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Volumn 80, Issue 16, 2006, Pages 7939-7951

Mutation of dileucine-like motifs in the human immunodeficiency virus type 1 capsid disrupts virus assembly, Gag-Gag interactions, Gag-membrane binding, and virion maturation

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN;

EID: 33746800672     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00355-06     Document Type: Article
Times cited : (56)

References (52)
  • 1
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino, J. S., and L. M. Traub. 2003. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72:395-447.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 2
    • 0032874018 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein
    • Burniston, M. T., A. Cimarelli, J. Colgan, S. P. Curtis, and J. Luban. 1999. Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein. J. Virol. 73:8527-8540.
    • (1999) J. Virol. , vol.73 , pp. 8527-8540
    • Burniston, M.T.1    Cimarelli, A.2    Colgan, J.3    Curtis, S.P.4    Luban, J.5
  • 3
    • 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
  • 4
    • 0029103178 scopus 로고
    • Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
    • Campbell, S., and V. M. Vogt. 1995. Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1. J. Virol. 69:6487-6497.
    • (1995) J. Virol. , vol.69 , pp. 6487-6497
    • Campbell, S.1    Vogt, V.M.2
  • 5
    • 0034011267 scopus 로고    scopus 로고
    • Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA
    • Cimarelli, A., S. Sandin, S. Hoglund, and J. Luban. 2000. Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA. J. Virol. 74:3046-3057.
    • (2000) J. Virol. , vol.74 , pp. 3046-3057
    • Cimarelli, A.1    Sandin, S.2    Hoglund, S.3    Luban, J.4
  • 6
    • 18144420374 scopus 로고    scopus 로고
    • Biochemical characterization of Rous sarcoma virus MA protein interaction with membranes
    • Dalton, A. K., P. S. Murray, D. Murray, and V. M. Vogt. 2005. Biochemical characterization of Rous sarcoma virus MA protein interaction with membranes. J. Virol. 79:6227-6238.
    • (2005) J. Virol. , vol.79 , pp. 6227-6238
    • Dalton, A.K.1    Murray, P.S.2    Murray, D.3    Vogt, V.M.4
  • 7
    • 0032506295 scopus 로고    scopus 로고
    • The role of nucleocapsid of HIV-1 in virus assembly
    • Dawson, L., and X. F. Yu. 1998. The role of nucleocapsid of HIV-1 in virus assembly. Virology 251:141-157.
    • (1998) Virology , vol.251 , pp. 141-157
    • Dawson, L.1    Yu, X.F.2
  • 8
    • 0041845304 scopus 로고    scopus 로고
    • Thermodynamic dissection of a low affinity protein-protein interface involved in human immunodeficiency virus assembly
    • del Alamo, M., J. L. Neira, and M. G. Mateu. 2003. Thermodynamic dissection of a low affinity protein-protein interface involved in human immunodeficiency virus assembly. J. Biol. Chem. 278:27923-27929.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27923-27929
    • Del Alamo, M.1    Neira, J.L.2    Mateu, M.G.3
  • 9
    • 9744221135 scopus 로고    scopus 로고
    • Retrovirus budding
    • Demirov, D. G., and E. O. Freed. 2004. Retrovirus budding. Virus Res. 106:87-102.
    • (2004) Virus Res. , vol.106 , pp. 87-102
    • Demirov, D.G.1    Freed, E.O.2
  • 11
    • 0027997831 scopus 로고
    • Functional domains of the capsid protein of human immunodeficiency virus type 1
    • Dorfman, T., A. Bukovsky, A. Ohagen, S. Hoglund, and H. G. Gottlinger. 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    Ohagen, A.3    Hoglund, S.4    Gottlinger, H.G.5
  • 12
    • 0026762403 scopus 로고
    • Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro
    • Ehrlich, L. S., B. E. Agresta, and C. A. Carter. 1992. Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro. J. Virol. 66:4874-4883.
    • (1992) J. Virol. , vol.66 , pp. 4874-4883
    • Ehrlich, L.S.1    Agresta, B.E.2    Carter, C.A.3
  • 13
    • 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
  • 14
    • 0029062117 scopus 로고
    • Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection
    • Freed, E. O., G. Englund, and M. A. Martin. 1995. Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection. J. Virol. 69:3949-3954.
    • (1995) J. Virol. , vol.69 , pp. 3949-3954
    • Freed, E.O.1    Englund, G.2    Martin, M.A.3
  • 15
    • 0028209824 scopus 로고
    • Evidence for a functional interaction between the V1/V2 and C4 domains of human immunodeficiency virus type 1 envelope glycoprotein gp120
    • Freed, E. O., and M. A. Martin. 1994. Evidence for a functional interaction between the V1/V2 and C4 domains of human immunodeficiency virus type 1 envelope glycoprotein gp120. J. Virol. 68:2503-2512.
    • (1994) J. Virol. , vol.68 , pp. 2503-2512
    • Freed, E.O.1    Martin, M.A.2
  • 16
    • 0028234481 scopus 로고
    • Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production
    • Freed, E. O., J. M. Orenstein, A. J. Buckler-White, and M. A. Martin. 1994. Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production. J. Virol. 68:5311-5320.
    • (1994) J. Virol. , vol.68 , pp. 5311-5320
    • Freed, E.O.1    Orenstein, J.M.2    Buckler-White, A.J.3    Martin, M.A.4
  • 17
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • Gamble, T. R., F. F. Vajdos, S. Yoo, D. K. Worthylake, M. Houseweart, W. I. Sundquist, and C. P. Hill. 1996. Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell 87:1285-1294.
    • (1996) Cell , vol.87 , pp. 1285-1294
    • Gamble, T.R.1    Vajdos, F.F.2    Yoo, S.3    Worthylake, D.K.4    Houseweart, M.5    Sundquist, W.I.6    Hill, C.P.7
  • 21
    • 0031954466 scopus 로고    scopus 로고
    • N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles
    • Gross, I., H. Hohenberg, C. Huckhagel, and H. G. Krausslich. 1998. N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles. J. Virol. 72:4798-4810.
    • (1998) J. Virol. , vol.72 , pp. 4798-4810
    • Gross, I.1    Hohenberg, H.2    Huckhagel, C.3    Krausslich, H.G.4
  • 22
    • 0030682425 scopus 로고    scopus 로고
    • In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus
    • Gross, I., H. Hohenberg, and H. G. Krausslich. 1997. In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus. Eur. J. Biochem. 249:592-600.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 592-600
    • Gross, I.1    Hohenberg, H.2    Krausslich, H.G.3
  • 23
    • 0028971135 scopus 로고
    • p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
    • Huang, M., J. M. Orenstein, M. A. Martin, and E. O. Freed. 1995. p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. J. Virol. 69:6810-6818.
    • (1995) J. Virol. , vol.69 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 24
    • 0031980211 scopus 로고    scopus 로고
    • Role of matrix in an early postentry step in the human immunodeficiency virus type 1 life cycle
    • Kiernan, R. E., A. Ono, G. Englund, and E. O. Freed. 1998. Role of matrix in an early postentry step in the human immunodeficiency virus type 1 life cycle. J. Virol. 72:4116-4126.
    • (1998) J. Virol. , vol.72 , pp. 4116-4126
    • Kiernan, R.E.1    Ono, A.2    Englund, G.3    Freed, E.O.4
  • 25
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li, S., C. P. Hill, W. I. Sundquist, and J. T. Finch. 2000. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 407:409-413.
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 26
    • 0037303648 scopus 로고    scopus 로고
    • A structurally disordered region at the C terminus of capsid plays essential roles in multimerization and membrane binding of the Gag protein of human immunodeficiency virus type 1
    • Liang, C., J. Hu, J. B. Whitney, L. Kleiman, and M. A. Wainberg. 2003. A structurally disordered region at the C terminus of capsid plays essential roles in multimerization and membrane binding of the Gag protein of human immunodeficiency virus type 1. J. Virol. 77:1772-1783.
    • (2003) J. Virol. , vol.77 , pp. 1772-1783
    • Liang, C.1    Hu, J.2    Whitney, J.B.3    Kleiman, L.4    Wainberg, M.A.5
  • 27
    • 2442662800 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag contains a dileucine-like motif that regulates association with multivesicular bodies
    • Lindwasser, O. W., and M. D. Resh. 2004. Human immunodeficiency virus type 1 Gag contains a dileucine-like motif that regulates association with multivesicular bodies. J. Virol. 78:6013-6023.
    • (2004) J. Virol. , vol.78 , pp. 6013-6023
    • Lindwasser, O.W.1    Resh, M.D.2
  • 28
    • 4444274530 scopus 로고    scopus 로고
    • The conserved carboxy terminus of the capsid domain of human immunodeficiency virus type 1 Gag protein is important for virion assembly and release
    • Melamed, D., M. Mark-Danieli, M. Kenan-Eichler, O. Kraus, A. Castiel, N. Laham, T. Pupko, F. Glaser, N. Ben-Tal, and E. Bacharach. 2004. The conserved carboxy terminus of the capsid domain of human immunodeficiency virus type 1 Gag protein is important for virion assembly and release. J. Virol. 78:9675-9688.
    • (2004) J. Virol. , vol.78 , pp. 9675-9688
    • Melamed, D.1    Mark-Danieli, M.2    Kenan-Eichler, M.3    Kraus, O.4    Castiel, A.5    Laham, N.6    Pupko, T.7    Glaser, F.8    Ben-Tal, N.9    Bacharach, E.10
  • 31
    • 0347993084 scopus 로고    scopus 로고
    • Evidence that HIV budding in primary macrophages occurs through the exosome release pathway
    • Nguyen, D. G., A. Booth, S. J. Gould, and J. E. Hildreth. 2003. Evidence that HIV budding in primary macrophages occurs through the exosome release pathway. J. Biol. Chem. 278:52347-52354.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52347-52354
    • Nguyen, D.G.1    Booth, A.2    Gould, S.J.3    Hildreth, J.E.4
  • 32
  • 33
    • 6944255361 scopus 로고    scopus 로고
    • Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
    • Ono, A., S. D. Ablan, S. J. Lockett, K. Nagashima, and E. O. Freed. 2004. Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane. Proc. Natl. Acad. Sci. USA 101:14889-14894.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14889-14894
    • Ono, A.1    Ablan, S.D.2    Lockett, S.J.3    Nagashima, K.4    Freed, E.O.5
  • 34
    • 0034108444 scopus 로고    scopus 로고
    • Relationship between human immunodeficiency virus type 1 Gag multimerization and membrane binding
    • Ono, A., D. Demirov, and E. O. Freed. 2000. Relationship between human immunodeficiency virus type 1 Gag multimerization 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
  • 35
    • 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
  • 36
    • 0347634393 scopus 로고    scopus 로고
    • Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body
    • Ono, A., and E. O. Freed. 2004. Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body. J. Virol. 78:1552-1563.
    • (2004) J. Virol. , vol.78 , pp. 1552-1563
    • Ono, A.1    Freed, E.O.2
  • 37
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in HIV-1 assembly and release
    • Ono, A., and E. O. Freed. 2001. Plasma membrane rafts play a critical role in HIV-1 assembly and release. Proc. Natl. Acad. Sci. USA 98:13925-13930.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13925-13930
    • Ono, A.1    Freed, E.O.2
  • 38
    • 0033999270 scopus 로고    scopus 로고
    • Role of the Gag matrix domain in targeting human immunodeficiency virus type 1 assembly
    • Ono, A., J. M. Orenstein, and E. O. Freed. 2000. Role of the Gag matrix domain in targeting human immunodeficiency virus type 1 assembly. J. Virol. 74:2855-2866.
    • (2000) J. Virol. , vol.74 , pp. 2855-2866
    • Ono, A.1    Orenstein, J.M.2    Freed, E.O.3
  • 39
    • 27644522295 scopus 로고    scopus 로고
    • Association of human immunodeficiency virus type 1 Gag with membrane does not require highly basic sequences in the nucleocapsid: Use of a novel Gag multimerization assay
    • Ono, A., A. A. Waheed, A. Joshi, and E. O. Freed. 2005. Association of human immunodeficiency virus type 1 Gag with membrane does not require highly basic sequences in the nucleocapsid: use of a novel Gag multimerization assay. J. Virol. 79:14131-14140.
    • (2005) J. Virol. , vol.79 , pp. 14131-14140
    • Ono, A.1    Waheed, A.A.2    Joshi, A.3    Freed, E.O.4
  • 40
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • Pelchen-Matthews, A., B. Kramer, and M. Marsh. 2003. Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol. 162:443-455.
    • (2003) J. Cell Biol. , vol.162 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 41
    • 0028296723 scopus 로고
    • Characterization of human immunodeficiency virus type 1 Pr55gag membrane association in a cell-free system: Requirement for a C-terminal domain
    • Platt, E. J., and O. K. Haffar. 1994. Characterization of human immunodeficiency virus type 1 Pr55gag membrane association in a cell-free system: requirement for a C-terminal domain. Proc. Natl. Acad. Sci. USA 91:4594-4598.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4594-4598
    • Platt, E.J.1    Haffar, O.K.2
  • 42
    • 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., K. Wehrly, S. E. Kuhmann, B. Chesebro, and D. Kabat. 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.
    • (1998) J. Virol. , vol.72 , pp. 2855-2864
    • Platt, E.J.1    Wehrly, K.2    Kuhmann, S.E.3    Chesebro, B.4    Kabat, D.5
  • 45
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Swanstrom, R., and J. W. Wills. 1997. Synthesis, assembly, and processing of viral proteins, p. 263-334. In J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 47
    • 0034855639 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells
    • Tang, S., T. Murakami, B. E. Agresta, S. Campbell, E. O. Freed, and J. G. Levin. 2001. Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells. J. Virol. 75:9357-9366.
    • (2001) J. Virol. , vol.75 , pp. 9357-9366
    • Tang, S.1    Murakami, T.2    Agresta, B.E.3    Campbell, S.4    Freed, E.O.5    Levin, J.G.6
  • 49
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • von Schwedler, U. K., K. M. Stray, J. E. Garrus, and W. I. Sundquist. 2003. Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J. Virol. 77:5439-5450.
    • (2003) J. Virol. , vol.77 , pp. 5439-5450
    • Von Schwedler, U.K.1    Stray, K.M.2    Garrus, J.E.3    Sundquist, W.I.4
  • 50
    • 0010296944 scopus 로고
    • Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160
    • Willey, R. L., J. S. Bonifacino, B. J. Potts, M. A. Martin, and R. D. Klausner. 1988. Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160. Proc. Natl. Acad. Sci. USA 85:9580-9584.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9580-9584
    • Willey, R.L.1    Bonifacino, J.S.2    Potts, B.J.3    Martin, M.A.4    Klausner, R.D.5
  • 52
    • 0028705684 scopus 로고
    • Generation of high-liter pseudotyped retroviral vectors with very broad host range
    • Yee, J. K., T. Friedmann, and J. C. Burns. 1994. Generation of high-liter pseudotyped retroviral vectors with very broad host range. Methods Cell Biol. 43(Pt. A):99-112.
    • (1994) Methods Cell Biol. , vol.43 , Issue.PART A , pp. 99-112
    • Yee, J.K.1    Friedmann, T.2    Burns, J.C.3


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