravir (MK-0518) in treatment-experienced patients with multidrug-resistant virus: a phase II randomised controlled trial. Lancet 369 (2007) 1261-1269
    • (2007) Lancet , vol.369 , pp. 1261-1269
    • Grinsztejn, B.1    Nguyen, B.Y.2    Katlama, C.3    Gatell, J.M.4    Lazzarin, A.5    Vittecoq, D.6    Gonzalez, C.J.7    Chen, J.8    Harvey, C.M.9    Isaacs, R.D.10
  • 18
    • 33748185656 scopus 로고    scopus 로고
    • Identification of the HIV-1 gp41 core-binding motif-HXXNPF
    • Huang J.H., Liu Z.Q., Liu S., Jiang S., and Chen Y.H. Identification of the HIV-1 gp41 core-binding motif-HXXNPF. FEBS Lett. 580 (2006) 4807-4814
    • (2006) FEBS Lett. , vol.580 , pp. 4807-4814
    • Huang, J.H.1    Liu, Z.Q.2    Liu, S.3    Jiang, S.4    Chen, Y.H.5
  • 19
    • 34247859078 scopus 로고    scopus 로고
    • The mechanism by which molecules containing the HIV gp41 core-binding motif HXXNPF inhibit HIV-1 envelope glycoprotein-mediated syncytium formation
    • Huang J.H., Yang H.W., Liu S., Li J., Jiang S., and Chen Y.H. The mechanism by which molecules containing the HIV gp41 core-binding motif HXXNPF inhibit HIV-1 envelope glycoprotein-mediated syncytium formation. Biochem. J. 403 (2007) 565-571
    • (2007) Biochem. J. , vol.403 , pp. 565-571
    • Huang, J.H.1    Yang, H.W.2    Liu, S.3    Li, J.4    Jiang, S.5    Chen, Y.H.6
  • 20
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn R., Lang T., and Südhof T.C. Membrane fusion. Cell 112 (2003) 519-533
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Südhof, T.C.3
  • 21
    • 0033041322 scopus 로고    scopus 로고
    • A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody
    • Jiang S., Lin K., Zhang L., and Debnath A.K. A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody. J. Virol. Methods 80 (1999) 85-96
    • (1999) J. Virol. Methods , vol.80 , pp. 85-96
    • Jiang, S.1    Lin, K.2    Zhang, L.3    Debnath, A.K.4
  • 22
    • 0019857117 scopus 로고
    • The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli
    • Kikuchi Y., Yoda K., Yamasaki M., and Tamura G. The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli. Nucl. Acids Res. 9 (1981) 5671-5678
    • (1981) Nucl. Acids Res. , vol.9 , pp. 5671-5678
    • Kikuchi, Y.1    Yoda, K.2    Yamasaki, M.3    Tamura, G.4
  • 23
    • 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 beta-galactosidase gene
    • Kimpton J., and Emerman M. Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene. J. Virol. 66 (1992) 2232-2239
    • (1992) J. Virol. , vol.66 , pp. 2232-2239
    • Kimpton, J.1    Emerman, M.2
  • 24
    • 0033551053 scopus 로고    scopus 로고
    • Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins
    • Kobe B., Center R.J., Kemp B.E., and Poumbourios P. Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 4319-4324
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4319-4324
    • Kobe, B.1    Center, R.J.2    Kemp, B.E.3    Poumbourios, P.4
  • 28
    • 34248155890 scopus 로고    scopus 로고
    • HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides
    • Liu S., Jing W., Cheung B., Lu H., Sun J., Yan X., Niu J., Farmar J., Wu S., and Jiang S. HIV gp41 C-terminal heptad repeat contains multifunctional domains. Relation to mechanisms of action of anti-HIV peptides. J. Biol. Chem. 282 (2007) 9612-9620
    • (2007) J. Biol. Chem. , vol.282 , 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
  • 29
    • 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. 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 (2005) 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
  • 30
    • 0036720982 scopus 로고    scopus 로고
    • C-terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread
    • Medinas R.J., Lambert D.M., and Tompkins W.A. C-terminal gp40 peptide analogs inhibit feline immunodeficiency virus: cell fusion and virus spread. J. Virol. 76 (2002) 9079-9086
    • (2002) J. Virol. , vol.76 , pp. 9079-9086
    • Medinas, R.J.1    Lambert, D.M.2    Tompkins, W.A.3
  • 32
    • 11144236493 scopus 로고    scopus 로고
    • Mutations conferring resistance to human immunodeficiency virus type 1 fusion inhibitors are restricted by gp41 and Rev-responsive element functions
    • Nameki D., Kodama E., Ikeuchi M., Mabuchi N., Otaka A., Tamamura H., Ohno M., Fujii N., and Matsuoka M. Mutations conferring resistance to human immunodeficiency virus type 1 fusion inhibitors are restricted by gp41 and Rev-responsive element functions. J. Virol. 79 (2005) 764-770
    • (2005) J. Virol. , vol.79 , pp. 764-770
    • Nameki, D.1    Kodama, E.2    Ikeuchi, M.3    Mabuchi, N.4    Otaka, A.5    Tamamura, H.6    Ohno, M.7    Fujii, N.8    Matsuoka, M.9
  • 34
    • 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. Evolution of the gp41 env region in HIV-infected patients receiving T-20, a fusion inhibitor. AIDS 16 (2002) 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
  • 35
    • 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. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 72 (1998) 986-993
    • (1998) J. Virol. , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 36
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root M.J., Kay M.S., and Kim P.S. Protein design of an HIV-1 entry inhibitor. Science 291 (2001) 884-888
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 37
    • 0032585364 scopus 로고    scopus 로고
    • Development of an in vitro assay system for screening of gp41 inhibitory compounds
    • Ryu J.R., Lee J., Choo S., Yoon S.H., Woo E.R., and Yu Y.G. Development of an in vitro assay system for screening of gp41 inhibitory compounds. Mol. Cells 8 (1998) 717-723
    • (1998) Mol. Cells , vol.8 , pp. 717-723
    • Ryu, J.R.1    Lee, J.2    Choo, S.3    Yoon, S.H.4    Woo, E.R.5    Yu, Y.G.6
  • 38
    • 11144340301 scopus 로고    scopus 로고
    • Class I and class II viral fusion protein structures reveal similar principles in membrane fusion
    • Schibli D.J., and Weissenhorn W. Class I and class II viral fusion protein structures reveal similar principles in membrane fusion. Mol. Membr. Biol. 21 (2004) 361-371
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 361-371
    • Schibli, D.J.1    Weissenhorn, W.2
  • 39
    • 2342544143 scopus 로고    scopus 로고
    • Piperazine-based CCR5 antagonists as HIV-1 inhibitors. IV. Discovery of 1-[(4,6-dimethyl-5-pyrimidinyl)carbonyl]-4-[4-[2-methoxy-1(R)-4-(trifluoromethyl)phenyl]ethyl-3(S)-methyl-1-piperazinyl]-4-methylpiperidine (Sch-417690/Sch-D), a potent, highly selective, and orally bioavailable CCR5 antagonist
    • Tagat J.R., McCombie S.W., Nazareno D., Labroli M.A., Xiao Y., Steensma R.W., Strizki J.M., Baroudy B.M., Cox K., Lachowicz J., Varty G., and Watkins R. Piperazine-based CCR5 antagonists as HIV-1 inhibitors. IV. Discovery of 1-[(4,6-dimethyl-5-pyrimidinyl)carbonyl]-4-[4-[2-methoxy-1(R)-4-(trifluoromethyl)phenyl]ethyl-3(S)-methyl-1-piperazinyl]-4-methylpiperidine (Sch-417690/Sch-D), a potent, highly selective, and orally bioavailable CCR5 antagonist. J. Med. Chem. 47 (2004) 2405-2408
    • (2004) J. Med. Chem. , vol.47 , pp. 2405-2408
    • Tagat, J.R.1    McCombie, S.W.2    Nazareno, D.3    Labroli, M.A.4    Xiao, Y.5    Steensma, R.W.6    Strizki, J.M.7    Baroudy, B.M.8    Cox, K.9    Lachowicz, J.10    Varty, G.11    Watkins, R.12
  • 40
    • 0033771310 scopus 로고    scopus 로고
    • Functional importance of the coiled-coil of the Ebola virus glycoprotein
    • Watanabe S., Takada A., Watanabe T., Ito H., Kida H., and Kawaoka Y. Functional importance of the coiled-coil of the Ebola virus glycoprotein. J. Virol. 74 (2000) 10194-10201
    • (2000) J. Virol. , vol.74 , pp. 10194-10201
    • Watanabe, S.1    Takada, A.2    Watanabe, T.3    Ito, H.4    Kida, H.5    Kawaoka, Y.6
  • 42
    • 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. 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 (2007) 3677-3684
    • (2007) FASEB J. , vol.21 , pp. 3677-3684
    • Wexler-Cohen, Y.1    Shai, Y.2
  • 43
    • 34548757309 scopus 로고    scopus 로고
    • Development of a FRET assay for monitoring of HIV gp41 core disruption
    • Xu Y., Hixon M.S., Dawson P.E., and Janda K.D. Development of a FRET assay for monitoring of HIV gp41 core disruption. J. Org. Chem. 72 (2007) 6700-6707
    • (2007) J. Org. Chem. , vol.72 , pp. 6700-6707
    • Xu, Y.1    Hixon, M.S.2    Dawson, P.E.3    Janda, K.D.4


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