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Volumn 70, Issue 9, 1996, Pages 5840-5844

Conditional human immunodeficiency virus type 1 protease mutants show no role for the viral protease early in virus replication

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Indexed keywords

PROTEINASE;

EID: 0029793658     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.9.5840-5844.1996     Document Type: Article
Times cited : (22)

References (41)
  • 1
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
    • Adachi, A., H. E. Gendelman, S. Koenig, T. Folks, R. Willey, A. Rabson, and M. A. Martin. 1986. Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J. Virol. 59:284-291.
    • (1986) J. Virol. , vol.59 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koenig, S.3    Folks, T.4    Willey, R.5    Rabson, A.6    Martin, M.A.7
  • 2
    • 0025169561 scopus 로고
    • An inhibitor of the protease blocks maturation of human and simian immunodeficiency viruses and spread of infection
    • Ashorn, P., T. J. McQuade, S. Thaisrivongs, A. G. Tomasselli, W. G. Tarpley, and B. Moss. 1990. An inhibitor of the protease blocks maturation of human and simian immunodeficiency viruses and spread of infection. Proc. Natl. Acad. Sci. USA 87:7472-7476.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7472-7476
    • Ashorn, P.1    McQuade, T.J.2    Thaisrivongs, S.3    Tomasselli, A.G.4    Tarpley, W.G.5    Moss, B.6
  • 4
    • 0026013779 scopus 로고
    • Amino acids encoded downstream of gag are not required by Rous sarcoma virus protease during gag-mediated assembly
    • Bennett, R. P., S. Rhee, H. C. Craven, E. Hunter, and J. W. Wills. 1991. Amino acids encoded downstream of gag are not required by Rous sarcoma virus protease during gag-mediated assembly. J. Virol. 65:272-280.
    • (1991) J. Virol. , vol.65 , pp. 272-280
    • Bennett, R.P.1    Rhee, S.2    Craven, H.C.3    Hunter, E.4    Wills, J.W.5
  • 5
    • 0021931766 scopus 로고
    • A deletion mutation in the 5′ part of the pol gene of Moloney murine leukemia virus blocks proteolytic processing of the gag and pol polyproteins
    • Crawford, S., and S. P. Goff. 1985. A deletion mutation in the 5′ part of the pol gene of Moloney murine leukemia virus blocks proteolytic processing of the gag and pol polyproteins. J. Virol. 53:899-907.
    • (1985) J. Virol. , vol.53 , pp. 899-907
    • Crawford, S.1    Goff, S.P.2
  • 6
    • 0027957967 scopus 로고
    • Dissociation and association of the HIV-1 protease dimer subunits: Equilibria and rates
    • Darke, P. L., S. P. Jordan, D. L. Hall, J. A. Zugay, J. A. Shafer, and L. C. Kuo. 1994. Dissociation and association of the HIV-1 protease dimer subunits: equilibria and rates. Biochemistry 33:98-105.
    • (1994) Biochemistry , vol.33 , pp. 98-105
    • Darke, P.L.1    Jordan, S.P.2    Hall, D.L.3    Zugay, J.A.4    Shafer, J.A.5    Kuo, L.C.6
  • 8
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
    • Gottlinger, H. G., J. G. Sodroski, and W. A. Haseltine. 1989. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. USA 86:5781-5785.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5781-5785
    • Gottlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 9
    • 0022271270 scopus 로고
    • Point mutations in the P30 domain of the gag gene of Moloney murine leukemia virus
    • Hsu, H. W., P. Schwartzberg, and S. P. Goff. 1985. Point mutations in the P30 domain of the gag gene of Moloney murine leukemia virus. Virology 142:211-214.
    • (1985) Virology , vol.142 , pp. 211-214
    • Hsu, H.W.1    Schwartzberg, P.2    Goff, S.P.3
  • 10
    • 0026708188 scopus 로고
    • Progression of early steps of human immunodeficiency virus type 1 replication in the presence of an inhibitor of viral protease
    • Jacobsen, H., L. L. Ahlborn, R. Gugel, and J. Mous. 1992. Progression of early steps of human immunodeficiency virus type 1 replication in the presence of an inhibitor of viral protease. J. Virol. 66:5087-5091.
    • (1992) J. Virol. , vol.66 , pp. 5087-5091
    • Jacobsen, H.1    Ahlborn, L.L.2    Gugel, R.3    Mous, J.4
  • 11
    • 0028689671 scopus 로고
    • Analysis of the role of the HIV-1 protease in virion assembly
    • Kaplan, A., M. Manchester, and R. Swanstrom. 1994. Analysis of the role of the HIV-1 protease in virion assembly. Methods Enzymol. 241:58-69.
    • (1994) Methods Enzymol. , vol.241 , pp. 58-69
    • Kaplan, A.1    Manchester, M.2    Swanstrom, R.3
  • 13
    • 0021846499 scopus 로고
    • Murine leukemia virus maturation: Protease region required for conversion from "immature" to "mature" core form and for virus infectivity
    • Katoh, I., Y. Yosbinaka, A. Rein, M. Shibuya, T. Odaka, and S. Oroszlan. 1985. Murine leukemia virus maturation: protease region required for conversion from "immature" to "mature" core form and for virus infectivity. Virology 145:280-292.
    • (1985) Virology , vol.145 , pp. 280-292
    • Katoh, I.1    Yosbinaka, Y.2    Rein, A.3    Shibuya, M.4    Odaka, T.5    Oroszlan, S.6
  • 15
    • 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 M. Emerman. 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. Viral. 66:2232-2239.
    • (1992) J. Viral. , vol.66 , pp. 2232-2239
    • Kimpton, J.1    Emerman, M.2
  • 17
    • 0028168754 scopus 로고
    • Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal
    • Lee, P. P., and M. L. Linial. 1994. Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal. J. Virol. 68:6644-6654.
    • (1994) J. Virol. , vol.68 , pp. 6644-6654
    • Lee, P.P.1    Linial, M.L.2
  • 18
    • 0023687861 scopus 로고
    • Purification and structural characterization of the putative gag-pol protease of human immunodeficiency virus
    • Lillehoj, E. P., F. H. Salazar, R. J. Mervis, M. G. Raum, H. W. Chan, N. Ahmad, and S. Venkatesan. 1988. Purification and structural characterization of the putative gag-pol protease of human immunodeficiency virus. J. Virol. 62:3053-3058.
    • (1988) J. Virol. , vol.62 , pp. 3053-3058
    • Lillehoj, E.P.1    Salazar, F.H.2    Mervis, R.J.3    Raum, M.G.4    Chan, H.W.5    Ahmad, N.6    Venkatesan, S.7
  • 19
    • 9444293777 scopus 로고    scopus 로고
    • Unpublished observation
    • Manchester, M. Unpublished observation.
    • Manchester, M.1
  • 20
    • 0028276793 scopus 로고
    • Identification of temperature-sensitive mutants of the human immunodeficiency virus type 1 protease through saturation mutagenesis
    • Manchester, M., L. Everitt, D. D. Loeb, C. A. Hutchison III, and R. Swanstrom. 1994. Identification of temperature-sensitive mutants of the human immunodeficiency virus type 1 protease through saturation mutagenesis. J. Biol. Chem. 269:7689-7695.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7689-7695
    • Manchester, M.1    Everitt, L.2    Loeb, D.D.3    Hutchison III, C.A.4    Swanstrom, R.5
  • 22
    • 0001707601 scopus 로고
    • 3′-Azido-3′-deoxythymidine (BW A509U): An antiviral agent that inhibits the infectivity and cytopathic effect of human T-lymphotropic virus type HI/lymphadenopathy-associated virus in vitro
    • Mitsuya, H., K. J. Welnhold, P. A. Furman, C. M. St, S. N. Lehrman, R. C. Gallo, D. Bolognesi, D. W. Barry, and S. Broder. 1985. 3′-Azido-3′-deoxythymidine (BW A509U): an antiviral agent that inhibits the infectivity and cytopathic effect of human T-lymphotropic virus type HI/lymphadenopathy-associated virus in vitro. Proc. Natl. Acad. Sci. USA 82:7096-7100.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7096-7100
    • Mitsuya, H.1    Welnhold, K.J.2    Furman, P.A.3    St, C.M.4    Lehrman, S.N.5    Gallo, R.C.6    Bolognesi, D.7    Barry, D.W.8    Broder, S.9
  • 23
    • 0027954403 scopus 로고
    • Antiviral activity of human immunodeficiency virus type 1 protease inhibitors in a single cycle of infection: Evidence for a role of protease in the early phase
    • Nagy, K., M. Young, C. Baboonian, J. Merson, P. Whittle, and S. Oroszlan. 1994. Antiviral activity of human immunodeficiency virus type 1 protease inhibitors in a single cycle of infection: evidence for a role of protease in the early phase. J. Virol. 68:757-765.
    • (1994) J. Virol. , vol.68 , pp. 757-765
    • Nagy, K.1    Young, M.2    Baboonian, C.3    Merson, J.4    Whittle, P.5    Oroszlan, S.6
  • 25
    • 0028046926 scopus 로고
    • Determination of kinetic rate constants for the binding of inhibitors to HIV-1 protease and for the association and dissociation of active homodimer
    • Pargellis, C. A., M. M. Morelock, E. T. Graham, P. Kinkade, S. Pav, K. Lubbe, D. Lamarre, and P. C. Anderson. 1994. Determination of kinetic rate constants for the binding of inhibitors to HIV-1 protease and for the association and dissociation of active homodimer. Biochemistry 33:12527-12534.
    • (1994) Biochemistry , vol.33 , pp. 12527-12534
    • Pargellis, C.A.1    Morelock, M.M.2    Graham, E.T.3    Kinkade, P.4    Pav, S.5    Lubbe, K.6    Lamarre, D.7    Anderson, P.C.8
  • 26
    • 0024334170 scopus 로고
    • Role of human immunodeficiency virus type 1-specific protease in core protein maturation and viral infectivity
    • Peng, C., B. K. Ho, T. W. Chang, and N. T. Chang. 1989. Role of human immunodeficiency virus type 1-specific protease in core protein maturation and viral infectivity. J. Virol. 63:2550-2256.
    • (1989) J. Virol. , vol.63 , pp. 2550-12256
    • Peng, C.1    Ho, B.K.2    Chang, T.W.3    Chang, N.T.4
  • 27
    • 0027971621 scopus 로고
    • The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions
    • Pettit, S. C., M. D. Moody, R. S. Wehbie, A. H. Kaplan, P. V. Nantermet, C. A. Klein, and R. Swanstrom. 1994. The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions. J. Virol. 68:8017-8027.
    • (1994) J. Virol. , vol.68 , pp. 8017-8027
    • Pettit, S.C.1    Moody, M.D.2    Wehbie, R.S.3    Kaplan, A.H.4    Nantermet, P.V.5    Klein, C.A.6    Swanstrom, R.7
  • 29
    • 0028873674 scopus 로고
    • Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: Effects on virion particle assembly, release, and infectivity
    • Reicin, A. S., S. Paik, R. D. Berkowitz, J. Luban, I. Lowy, and S. P. Golf. 1995. Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: effects on virion particle assembly, release, and infectivity. J. Virol. 69:642-650.
    • (1995) J. Virol. , vol.69 , pp. 642-650
    • Reicin, A.S.1    Paik, S.2    Berkowitz, R.D.3    Luban, J.4    Lowy, I.5    Golf, S.P.6
  • 30
    • 0025740377 scopus 로고
    • In situ processing of a retroviral nucleocapsid protein by the viral proteinase
    • Roberts, M. M., T. D. Copeland, and S. Oroszlan. 1991. In situ processing of a retroviral nucleocapsid protein by the viral proteinase. Protein Eng. 4:695-700.
    • (1991) Protein Eng. , vol.4 , pp. 695-700
    • Roberts, M.M.1    Copeland, T.D.2    Oroszlan, S.3
  • 31
    • 0024340454 scopus 로고
    • The preparation and biochemical characterization of intact capsids of equine infectious anemia virus
    • Roberts, M. M., and S. Oroszlan. 1989. The preparation and biochemical characterization of intact capsids of equine infectious anemia virus. Biochem. Biophys. Res. Commun. 160:486-494.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 486-494
    • Roberts, M.M.1    Oroszlan, S.2
  • 34
    • 0026476301 scopus 로고
    • Importance of p12 protein in Mason-Pfizer monkey virus assembly and infectivity
    • Sommerfelt, M. A., S. S. Rhee, and E. Hunter. 1992. Importance of p12 protein in Mason-Pfizer monkey virus assembly and infectivity. J. Virol. 66:7005-7011.
    • (1992) J. Virol. , vol.66 , pp. 7005-7011
    • Sommerfelt, M.A.1    Rhee, S.S.2    Hunter, E.3
  • 35
    • 0025000261 scopus 로고
    • Properties of avian retrovirus particles defective in viral protease
    • Stewart, L., G. Schatz, and V. M. Vogt 1990. Properties of avian retrovirus particles defective in viral protease. J. Virol. 64:5076-5092.
    • (1990) J. Virol. , vol.64 , pp. 5076-5092
    • Stewart, L.1    Schatz, G.2    Vogt, V.M.3
  • 36
    • 0026465274 scopus 로고
    • Mutational analysis of the major homology region of Mason-Pfizer monkey virus by use of saturation mutagenesis
    • Strambio de Castillia, C., and E. Hunter. 1992. Mutational analysis of the major homology region of Mason-Pfizer monkey virus by use of saturation mutagenesis. J. Virol. 66:7021-7032.
    • (1992) J. Virol. , vol.66 , pp. 7021-7032
    • Strambio De Castillia, C.1    Hunter, E.2
  • 37
    • 0026676828 scopus 로고
    • Inhibition of HIV by an anti-HIV protease synthetic peptide blocks an early step of viral replication
    • Venaud, S., N. Yahi, J. L. Fehrentz, N. Guettari, D. Nisato, I. Hirsch, and J. C. Chermann. 1992. Inhibition of HIV by an anti-HIV protease synthetic peptide blocks an early step of viral replication. Res. Virol. 143:311-319.
    • (1992) Res. Virol. , vol.143 , pp. 311-319
    • Venaud, S.1    Yahi, N.2    Fehrentz, J.L.3    Guettari, N.4    Nisato, D.5    Hirsch, I.6    Chermann, J.C.7
  • 38
    • 2942745047 scopus 로고
    • Cleavage of Rous sarcoma viral polypeptide precursor into internal structural proteins in vitro involves viral protein p15
    • von der Helm, K. 1977. Cleavage of Rous sarcoma viral polypeptide precursor into internal structural proteins in vitro involves viral protein p15. Proc. Natl. Acad. Sci. USA 74:911-915.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 911-915
    • Von Der Helm, K.1
  • 39
    • 0027160015 scopus 로고
    • Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants
    • Wang, C. T., and E. Barklis. 1993. Assembly, processing, and infectivity of human immunodeficiency virus type 1 gag mutants. J. Virol. 67:4264-4273.
    • (1993) J. Virol. , vol.67 , pp. 4264-4273
    • Wang, C.T.1    Barklis, E.2
  • 40
    • 0017669839 scopus 로고
    • Properties of a P70 proteolytic factor of murine leukemia viruses
    • Yoshinaka, Y., and R. B. Luftig. 1977. Properties of a P70 proteolytic factor of murine leukemia viruses. Cell 12:709-719.
    • (1977) Cell , vol.12 , pp. 709-719
    • Yoshinaka, Y.1    Luftig, R.B.2
  • 41
    • 0026801974 scopus 로고
    • The C terminus of human immunodeficiency virus type 1 matrix protein is involved in early steps of the virus life cycle
    • Yu, X., Q. C. Yu, T. H. Lee, and M. Essex. 1992. The C terminus of human immunodeficiency virus type 1 matrix protein is involved in early steps of the virus life cycle. J. Virol. 66:5667-5670.
    • (1992) J. Virol. , vol.66 , pp. 5667-5670
    • Yu, X.1    Yu, Q.C.2    Lee, T.H.3    Essex, M.4


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