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Volumn 70, Issue 12, 1996, Pages 8645-8652

The role of gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; GENE PRODUCT; VIRUS DNA; VIRUS PROTEIN;

EID: 0029961364     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.12.8645-8652.1996     Document Type: Article
Times cited : (121)

References (48)
  • 1
    • 0003286669 scopus 로고
    • Transfection of molecularly cloned HIV genomes
    • A. Aldovini and B. D. Walker (ed.), Stockton Press, New York
    • Aldovini, A., and M. B. Feinberg. 1990. Transfection of molecularly cloned HIV genomes, p. 166. In A. Aldovini and B. D. Walker (ed.), Techniques in HIV research. Stockton Press, New York.
    • (1990) Techniques in HIV Research , pp. 166
    • Aldovini, A.1    Feinberg, M.B.2
  • 2
    • 0027501033 scopus 로고
    • Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus Gag proteins
    • Bennett, R. P., T. D. Nelle, and J. W. Wills. 1993. Functional chimeras of the Rous sarcoma virus and human immunodeficiency virus Gag proteins. J. Virol. 67:6487-6498.
    • (1993) J. Virol. , vol.67 , pp. 6487-6498
    • Bennett, R.P.1    Nelle, T.D.2    Wills, J.W.3
  • 3
    • 0025608303 scopus 로고
    • A sequence in the carboxy terminus of the HIV-1 matrix protein is highly similar to sequences in membrane-associated proteins of other RNA viruses: Possible functional implications
    • Bloomberg, J., and P. Medstrand. 1990. A sequence in the carboxy terminus of the HIV-1 matrix protein is highly similar to sequences in membrane-associated proteins of other RNA viruses: possible functional implications. New Biol. 2:1044-1046.
    • (1990) New Biol. , vol.2 , pp. 1044-1046
    • Bloomberg, J.1    Medstrand, P.2
  • 4
    • 0023647997 scopus 로고
    • Correct integration of retroviral DNA in vitro
    • Brown, P. O., B. Bowerman, H. E. Varmus, and J. M. Bishop. 1987. Correct integration of retroviral DNA in vitro. Cell 49:347-356.
    • (1987) Cell , vol.49 , pp. 347-356
    • Brown, P.O.1    Bowerman, B.2    Varmus, H.E.3    Bishop, J.M.4
  • 6
    • 0024278041 scopus 로고
    • Sequence and spacing requirements of a retrovirus integration site
    • Colicelli, J., and S. P. Goff. 1988. Sequence and spacing requirements of a retrovirus integration site. J. Mol. Biol. 199:47-50.
    • (1988) J. Mol. Biol. , vol.199 , pp. 47-50
    • Colicelli, J.1    Goff, S.P.2
  • 7
    • 0023084134 scopus 로고
    • Use of eukaryotic expression technology in the functional analysis of cloned genes
    • Cullen, B. 1987. Use of eukaryotic expression technology in the functional analysis of cloned genes. Methods Enzymol. 152:684-704.
    • (1987) Methods Enzymol. , vol.152 , pp. 684-704
    • Cullen, B.1
  • 8
    • 0001931483 scopus 로고
    • Protein biosynthesis and assembly
    • R. Weiss, N. Teich, H. Varmus, and J. Coffin (ed.), Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Dickson, C., R. Eisenman, H. Fan, E. Hunter, and N. Teich. 1984. Protein biosynthesis and assembly, p. 513-648. In R. Weiss, N. Teich, H. Varmus, and J. Coffin (ed.), RNA tumor viruses, vol. 1. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1984) RNA Tumor Viruses , vol.1 , pp. 513-648
    • Dickson, C.1    Eisenman, R.2    Fan, H.3    Hunter, E.4    Teich, N.5
  • 9
    • 0027997831 scopus 로고
    • Functional domains of the capsid protein of human immunodeficiency virus type I
    • Dorfman, T., A. Bukovsky, A. Ohagen, S. Hoglund, and H. Gottlinger. 1994. Functional domains of the capsid protein of human immunodeficiency virus type I. J. Virol. 68:8180-8187.
    • (1994) J. Virol. , vol.68 , pp. 8180-8187
    • Dorfman, T.1    Bukovsky, A.2    Ohagen, A.3    Hoglund, S.4    Gottlinger, H.5
  • 10
    • 0025273268 scopus 로고
    • Cell-induced conformational change in poliovirus: Externalization of the amino terminus of VP1 is responsible for liposome binding
    • Fricks, C. E., and J. M. Hogle. 1990. Cell-induced conformational change in poliovirus: externalization of the amino terminus of VP1 is responsible for liposome binding. J. Virol. 64:1934-1945.
    • (1990) J. Virol. , vol.64 , pp. 1934-1945
    • Fricks, C.E.1    Hogle, J.M.2
  • 11
    • 0028839344 scopus 로고
    • HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase
    • Gallay, P., S. Swingler, J. Song, F. Bushman, and D. Trono. 1995. HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase. Cell 83:569-576.
    • (1995) Cell , vol.83 , pp. 569-576
    • Gallay, P.1    Swingler, S.2    Song, J.3    Bushman, F.4    Trono, D.5
  • 12
    • 0025904765 scopus 로고
    • Assembly and morphology of HIV: Potential effect of structure on viral function
    • Gelderblom, H. R. 1991. Assembly and morphology of HIV: potential effect of structure on viral function. AIDS 5:617-638.
    • (1991) AIDS , vol.5 , pp. 617-638
    • Gelderblom, H.R.1
  • 13
    • 0023099283 scopus 로고
    • Fine structure of the human immunodeficiency virus (HIV) and immunolocalization of structural proteins
    • Gelderblom, H. R., E. H. Hausmann, M. Ozel, G. Pauli, and M. A. Koch. 1987. Fine structure of the human immunodeficiency virus (HIV) and immunolocalization of structural proteins. Virology 156:171-176.
    • (1987) Virology , vol.156 , pp. 171-176
    • Gelderblom, H.R.1    Hausmann, E.H.2    Ozel, M.3    Pauli, G.4    Koch, M.A.5
  • 15
    • 0025283822 scopus 로고
    • Noninfectious human immunodeficiency virus type 1 mutants deficient in genomic RNA
    • Gorelick, R. J., S. M. Nigida, J. R. Bess, L. O. Arthur, L. E. Henderson, and A. Rein. 1990, Noninfectious human immunodeficiency virus type 1 mutants deficient in genomic RNA. J. Virol. 64:3207-3211.
    • (1990) J. Virol. , vol.64 , pp. 3207-3211
    • Gorelick, R.J.1    Nigida, S.M.2    Bess, J.R.3    Arthur, L.O.4    Henderson, L.E.5    Rein, A.6
  • 16
    • 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
  • 17
    • 0025316594 scopus 로고
    • Human immunodeficiency virus-like, nonreplicating. gag-env particles assemble in a recombinant vaccinia virus expression system
    • Haffar, O., J. Garrigues, B. Travis, P. Moran, J. Zarling, and S.-L. Hu. 1990. Human immunodeficiency virus-like, nonreplicating. gag-env particles assemble in a recombinant vaccinia virus expression system. J. Virol. 64:2653-2659.
    • (1990) J. Virol. , vol.64 , pp. 2653-2659
    • Haffar, O.1    Garrigues, J.2    Travis, B.3    Moran, P.4    Zarling, J.5    Hu, S.-L.6
  • 19
    • 0028200823 scopus 로고
    • Role of vif during packing of the core of HIV-1
    • Hoglund, S., A. Ohoagen, K. Lawrence, and D. Gabzuda. 1994. Role of vif during packing of the core of HIV-1. Virology 201:349-355.
    • (1994) Virology , vol.201 , pp. 349-355
    • Hoglund, S.1    Ohoagen, A.2    Lawrence, K.3    Gabzuda, D.4
  • 20
    • 0022271270 scopus 로고
    • Point mutations in the P30 domain of the gag gene of the Moloney murine leukemia virus
    • Hsu, H.-W., P. Schwartzberg, and S. Goff. 1985. Point mutations in the P30 domain of the gag gene of the Moloney murine leukemia virus. Virology 142:211-214.
    • (1985) Virology , vol.142 , pp. 211-214
    • Hsu, H.-W.1    Schwartzberg, P.2    Goff, S.3
  • 21
    • 0024392730 scopus 로고
    • Human immunodeficiency virus-like particles produced by a vaccinia expression vector
    • Karacostas, V., K. Nagashima, M. A. Gonda, and B. Moss. 1989. Human immunodeficiency virus-like particles produced by a vaccinia expression vector. Proc. Natl. Acad. Sci. USA 86:8964-8967.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8964-8967
    • Karacostas, V.1    Nagashima, K.2    Gonda, M.A.3    Moss, B.4
  • 23
    • 0029013585 scopus 로고
    • The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity
    • Krausslich, H.-G., M. Facke, A.-M. Heuser, J. Konvalinka, and H. Zentgraf. 1995. The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity. J. Virol. 69:3407-3419.
    • (1995) J. Virol. , vol.69 , pp. 3407-3419
    • Krausslich, H.-G.1    Facke, M.2    Heuser, A.-M.3    Konvalinka, J.4    Zentgraf, H.5
  • 24
    • 0028805216 scopus 로고
    • The vif protein of human and simian immunodeficiency viruses is packaged into virions and associated with viral core structures
    • Liu, H., X. Wu, M. Newman, G. Shaw, B. H. Hahn, and J. C. Kappes. 1995. The vif protein of human and simian immunodeficiency viruses is packaged into virions and associated with viral core structures. J. Virol. 69:7630-7638.
    • (1995) J. Virol. , vol.69 , pp. 7630-7638
    • Liu, H.1    Wu, X.2    Newman, M.3    Shaw, G.4    Hahn, B.H.5    Kappes, J.C.6
  • 25
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type I gag protein hinds to cyclophilins A and B
    • Luban, J., K. L. Bossolt, E. K. Franke, G. V. Kalpana, and S. P. Goff. 1993. Human immunodeficiency virus type I gag protein hinds to cyclophilins A and B. Cell 73:1067-1078.
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.P.5
  • 26
    • 0027278132 scopus 로고
    • Effect of linker insertion mutations in the human immunodeficiency virus type 1 gag gene on activation of viral protease expressed in bacteria
    • Luban, J., C. Lee, and S. P. Goff. 1993. Effect of linker insertion mutations in the human immunodeficiency virus type 1 gag gene on activation of viral protease expressed in bacteria. J. Virol. 67:3630-3634.
    • (1993) J. Virol. , vol.67 , pp. 3630-3634
    • Luban, J.1    Lee, C.2    Goff, S.P.3
  • 27
    • 0028342554 scopus 로고
    • Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis
    • Mammano, F., A. Ohagen, S. Hoglund, and H. G. Gottlinger. 1994. Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis. J. Virol. 68:4927-4936.
    • (1994) J. Virol. , vol.68 , pp. 4927-4936
    • Mammano, F.1    Ohagen, A.2    Hoglund, S.3    Gottlinger, H.G.4
  • 28
    • 0026585458 scopus 로고
    • Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells
    • Mergener, K., M. Facke, R. Welker, V. Brinkmann, H. R. Gelderblom, and H. G. Krausslich. 1992. Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells. Virology 186:25-39.
    • (1992) Virology , vol.186 , pp. 25-39
    • Mergener, K.1    Facke, M.2    Welker, R.3    Brinkmann, V.4    Gelderblom, H.R.5    Krausslich, H.G.6
  • 29
    • 0027200296 scopus 로고
    • Mutations in the protease gene of human immunodeficiency virus type 1 affect release and stability of virus particles
    • Park, J., and C. D. Morrow. 1993. Mutations in the protease gene of human immunodeficiency virus type 1 affect release and stability of virus particles. Virology 194:843-8511.
    • (1993) Virology , vol.194 , pp. 843-8511
    • Park, J.1    Morrow, C.D.2
  • 30
    • 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. 63:2550-2556.
    • (1989) J. Virol. , vol.63 , pp. 2550-2556
    • Peng, C.1    Ho, B.K.2    Chang, T.W.3    Chang, N.T.4
  • 31
    • 0021112599 scopus 로고
    • Localization of lipid-protein and protein-protein interactions within the murine retrovirus gag precursor by a novel peptidemapping technique
    • Pepinsky, R. B. 1983. Localization of lipid-protein and protein-protein interactions within the murine retrovirus gag precursor by a novel peptidemapping technique. J. Biol. Chem. 258:11229-11235.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11229-11235
    • Pepinsky, R.B.1
  • 32
    • 0026332220 scopus 로고
    • Isolation and characterization of a dideoxyguanosine triphosphate-resistant mutant of human immunodeficiency virus reverse transcriptase
    • Prasad, V. R., I. Lowy, T. De Los Santos, L. Chiang, and S. P. Goff. 1991. Isolation and characterization of a dideoxyguanosine triphosphate-resistant mutant of human immunodeficiency virus reverse transcriptase. Proc. Natl. Acad. Sci. USA 88:11363-11367.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11363-11367
    • Prasad, V.R.1    Lowy, I.2    De Los Santos, T.3    Chiang, L.4    Goff, S.P.5
  • 33
    • 0020561224 scopus 로고
    • Immunoglobulin gene transcription is activated by downstream sequence elements
    • Queen, C., and D. Baltimore. 1983. Immunoglobulin gene transcription is activated by downstream sequence elements. Cell 33:741-748.
    • (1983) Cell , vol.33 , pp. 741-748
    • Queen, C.1    Baltimore, D.2
  • 35
    • 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. Paik, R. Berkowitz, J. Luban, I. Lowy, and S. Goff. 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.1    Paik, S.2    Berkowitz, R.3    Luban, J.4    Lowy, I.5    Goff, S.6
  • 36
    • 0026572387 scopus 로고
    • Expression and extracellular release of human immunodeficiency virus type 1 Gag precursors by recombinant baculovirus-infected cells
    • Royer, M., S. S. Hong, B. Gay, M. Cerutti, and P. Boulanger. 1992. Expression and extracellular release of human immunodeficiency virus type 1 Gag precursors by recombinant baculovirus-infected cells. J. Virol. 66:3230-3235.
    • (1992) J. Virol. , vol.66 , pp. 3230-3235
    • Royer, M.1    Hong, S.S.2    Gay, B.3    Cerutti, M.4    Boulanger, P.5
  • 37
    • 0025312215 scopus 로고
    • Production of human immunodeficiency virus (HIV)-like particles from cells infected with recombinant vaccinia viruses carrying the gag gene of HIV
    • Shioda, A. J., M.-I. Cho, M.-L. Hammarskjold, and D. Rekosh. 1990. Production of human immunodeficiency virus (HIV)-like particles from cells infected with recombinant vaccinia viruses carrying the gag gene of HIV. Virology 175:139-148.
    • (1990) Virology , vol.175 , pp. 139-148
    • Shioda, A.J.1    Cho, M.-I.2    Hammarskjold, M.-L.3    Rekosh, D.4
  • 38
    • 0025329086 scopus 로고
    • gag-pol expressed from a simian virus 40 late replacement vector are efficiently processed and assembled into virus-like particles
    • gag-pol expressed from a simian virus 40 late replacement vector are efficiently processed and assembled into virus-like particles. J. Virol. 64:2743-2750.
    • (1990) J. Virol. , vol.64 , pp. 2743-2750
    • Smith, A.J.1    Cho, M.-I.2    Hammarskjold, M.-L.3    Rekosh, D.4
  • 39
    • 0029130067 scopus 로고
    • Characterization of deletion mutants in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporation
    • Srinivasakumar, N., M.-L. Hammarskjold, and D. Rekosh. 1995. Characterization of deletion mutants in the capsid region of human immunodeficiency virus type 1 that affect particle formation and Gag-Pol precursor incorporation. J. Virol. 69:6106-6114.
    • (1995) J. Virol. , vol.69 , pp. 6106-6114
    • Srinivasakumar, N.1    Hammarskjold, M.-L.2    Rekosh, D.3
  • 40
    • 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
  • 41
    • 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
  • 42
    • 0015962730 scopus 로고
    • Structural studies of avian myeloblastosis virus: Comparison of polypeptides in virion and core component by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Stromberg, K., N. E. Hurley, N. L. Davis, R. R. Rueckert, and E. Fleissner. 1974. Structural studies of avian myeloblastosis virus: comparison of polypeptides in virion and core component by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. J. Virol. 13:513-528.
    • (1974) J. Virol. , vol.13 , pp. 513-528
    • Stromberg, K.1    Hurley, N.E.2    Davis, N.L.3    Rueckert, R.R.4    Fleissner, E.5
  • 43
    • 0027179103 scopus 로고
    • Vif is crucial for human immunodeficiency virus type 3 proviral DNA synthesis in infected cells
    • von Schwedler, U., J. Song, C. Aiken, and D. Trono. 1993. vif is crucial for human immunodeficiency virus type 3 proviral DNA synthesis in infected cells. J. Virol. 67:4945-4955.
    • (1993) J. Virol. , vol.67 , pp. 4945-4955
    • Von Schwedler, U.1    Song, J.2    Aiken, C.3    Trono, D.4
  • 44
    • 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
  • 45
    • 0027328715 scopus 로고
    • Characterization of a small (25-kilodalton) derivative of the Rous sarcoma virus Gag protein competent for particle release
    • Weldon, R. A. J., and J. W. Wills. 1993. Characterization of a small (25-kilodalton) derivative of the Rous sarcoma virus Gag protein competent for particle release. J. Virol. 67:5550-5561.
    • (1993) J. Virol. , vol.67 , pp. 5550-5561
    • Weldon, R.A.J.1    Wills, J.W.2
  • 46
    • 0025728301 scopus 로고
    • Form, function, and use of retroviral Gag proteins
    • Wills, J. W., and R. C. Craven. 1991. Form, function, and use of retroviral Gag proteins. AIDS 5:639-654.
    • (1991) AIDS , vol.5 , pp. 639-654
    • Wills, J.W.1    Craven, R.C.2
  • 47
    • 0017742049 scopus 로고
    • Murine leukemia virus morphogenesis: Cleavage of P70 in vitro can be accompanied by a shift from a concentrically coiled internal strand ("immature") to a collapsed ("mature") form of the virus core
    • Yoshinaka, Y., and R. B. Luftig. 1977. Murine leukemia virus morphogenesis: cleavage of P70 in vitro can be accompanied by a shift from a concentrically coiled internal strand ("immature") to a collapsed ("mature") form of the virus core. Proc. Natl. Acad. Sci. USA 74:3446-3450.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3446-3450
    • Yoshinaka, Y.1    Luftig, R.B.2
  • 48
    • 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. 64:5667-5670.
    • (1992) J. Virol. , vol.64 , pp. 5667-5670
    • Yu, X.1    Yu, Q.C.2    Lee, T.H.3    Essex, M.4


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