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Volumn 75, Issue 12, 2001, Pages 5473-5481

The late stage of human immunodeficiency virus type 1 assembly is an energy-dependent process

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GAG PROTEIN; VIRUS PROTEIN;

EID: 0035012785     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.75.12.5473-5481.2001     Document Type: Article
Times cited : (31)

References (48)
  • 1
    • 0024285837 scopus 로고
    • Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome)
    • Arrigo, A. P., K. Tanaka, A. L. Goldberg, and W. J. Welch. 1988. Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome). Nature 331:192-194.
    • (1988) Nature , vol.331 , pp. 192-194
    • Arrigo, A.P.1    Tanaka, K.2    Goldberg, A.L.3    Welch, W.J.4
  • 2
    • 0026592529 scopus 로고
    • Tightly hound zinc in human immunodeficiency virus type 1, human T-cell leukemia virus type 1, and other retroviruses
    • Bess, J. W., Jr., P. J. Powell, H. J. Issaq, L. J. Schumack, M. K. Grimes, L. E. Henderson, and L. O. Arthur. 1992. Tightly hound zinc in human immunodeficiency virus type 1, human T-cell leukemia virus type 1, and other retroviruses. J. Virol. 66:840-847.
    • (1992) J. Virol. , vol.66 , pp. 840-847
    • Bess J.W., Jr.1    Powell, P.J.2    Issaq, H.J.3    Schumack, L.J.4    Grimes, M.K.5    Henderson, L.E.6    Arthur, L.O.7
  • 3
    • 0033779574 scopus 로고    scopus 로고
    • Multiple blocks to human immunodeficiency virus type 1 replication in rodent cells
    • Bieniasz, P. D., and B. R. Cullen. 2000. Multiple blocks to human immunodeficiency virus type 1 replication in rodent cells. J. Virol. 74:9868-9877.
    • (2000) J. Virol. , vol.74 , pp. 9868-9877
    • Bieniasz, P.D.1    Cullen, B.R.2
  • 4
    • 0033027711 scopus 로고    scopus 로고
    • In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain
    • Campbell, S., and A. Rein. 1999. In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain. J. Virol. 73:2270-2279.
    • (1999) J. Virol. , vol.73 , pp. 2270-2279
    • Campbell, S.1    Rein, A.2
  • 5
    • 0033981656 scopus 로고    scopus 로고
    • Biochemical requirements of virus wrapping by the endoplasmic reticulum: Involvement of ATP and endoplasmic reticulum calcium store during envelopment of African swine fever virus
    • Cobbold, C., S. M. Brookes, and T. Wileman. 2000. Biochemical requirements of virus wrapping by the endoplasmic reticulum: involvement of ATP and endoplasmic reticulum calcium store during envelopment of African swine fever virus. J. Virol. 74:2151-2160.
    • (2000) J. Virol. , vol.74 , pp. 2151-2160
    • Cobbold, C.1    Brookes, S.M.2    Wileman, T.3
  • 6
    • 0024294338 scopus 로고
    • Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin
    • Copeland, C. S., K. P. Zimmer, K. R. Wagner, G. A. Healey, I. Mellman, and A. Helenius. 1988. Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin. Cell 53:197-209.
    • (1988) Cell , vol.53 , pp. 197-209
    • Copeland, C.S.1    Zimmer, K.P.2    Wagner, K.R.3    Healey, G.A.4    Mellman, I.5    Helenius, A.6
  • 7
    • 0032980410 scopus 로고    scopus 로고
    • ATP depletion blocks herpes simplex virus DNA packaging and capsid maturation
    • Dasgupta, A., and D. W. Wilson. 1999. ATP depletion blocks herpes simplex virus DNA packaging and capsid maturation. J. Virol. 73:2006-2015.
    • (1999) J. Virol. , vol.73 , pp. 2006-2015
    • Dasgupta, A.1    Wilson, D.W.2
  • 8
    • 0023945067 scopus 로고
    • In vitro fusion of endosomes following receptor-mediated enducytosis
    • Diaz, R., L. Mayorga, and P. Stahl. 1988. In vitro fusion of endosomes following receptor-mediated enducytosis. J. Biol. Chem. 263:6093-6100.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6093-6100
    • Diaz, R.1    Mayorga, L.2    Stahl, P.3
  • 9
    • 0023550869 scopus 로고
    • Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers
    • Doms, R. W., D. S. Keller, A. Helenius, and W. E. Balch. 1987. Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers. J. Cell Biol. 105:1957-1969.
    • (1987) J. Cell Biol. , vol.105 , pp. 1957-1969
    • Doms, R.W.1    Keller, D.S.2    Helenius, A.3    Balch, W.E.4
  • 10
    • 0027997831 scopus 로고
    • Functional domains of the capsid protein of human immunodeficiency virus type 1
    • Dorfman, T., A. Bukovsky, Å. Öhagen, S. Höglund, and H. G. Göttlinger. 1994. Functional domains of the capsid protein of human immunodeficiency virus type 1. J. Virol. 68:8180-8187.
    • (1994) J. Virol. , vol.68 , pp. 8180-8187
    • Dorfman, T.1    Bukovsky, A.2    Öhagen, Å.3    Höglund, S.4    Göttlinger, H.G.5
  • 11
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 Gag proteins: Diverse functions in the virus life cycle
    • Freed, E. O. 1998. HIV-1 Gag proteins: diverse functions in the virus life cycle. Virology 251:1-15.
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 12
    • 0031614235 scopus 로고    scopus 로고
    • Recent advances and remaining problems in HIV assembly
    • Garnier, L., J. Bradford Bowzard, and J. W. Wills. 1998. Recent advances and remaining problems in HIV assembly. AIDS 12:S5-S16.
    • (1998) AIDS , vol.12
    • Garnier, L.1    Bradford Bowzard, J.2    Wills, J.W.3
  • 14
    • 0023099283 scopus 로고
    • Fine structure of human immunodeficiency virus (HIV) and immunolocalization of structural proteins
    • Gelderblom, H. R., E. H. S. Hausmann, M. Ozel, G. Pauli, and M. A. Koch. 1987. Fine structure of 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.S.2    Ozel, M.3    Pauli, G.4    Koch, M.A.5
  • 17
    • 0026317877 scopus 로고
    • Effect of mutations affecting the p6 Gag protein on human immunodeficiency virus particle release
    • Gottlinger, H. G., T. Dorfman, J. G. Sodroski, and W. A. Haseltine. 1991. Effect of mutations affecting the p6 Gag protein on human immunodeficiency virus particle release. Proc. Natl. Acad. Sci. USA 88:3195-3199.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3195-3199
    • Gottlinger, H.G.1    Dorfman, T.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 18
    • 0024338208 scopus 로고
    • Identification of protein intermediates in the processing of the p55 HIV-1 gag precursor in cells infected with recombinant vaccinia virus
    • Gowda, S. D., B. S. Stein, and E. G. Engleman. 1989. Identification of protein intermediates in the processing of the p55 HIV-1 gag precursor in cells infected with recombinant vaccinia virus. J. Biol. Chem. 264:8459-8462.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8459-8462
    • Gowda, S.D.1    Stein, B.S.2    Engleman, E.G.3
  • 19
    • 0026515142 scopus 로고
    • Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: Posttranslational modifications, proteolytic processings, and complete aminci acid sequences
    • Henderson, L. E., M. A. Bowers, R. C. Sowder II, S. A. Serabyn, D. G. Johnson, J. W. Bess, Jr., L. O. Arthur, D. K. Bryant, and C. Fenselau. 1992. Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: posttranslational modifications, proteolytic processings, and complete aminci acid sequences. J. Virol. 66:1856-1865.
    • (1992) J. Virol. , vol.66 , pp. 1856-1865
    • Henderson, L.E.1    Bowers, M.A.2    Sowder R.C. II3    Serabyn, S.A.4    Johnson, D.G.5    Bess J.W., Jr.6    Arthur, L.O.7    Bryant, D.K.8    Fenselau, C.9
  • 20
    • 0033856584 scopus 로고    scopus 로고
    • Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging
    • Hermida-Matsumoto, L., and M. D. Resh. 2000. Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging. J. Virol. 74:8670-8679.
    • (2000) J. Virol. , vol.74 , pp. 8670-8679
    • Hermida-Matsumoto, L.1    Resh, M.D.2
  • 21
    • 0027932364 scopus 로고
    • The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency
    • Kaplan, A. H., M. Manchester, and R. Swanstrom. 1994. The activity of the protease of human immunodeficiency virus type 1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency. J. Virol. 68:6782-6786.
    • (1994) J. Virol. , vol.68 , pp. 6782-6786
    • Kaplan, A.H.1    Manchester, M.2    Swanstrom, R.3
  • 22
    • 0025828543 scopus 로고
    • Human immunodeficiency virus type 1 Gag proteins are processed in two cellular compartments
    • Kaplan, A. H., and R. Swanstrom. 1991. Human immunodeficiency virus type 1 Gag proteins are processed in two cellular compartments. Proc. Natl. Acad. Sci. USA 88:4528-4532.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4528-4532
    • Kaplan, A.H.1    Swanstrom, R.2
  • 23
    • 0031044374 scopus 로고    scopus 로고
    • A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system
    • Lingappa, J. R., R. L. Hill, M. L. Wong, and R. S. Hegde. 1997. A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system. J. Cell Biol. 136:567-581.
    • (1997) J. Cell Biol. , vol.136 , pp. 567-581
    • Lingappa, J.R.1    Hill, R.L.2    Wong, M.L.3    Hegde, R.S.4
  • 26
    • 0033600753 scopus 로고    scopus 로고
    • In vitro assembly of human immunodeficiency virus type 1 Gag protein
    • Morikawa, Y., T. Goto, and K. Sano. 1999. In vitro assembly of human immunodeficiency virus type 1 Gag protein. J. Biol. Chem. 274:27997-28002.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27997-28002
    • Morikawa, Y.1    Goto, T.2    Sano, K.3
  • 27
    • 0034108444 scopus 로고    scopus 로고
    • Relationship between human immunodeficiency virus type 1 Gag mullimerization and membrane binding
    • Ono, A., D. Demirov, and E. O. Freed. 2000. Relationship between human immunodeficiency virus type 1 Gag mullimerization and membrane binding. J. Virol. 74:5142-5150.
    • (2000) J. Virol. , vol.74 , pp. 5142-5150
    • Ono, A.1    Demirov, D.2    Freed, E.O.3
  • 28
    • 0032951899 scopus 로고    scopus 로고
    • Binding of human immunodeficiency virus type 1 Gag to membrane: Role of the matrix amino terminus
    • Ono, A., and E. O. Freed. 1999. Binding of human immunodeficiency virus type 1 Gag to membrane: role of the matrix amino terminus. J. Virol. 73:4136-4144.
    • (1999) J. Virol. , vol.73 , pp. 4136-4144
    • Ono, A.1    Freed, E.O.2
  • 29
    • 0344766117 scopus 로고    scopus 로고
    • Opposing effects of human immunodeficiency virus type 1 matrix mutations support a myristyl switch model of Gag membrane targeting
    • Paillart, J.-C., and H. G. Gottlinger. 1999, Opposing effects of human immunodeficiency virus type 1 matrix mutations support a myristyl switch model of Gag membrane targeting. J. Virol. 73:2604-2612.
    • (1999) J. Virol. , vol.73 , pp. 2604-2612
    • Paillart, J.-C.1    Gottlinger, H.G.2
  • 31
    • 0033989193 scopus 로고    scopus 로고
    • A cell-line-specific defect in the intracellular transport and release of assembled retroviral capsids
    • Parker, S. D., and E. Hunter. 2000. A cell-line-specific defect in the intracellular transport and release of assembled retroviral capsids. J. Virol. 74: 784-795.
    • (2000) J. Virol. , vol.74 , pp. 784-795
    • Parker, S.D.1    Hunter, E.2
  • 32
    • 0034700146 scopus 로고    scopus 로고
    • Ubiquitin is part of the retrovirus budding machinery
    • Patnaik, A., V. Chau, and J. W. Wills. 2000. Ubiquitin is part of the retrovirus budding machinery. Proc. Natl. Acad. Sci. USA 97:13069-13074.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13069-13074
    • Patnaik, A.1    Chau, V.2    Wills, J.W.3
  • 33
    • 0019266949 scopus 로고
    • Role of intracellular proteins in the regulation of calcium action and transmitter release during exocytosis
    • Pollard, H. B., C. J. Pazoles, C. E. Creutz, and O. Zinder. 1980. Role of intracellular proteins in the regulation of calcium action and transmitter release during exocytosis. Monogr. Neural Sci. 7:106-116.
    • (1980) Monogr. Neural Sci. , vol.7 , pp. 106-116
    • Pollard, H.B.1    Pazoles, C.J.2    Creutz, C.E.3    Zinder, O.4
  • 34
    • 0025310611 scopus 로고
    • Preassembled capsids of type D retroviruses contain a signal sufficient for targeting specifically to the plasma membrane
    • Rhee, S. S., H. Hui, and E. Hunter. 1990. Preassembled capsids of type D retroviruses contain a signal sufficient for targeting specifically to the plasma membrane. J. Virol. 64:3844-3852.
    • (1990) J. Virol. , vol.64 , pp. 3844-3852
    • Rhee, S.S.1    Hui, H.2    Hunter, E.3
  • 37
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert, U., L. C. Anton, J. Gibbs, C. C. Norbury, J. W. Yewdell, and J. R. Bennink. 2000. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404:770-774.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 39
    • 0030763024 scopus 로고    scopus 로고
    • Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism
    • Spearman, P., R. Horton, L. Ratner, and I. Kuli-Zade. 1997. Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism. J. Virol. 71:6582-6592.
    • (1997) J. Virol. , vol.71 , pp. 6582-6592
    • Spearman, P.1    Horton, R.2    Ratner, L.3    Kuli-Zade, I.4
  • 41
    • 0033548603 scopus 로고    scopus 로고
    • Cycloheximide-induced T-cell death is mediated by a Fas-associated death domain-dependent mechanism
    • Tang, D., J. M. Lahti, J. Grenet, and V. J. Kidd. 1999. Cycloheximide-induced T-cell death is mediated by a Fas-associated death domain-dependent mechanism. J. Biol. Chem. 274:7245-7252.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7245-7252
    • Tang, D.1    Lahti, J.M.2    Grenet, J.3    Kidd, V.J.4
  • 42
    • 0034086728 scopus 로고    scopus 로고
    • Kinetic analysis of human immunodeficiency virus type 1 assembly reveals the presence of sequential intermediates
    • Tritel, M., and M. D. Resh. 2000. Kinetic analysis of human immunodeficiency virus type 1 assembly reveals the presence of sequential intermediates. J. Virol. 74:5845-5855.
    • (2000) J. Virol. , vol.74 , pp. 5845-5855
    • Tritel, M.1    Resh, M.D.2
  • 43
    • 84866476582 scopus 로고    scopus 로고
    • 2-terminal myristoylation and palmitoylation at cysteine-3
    • 2-terminal myristoylation and palmitoylation at cysteine-3. J. Cell Biol. 136:1023-1035.
    • (1997) J. Cell Biol. , vol.136 , pp. 1023-1035
    • Van't Hof, W.1    Resh, M.D.2
  • 44
    • 2642608675 scopus 로고    scopus 로고
    • Type D retrovirus capsid assembly and release are active events requiring ATP
    • Weldon, R. A., Jr., W. B. Parker, M. Sakalian, and E. Hunter. 1998. Type D retrovirus capsid assembly and release are active events requiring ATP. J. Virol. 72:3098-3106.
    • (1998) J. Virol. , vol.72 , pp. 3098-3106
    • Weldon R.A., Jr.1    Parker, W.B.2    Sakalian, M.3    Hunter, E.4
  • 45
    • 0033809342 scopus 로고    scopus 로고
    • Gag in immature human immunodeficiency virus type 1 particles
    • Gag in immature human immunodeficiency virus type 1 particles. J. Virol. 74:9381-9387.
    • (2000) J. Virol. , vol.74 , pp. 9381-9387
    • Wyma, D.J.1    Kotov, A.2    Aiken, C.3
  • 46
    • 0032546790 scopus 로고
    • c-myc mRNA is down-regulated during myogenic differentiation by accelerated decay that depends on translation of regulatory coding elements
    • Yeilding, N. M., W. N. Procopio, M. T. Rehman, and W. M. Lee. 1948. c-myc mRNA is down-regulated during myogenic differentiation by accelerated decay that depends on translation of regulatory coding elements. J. Biol. Chem. 273:15749-15757.
    • (1948) J. Biol. Chem. , vol.273 , pp. 15749-15757
    • Yeilding, N.M.1    Procopio, W.N.2    Rehman, M.T.3    Lee, W.M.4
  • 47
    • 0028218274 scopus 로고
    • Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids
    • Zhou, W., L. J. Parent, J. W. Wills, and M. D. Resh. 1994. Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. J. Virol. 68:2556-2569.
    • (1994) J. Virol. , vol.68 , pp. 2556-2569
    • Zhou, W.1    Parent, L.J.2    Wills, J.W.3    Resh, M.D.4
  • 48
    • 0029861657 scopus 로고    scopus 로고
    • Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
    • Zhou, W., and M. D. Resh. 1996. Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. J. Virol. 70:8540-8548.
    • (1996) J. Virol. , vol.70 , pp. 8540-8548
    • Zhou, W.1    Resh, M.D.2


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