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Volumn 78, Issue 3, 2004, Pages 1503-1512

Both the PPPY and PTAP Motifs Are Involved in Human T-Cell Leukemia Virus Type 1 Particle Release

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; MUTANT PROTEIN; VIRUS PROTEIN;

EID: 0347634395     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.3.1503-1512.2004     Document Type: Article
Times cited : (49)

References (50)
  • 1
    • 0034157875 scopus 로고    scopus 로고
    • Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
    • Babst, M., G. Odorizzi, E. J. Estepa, and S. D. Emr. 2000. Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking. Traffic 1:248-258.
    • (2000) Traffic , vol.1 , pp. 248-258
    • Babst, M.1    Odorizzi, G.2    Estepa, E.J.3    Emr, S.D.4
  • 2
    • 0034529206 scopus 로고    scopus 로고
    • Differential budding efficiencies of human T-cell leukemia virus type (HTLV-1) Gag and Gag-Pro polyproteins from insect and mammalian cells
    • Bouamr, F., L. Garnier, F. Rayne, A. Verna, N. Rebeyrotte, M. Cerutti, and R. Z. Mamoun. 2000. Differential budding efficiencies of human T-cell leukemia virus type (HTLV-1) Gag and Gag-Pro polyproteins from insect and mammalian cells. Virology 278:597-609.
    • (2000) Virology , vol.278 , pp. 597-609
    • Bouamr, F.1    Garnier, L.2    Rayne, F.3    Verna, A.4    Rebeyrotte, N.5    Cerutti, M.6    Mamoun, R.Z.7
  • 3
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant, M., and L. Ratner. 1990. Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. Proc. Natl. Acad. Sci. USA 87:523-527.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 4
    • 0028556951 scopus 로고
    • Detection of human T-cell leukemia virus 1 permissive cells using cell lines producing selectable recombinant virions
    • Copeland, K. F. T., A. G. M. Haaksma, D. Derse, and J. L. Heeney. 1994. Detection of human T-cell leukemia virus 1 permissive cells using cell lines producing selectable recombinant virions. J. Virol. Methods 50:219-226.
    • (1994) J. Virol. Methods , vol.50 , pp. 219-226
    • Copeland, K.F.T.1    Haaksma, A.G.M.2    Derse, D.3    Heeney, J.L.4
  • 5
    • 0033050343 scopus 로고    scopus 로고
    • Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras
    • Craven, R. C., R. N. Harty, J. Paragas, P. Palese, and J. W. Wills. 1999. Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras. J. Virol. 73:3359-3365.
    • (1999) J. Virol. , vol.73 , pp. 3359-3365
    • Craven, R.C.1    Harty, R.N.2    Paragas, J.3    Palese, P.4    Wills, J.W.5
  • 6
    • 0037154214 scopus 로고    scopus 로고
    • Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function
    • Demirov, D. G., A. Ono, J. M. Orenstein, and E. O. Freed. 2002. Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function. Proc. Natl. Acad. Sci. USA 99:955-960.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 955-960
    • Demirov, D.G.1    Ono, A.2    Orenstein, J.M.3    Freed, E.O.4
  • 7
    • 0036239363 scopus 로고    scopus 로고
    • Viral late domains
    • Freed, E. O. 2002. Viral late domains. J. Virol. 76:4679-4087.
    • (2002) J. Virol. , vol.76 , pp. 4679-4087
    • Freed, E.O.1
  • 9
    • 0026317877 scopus 로고
    • Effect of mutations affecting the p6gag 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 p6gag 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
  • 10
    • 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
    • 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
  • 13
    • 0002168907 scopus 로고
    • Macromolecular interactions in the assembly of HIV and other retroviruses
    • Hunter, E. 1994. Macromolecular interactions in the assembly of HIV and other retroviruses. Semin. Virol. 5:71-83.
    • (1994) Semin. Virol. , vol.5 , pp. 71-83
    • Hunter, E.1
  • 14
    • 0033590187 scopus 로고    scopus 로고
    • Bovine leukemia virus Gag particle assembly in insect cells: Formation of chimeric particles by domain-switched leukemia/lentivirus Gag polyprotein
    • Kakker, N. K., M. V. Mikhailov, M. V. Nermut, A. Burny, and P. Roy. 1999. Bovine leukemia virus Gag particle assembly in insect cells: formation of chimeric particles by domain-switched leukemia/lentivirus Gag polyprotein. Virology 265:308-318.
    • (1999) Virology , vol.265 , pp. 308-318
    • Kakker, N.K.1    Mikhailov, M.V.2    Nermut, M.V.3    Burny, A.4    Roy, P.5
  • 15
    • 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
  • 16
    • 0036138043 scopus 로고    scopus 로고
    • Intracellular distribution of human T-cell leukemia virus type 1 Gag proteins is independent of interaction with intracellular membranes
    • Le Blanc, I., V. Blot, I. Bouchaert, J. Salamero, B. Goud, A. R. Rosenberg, and M. C. Dokhelar. 2002. Intracellular distribution of human T-cell leukemia virus type 1 Gag proteins is independent of interaction with intracellular membranes. J. Virol. 76:905-911.
    • (2002) J. Virol. , vol.76 , pp. 905-911
    • Le Blanc, I.1    Blot, V.2    Bouchaert, I.3    Salamero, J.4    Goud, B.5    Rosenberg, A.R.6    Dokhelar, M.C.7
  • 17
    • 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
  • 18
    • 0033019287 scopus 로고    scopus 로고
    • Multiple functions for the basic amino acids of the human T-cell leukemia virus type 1 matrix protein in viral transmission
    • Le Blanc, I., A. R. Rosenberg, and M. C. Dokhelar. 1999. Multiple functions for the basic amino acids of the human T-cell leukemia virus type 1 matrix protein in viral transmission. J. Virol. 73:1860-1867.
    • (1999) J. Virol. , vol.73 , pp. 1860-1867
    • Le Blanc, I.1    Rosenberg, A.R.2    Dokhelar, M.C.3
  • 19
    • 0033939453 scopus 로고    scopus 로고
    • Sorting in the endosomal system in yeast and animal cells
    • Lemmon, S. K., and L. M. Traub. 2000. Sorting in the endosomal system in yeast and animal cells. Curr. Opin. Cell Biol. 12:457-466.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 457-466
    • Lemmon, S.K.1    Traub, L.M.2
  • 20
    • 0036148338 scopus 로고    scopus 로고
    • Functional replacement and positional dependence of homologous and heterologous L domains in equine infectious anemia virus replication
    • Li, F., C. Chen, B. A. Puffer, and R. C. Montelaro. 2002. Functional replacement and positional dependence of homologous and heterologous L domains in equine infectious anemia virus replication. J. Virol. 76:1569-1577.
    • (2002) J. Virol. , vol.76 , pp. 1569-1577
    • Li, F.1    Chen, C.2    Puffer, B.A.3    Montelaro, R.C.4
  • 21
    • 0037303193 scopus 로고    scopus 로고
    • Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: Involvement of host proteins TSG101 and VPS-4
    • Licata, J. M., M. Simpson-Holley, N. T. Wright, Z. Han, J. Paragas, and R. N. Harty. 2003. Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4. J. Virol. 77:1812-1819.
    • (2003) J. Virol. , vol.77 , pp. 1812-1819
    • Licata, J.M.1    Simpson-Holley, M.2    Wright, N.T.3    Han, Z.4    Paragas, J.5    Harty, R.N.6
  • 22
    • 0036400001 scopus 로고    scopus 로고
    • The primary nucleotide sequence of the bovine leukemia virus RNA packaging signal can influence efficient RNA packaging and virus replication
    • Mansky, L. M., and L. C. Gajary. 2002. The primary nucleotide sequence of the bovine leukemia virus RNA packaging signal can influence efficient RNA packaging and virus replication. Virology 301:272-280.
    • (2002) Virology , vol.301 , pp. 272-280
    • Mansky, L.M.1    Gajary, L.C.2
  • 23
    • 0029040494 scopus 로고
    • The bovine leukemia virus encapsidation signal is discontinuous and extends into the 5′ end of the gag gene
    • Mansky, L. M., A. E. Krueger, and H. M. Temin. 1995. The bovine leukemia virus encapsidation signal is discontinuous and extends into the 5′ end of the gag gene. J. Virol. 69:3282-3289.
    • (1995) J. Virol. , vol.69 , pp. 3282-3289
    • Mansky, L.M.1    Krueger, A.E.2    Temin, H.M.3
  • 24
    • 0031901639 scopus 로고    scopus 로고
    • The bovine leukemia virus encapsidation signal is composed of RNA secondary structures
    • Mansky, L. M., and R. M. Wisniewski. 1998. The bovine leukemia virus encapsidation signal is composed of RNA secondary structures. J. Virol. 72:3196-3204.
    • (1998) J. Virol. , vol.72 , pp. 3196-3204
    • Mansky, L.M.1    Wisniewski, R.M.2
  • 25
    • 0037383128 scopus 로고    scopus 로고
    • Role of ESCRT-1 in retroviral budding
    • Martin-Serrano, J., T. Zang, and P. D. Bieniasz. 2003. Role of ESCRT-1 in retroviral budding. J. Virol. 77:4794-4804.
    • (2003) J. Virol. , vol.77 , pp. 4794-4804
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 26
    • 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
  • 28
    • 0037334391 scopus 로고    scopus 로고
    • Retroviruses have differing requirements for proteasome function in the budding process
    • Ott, D. E., L. V. Coren, R. C. Sowder, J. Adams, and U. Schubert. 2003. Retroviruses have differing requirements for proteasome function in the budding process. J. Virol. 77:3384-3393.
    • (2003) J. Virol. , vol.77 , pp. 3384-3393
    • Ott, D.E.1    Coren, L.V.2    Sowder, R.C.3    Adams, J.4    Schubert, U.5
  • 30
    • 0036184661 scopus 로고    scopus 로고
    • Budding of equine infectious anemia virus is insensitive to proteasome inhibitors
    • Patnaik, A., V. Chau, F. Li, R. C. Montelaro, and J. W. Wills. 2002. Budding of equine infectious anemia virus is insensitive to proteasome inhibitors. J. Virol. 76:2641-2647.
    • (2002) J. Virol. , vol.76 , pp. 2641-2647
    • Patnaik, A.1    Chau, V.2    Li, F.3    Montelaro, R.C.4    Wills, J.W.5
  • 31
    • 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
  • 32
    • 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
  • 33
    • 0031797730 scopus 로고    scopus 로고
    • Equine infectious anemia virus Gag polyprotein late domain specifically recruits cellular AP-2 adapter protein complexes during virion assembly
    • Puffer, B. A., S. C. Watkins, and R. C. Montelaro. 1998. Equine infectious anemia virus Gag polyprotein late domain specifically recruits cellular AP-2 adapter protein complexes during virion assembly. J. Virol. 72:10218-10221.
    • (1998) J. Virol. , vol.72 , pp. 10218-10221
    • Puffer, B.A.1    Watkins, S.C.2    Montelaro, R.C.3
  • 34
    • 0025351117 scopus 로고
    • Ubiquitin in avian leukosis virus particles
    • Putterman, D., R. B. Pepinsky, and V. M. Vogt. 1990. Ubiquitin in avian leukosis virus particles. Virology 176:633-637.
    • (1990) Virology , vol.176 , pp. 633-637
    • Putterman, D.1    Pepinsky, R.B.2    Vogt, V.M.3
  • 36
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class E vps mutants
    • Raymond, C. K., I. Howald-Stevenson, C. A. Vater, and T. H. Stevens. 1992. Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants. Mol. Biol. Cell 3:1389-1402.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1389-1402
    • Raymond, C.K.1    Howald-Stevenson, I.2    Vater, C.A.3    Stevens, T.H.4
  • 37
    • 0022794486 scopus 로고
    • Myristylation site in Pr65gag is essential for virus particle formation by Moloney murine leukemia virus
    • Rein, A., M. R. McClure, N. R. Rice, R. B. Luftig, and A. M. Schultz. 1986. Myristylation site in Pr65gag is essential for virus particle formation by Moloney murine leukemia virus. Proc. Natl. Acad. Sci. USA 83:7246-7250.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7246-7250
    • Rein, A.1    McClure, M.R.2    Rice, N.R.3    Luftig, R.B.4    Schultz, A.M.5
  • 40
    • 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, Plainview, 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, Plainview, N.Y.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 42
    • 0034700119 scopus 로고    scopus 로고
    • Ubiquitin in retrovirus assembly: Actor or bystander?
    • Vogt, V. M. 2000. Ubiquitin in retrovirus assembly: actor or bystander? Proc. Natl. Acad. Sci. USA 97:12945-12947.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12945-12947
    • Vogt, V.M.1
  • 43
    • 0036315329 scopus 로고    scopus 로고
    • Analysis of bovine leukemia virus Gag membrane targeting and late domain function
    • Wang, H., K. M. Norris, and L. M. Mansky. 2002. Analysis of bovine leukemia virus Gag membrane targeting and late domain function. J. Virol. 76:8485-8493.
    • (2002) J. Virol. , vol.76 , pp. 8485-8493
    • Wang, H.1    Norris, K.M.2    Mansky, L.M.3
  • 44
    • 0027328715 scopus 로고
    • Characterization of a small (25-kilodalton) derivative of the Rous sarcoma virus Gag protein competent for particle release
    • Weldon, R. A., 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.1    Wills, J.W.2
  • 45
    • 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
  • 46
    • 0025728301 scopus 로고
    • Form, function, and use of retroviral gag proteins
    • Wills, J. W., and R. 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.2
  • 47
    • 0029978648 scopus 로고    scopus 로고
    • Fine mapping and characterization of the Rous sarcoma virus Pr76gag late assembly domain
    • Xiang, Y., C. E. Cameron, J. W. Wills, and J. Leis. 1996. Fine mapping and characterization of the Rous sarcoma virus Pr76gag late assembly domain. J. Virol. 70:5695-5700.
    • (1996) J. Virol. , vol.70 , pp. 5695-5700
    • Xiang, Y.1    Cameron, C.E.2    Wills, J.W.3    Leis, J.4
  • 48
    • 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
  • 49
    • 0033854158 scopus 로고    scopus 로고
    • Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses
    • Yuan, B., S. Campbell, E. Bacharach, A. Rein, and S. P. Goff, 2000. Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses. J. Virol. 74:7250-7260.
    • (2000) J. Virol. , vol.74 , pp. 7250-7260
    • Yuan, B.1    Campbell, S.2    Bacharach, E.3    Rein, A.4    Goff, S.P.5
  • 50
    • 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


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