메뉴 건너뛰기




Volumn 82, Issue 19, 2008, Pages 9770-9775

Basal budding and replication of the murine leukemia virus are independent of the Gag L domains

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; MUTANT PROTEIN;

EID: 52649111176     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00741-08     Document Type: Article
Times cited : (6)

References (35)
  • 1
    • 0034003832 scopus 로고    scopus 로고
    • Deletion of a short, untranslated region adjacent to the polypurine tract in Moloney murine leukemia virus leads to formation of aberrant 5′ plus-strand DNA ends in vivo
    • Bacharach, E., J. Gonsky, D. Lim, and S. P. Goff. 2000. Deletion of a short, untranslated region adjacent to the polypurine tract in Moloney murine leukemia virus leads to formation of aberrant 5′ plus-strand DNA ends in vivo. J. Virol. 74:4755-4764.
    • (2000) J. Virol , vol.74 , pp. 4755-4764
    • Bacharach, E.1    Gonsky, J.2    Lim, D.3    Goff, S.P.4
  • 2
    • 0033959713 scopus 로고    scopus 로고
    • ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking
    • Bishop, N., and P. Woodman. 2000. ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking. Mol. Biol. Cell 11:227-239.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 227-239
    • Bishop, N.1    Woodman, P.2
  • 3
    • 0242331750 scopus 로고    scopus 로고
    • Bouamr, F., J. A. Melillo, M. Q. Wang, K. Nagashima, M. de Los Santos, A. Rein, and S. P. Goff. 2003. PPPYVEPTAP motif is the late domain of human T-cell leukemia virus type 1 Gag and mediates its functional interaction with cellular proteins Nedd4 and Tsg101. J. Virol. 77:11882-11895. (Erratum, 78:4383, 2004.)
    • Bouamr, F., J. A. Melillo, M. Q. Wang, K. Nagashima, M. de Los Santos, A. Rein, and S. P. Goff. 2003. PPPYVEPTAP motif is the late domain of human T-cell leukemia virus type 1 Gag and mediates its functional interaction with cellular proteins Nedd4 and Tsg101. J. Virol. 77:11882-11895. (Erratum, 78:4383, 2004.)
  • 4
    • 34347385894 scopus 로고    scopus 로고
    • Parallels between cytokinesis and retroviral budding: A role for the ESCRT machinery
    • Carlton, J. G., and J. Martin-Serrano. 2007. Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery. Science 316:1908-1912.
    • (2007) Science , vol.316 , pp. 1908-1912
    • Carlton, J.G.1    Martin-Serrano, J.2
  • 5
    • 39549095341 scopus 로고    scopus 로고
    • Mechanisms for enveloped virus budding: Can some viruses do without an ESCRT?
    • Chen, B. J., and R. A. Lamb. 2008. Mechanisms for enveloped virus budding: can some viruses do without an ESCRT? Virology 372:221-232.
    • (2008) Virology , vol.372 , pp. 221-232
    • Chen, B.J.1    Lamb, R.A.2
  • 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. 199:47-59.
    • (1988) J. Mol. Biol , vol.199 , pp. 47-59
    • Colicelli, J.1    Goff, S.P.2
  • 7
    • 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
  • 8
    • 36248936657 scopus 로고    scopus 로고
    • Beyond Tsg101: The role of Alix in 'ESCRTing' HIV-1
    • Fujii, K., J. H. Hurley, and E. O. Freed. 2007. Beyond Tsg101: the role of Alix in 'ESCRTing' HIV-1. Nat. Rev. Microbiol. 5:912-916.
    • (2007) Nat. Rev. Microbiol , vol.5 , pp. 912-916
    • Fujii, K.1    Hurley, J.H.2    Freed, E.O.3
  • 10
    • 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
  • 11
    • 0042389562 scopus 로고    scopus 로고
    • The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to virus release
    • Gottwein, E., J. Bodem, B. Muller, A. Schmechel, H. Zentgraf, and H. G. Krausslich. 2003. The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to virus release. J. Virol. 77:9474-9485.
    • (2003) J. Virol , vol.77 , pp. 9474-9485
    • Gottwein, E.1    Bodem, J.2    Muller, B.3    Schmechel, A.4    Zentgraf, H.5    Krausslich, H.G.6
  • 12
    • 0034610295 scopus 로고    scopus 로고
    • A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: Implications for filovirus budding
    • Harty, R. N., M. E. Brown, G. Wang, J. Huibregtse, and F. P. Hayes. 2000. A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: implications for filovirus budding. Proc. Natl. Acad. Sci. USA 97:13871-13876.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13871-13876
    • Harty, R.N.1    Brown, M.E.2    Wang, G.3    Huibregtse, J.4    Hayes, F.P.5
  • 13
    • 0033050750 scopus 로고    scopus 로고
    • A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: Implications for viral budding
    • Harty, R. N., J. Paragas, M. Sudol, and P. Palese. 1999. A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: implications for viral budding. J. Virol. 73:2921-2929.
    • (1999) J. Virol , vol.73 , pp. 2921-2929
    • Harty, R.N.1    Paragas, J.2    Sudol, M.3    Palese, P.4
  • 14
    • 0028971135 scopus 로고
    • p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. 1
    • 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. 1. Virol. 69:6810-6818.
    • (1995) Virol , vol.69 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 15
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: Structure and mechanism of a membrane-trafficking network
    • Hurley, J. H., and S. D. Emr. 2006. The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu. Rev. Biophys. Biomol. Struct. 35:277-298.
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 16
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann, D. J., G. Odorizzi, and S. D. Emr. 2002. Receptor downregulation and multivesicular-body sorting. Nat. Rev. Mol. Cell Biol. 3:893-905.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 17
    • 0035949489 scopus 로고    scopus 로고
    • Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells
    • Kikonyogo, A., F. Bouamr, M. L. Vana, Y. Xiang, A. Aiyar, C. Carter, and J. Leis. 2001. Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells. Proc. Natl. Acad. Sci. USA 98:11199-11204.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11199-11204
    • Kikonyogo, A.1    Bouamr, F.2    Vana, M.L.3    Xiang, Y.4    Aiyar, A.5    Carter, C.6    Leis, J.7
  • 18
    • 0036776607 scopus 로고    scopus 로고
    • The PPPY motif of human T-cell leukemia virus type 1 Gag protein is required early in the budding process
    • Le Blanc, I., M. C. Prevost, M. C. Dokhelar, and A. R. Rosenberg. 2002. The PPPY motif of human T-cell leukemia virus type 1 Gag protein is required early in the budding process. J. Virol. 76:10024-10029.
    • (2002) J. Virol , vol.76 , pp. 10024-10029
    • Le Blanc, I.1    Prevost, M.C.2    Dokhelar, M.C.3    Rosenberg, A.R.4
  • 19
    • 43249108765 scopus 로고    scopus 로고
    • Functional hierarchy of two L domains in porcine endogenous retrovirus (PERV) that influence release and infectivity
    • Marcucci, K. T., Y. Martina, F. Harrison, C. A. Wilson, and D. R. Salomon. 2008. Functional hierarchy of two L domains in porcine endogenous retrovirus (PERV) that influence release and infectivity. Virology 375:637-645.
    • (2008) Virology , vol.375 , pp. 637-645
    • Marcucci, K.T.1    Martina, Y.2    Harrison, F.3    Wilson, C.A.4    Salomon, D.R.5
  • 20
    • 19944384581 scopus 로고    scopus 로고
    • Single point mutations in the zinc finger motifs of the human immunodeficiency virus type 1 nucleocapsid alter RNA binding specificities of the gag protein and enhance packaging and infectivity
    • Mark-Danieli, M., N. Laham, M. Kenan-Eichler, A. Castiel, D. Melamed, M. Landau, N. M. Bouvier, M. J. Evans, and E. Bacharach. 2005. Single point mutations in the zinc finger motifs of the human immunodeficiency virus type 1 nucleocapsid alter RNA binding specificities of the gag protein and enhance packaging and infectivity. J. Virol. 79:7756-7767.
    • (2005) J. Virol , vol.79 , pp. 7756-7767
    • Mark-Danieli, M.1    Laham, N.2    Kenan-Eichler, M.3    Castiel, A.4    Melamed, D.5    Landau, M.6    Bouvier, N.M.7    Evans, M.J.8    Bacharach, E.9
  • 21
    • 0142123069 scopus 로고    scopus 로고
    • Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins
    • Martin-Serrano, J., A. Yarovoy, D. Perez-Caballero, and P. D. Bieniasz. 2003. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc. Natl. Acad. Sci. USA 100:12414-12419.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12414-12419
    • Martin-Serrano, J.1    Yarovoy, A.2    Perez-Caballero, D.3    Bieniasz, P.D.4
  • 22
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano, J., T. Zang, and P. D. Bieniasz. 2001. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat. Med. 7:1313-1319.
    • (2001) Nat. Med , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 24
    • 37749018903 scopus 로고    scopus 로고
    • Biogenesis and function of multivesicular bodies
    • Piper, R. C., and D. J. Katzmann. 2007. Biogenesis and function of multivesicular bodies. Annu. Rev. Cell Dev. Biol. 23:519-547.
    • (2007) Annu. Rev. Cell Dev. Biol , vol.23 , pp. 519-547
    • Piper, R.C.1    Katzmann, D.J.2
  • 26
    • 0030858622 scopus 로고    scopus 로고
    • Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein
    • Puffer, B. A., L. J. Parent, J. W. Wills, and R. C. Montelaro. 1997. Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein. J. Virol. 71:6541-6546.
    • (1997) J. Virol , vol.71 , pp. 6541-6546
    • Puffer, B.A.1    Parent, L.J.2    Wills, J.W.3    Montelaro, R.C.4
  • 27
    • 22844435415 scopus 로고    scopus 로고
    • Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding
    • Segura-Morales, C., C. Pescia, C. Chatellard-Causse, R. Sadoul, E. Bertrand, and E. Basyuk. 2005. Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding. J. Biol. Chem. 280:27004-27012.
    • (2005) J. Biol. Chem , vol.280 , pp. 27004-27012
    • Segura-Morales, C.1    Pescia, C.2    Chatellard-Causse, C.3    Sadoul, R.4    Bertrand, E.5    Basyuk, E.6
  • 28
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack, B., A. Calistri, S. Craig, E. Popova, and H. G. Gottlinger. 2003. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114:689-699.
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 29
    • 37049034076 scopus 로고    scopus 로고
    • Ubiquitin depletion and dominant-negative VPS4 inhibit rhabdovirus budding without affecting alphavirus budding
    • Taylor, G. M., P. I. Hanson, and M. Kielian. 2007. Ubiquitin depletion and dominant-negative VPS4 inhibit rhabdovirus budding without affecting alphavirus budding. J. Virol. 81:13631-13639.
    • (2007) J. Virol , vol.81 , pp. 13631-13639
    • Taylor, G.M.1    Hanson, P.I.2    Kielian, M.3
  • 30
    • 0028844265 scopus 로고
    • Assays for retroviral reverse transcriptase
    • Telesnitsky, A., S. Blain, and S. P. Goff. 1995. Assays for retroviral reverse transcriptase. Methods Enzymol. 262:347-362.
    • (1995) Methods Enzymol , vol.262 , pp. 347-362
    • Telesnitsky, A.1    Blain, S.2    Goff, S.P.3
  • 32
    • 0028070639 scopus 로고
    • An assembly domain of the Rous sarcoma virus Gag protein required late in budding
    • Wills, J. W., C. E. Cameron, C. B. Wilson, Y. Xiang, R. P. Bennett, and J. Leis. 1994. An assembly domain of the Rous sarcoma virus Gag protein required late in budding. J. Virol. 68:6605-6618.
    • (1994) J. Virol , vol.68 , pp. 6605-6618
    • Wills, J.W.1    Cameron, C.E.2    Wilson, C.B.3    Xiang, Y.4    Bennett, R.P.5    Leis, J.6
  • 33
    • 0031968983 scopus 로고    scopus 로고
    • A proline-rich motif (PPPY) in the Gag polyprotein of Mason-Pfizer monkey virus plays a maturation-independent role in virion release
    • Yasuda, J., and E. Hunter. 1998. A proline-rich motif (PPPY) in the Gag polyprotein of Mason-Pfizer monkey virus plays a maturation-independent role in virion release. J. Virol. 72:4095-4103.
    • (1998) J. Virol , vol.72 , pp. 4095-4103
    • Yasuda, J.1    Hunter, E.2
  • 34
    • 0029582762 scopus 로고
    • Role of the C terminus Gag protein in human immunodeficiency virus type 1 virion assembly and maturation
    • Yu, X. F., Z. Matsuda, Q. C. Yu, T. H. Lee, and M. Essex. 1995. Role of the C terminus Gag protein in human immunodeficiency virus type 1 virion assembly and maturation. J. Gen. Virol. 76:3171-3179.
    • (1995) J. Gen. Virol , vol.76 , pp. 3171-3179
    • Yu, X.F.1    Matsuda, Z.2    Yu, Q.C.3    Lee, T.H.4    Essex, M.5
  • 35
    • 0344035661 scopus 로고    scopus 로고
    • Mutations altering the moloney murine leukemia virus p12 Gag protein affect virion production and early events of the virus life cycle
    • Yuan, B., X. Li, and S. P. Goff. 1999. Mutations altering the moloney murine leukemia virus p12 Gag protein affect virion production and early events of the virus life cycle. EMBO J. 18:4700-4710.
    • (1999) EMBO J , vol.18 , pp. 4700-4710
    • Yuan, B.1    Li, X.2    Goff, S.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.