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Volumn 4, Issue 11, 2003, Pages 785-801

Visualization of retroviral replication in living cells reveals budding into multivesicular bodies

Author keywords

Human immunodeficiency virus (HIV); Imaging of viral replication; Multivesicular body (MVB); Murine leukemia virus (MLV); Retroviral budding and assembly

Indexed keywords

CELL PROTEIN; FLUORESCENT DYE; GAG PROTEIN; POLYPROTEIN;

EID: 10744224318     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-0854.2003.00135.x     Document Type: Article
Times cited : (336)

References (61)
  • 1
    • 0035659634 scopus 로고    scopus 로고
    • The HIV-1 assembly machine
    • Gottlinger HG. The HIV-1 assembly machine. Aids 2001;15 (Suppl. 5): S13-S20.
    • (2001) Aids , vol.15 , Issue.SUPPL. 5
    • Gottlinger, H.G.1
  • 2
    • 0001469617 scopus 로고    scopus 로고
    • Retroviridae: The retroviruses and their replication
    • Knipe DM, Howley PM, eds. 4th edn. Philadelphia: PA. Lippincott
    • Goff S. Retroviridae: the retroviruses and their replication. In: Knipe DM, Howley PM, eds. Fields Virology, 4th edn. Philadelphia: PA. Lippincott; 2001. pp 1871-1940.
    • (2001) Fields Virology , pp. 1871-1940
    • Goff, S.1
  • 3
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • Coffin JM, Hughes SH, Varmus HE, eds. Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press
    • Swanstrom R, Wills JW. Synthesis, assembly, and processing of viral proteins. In: Coffin JM, Hughes SH, Varmus HE, eds. Retroviruses. Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press; 1997. pp 263-334.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 4
    • 0031720833 scopus 로고    scopus 로고
    • Molecular events in the assembly of retrovirus particles
    • Sakalian M, Hunter E. Molecular events in the assembly of retrovirus particles. Adv Exp Mad Biol 1998;440:329-339.
    • (1998) Adv. Exp. Mad. Biol. , vol.440 , pp. 329-339
    • Sakalian, M.1    Hunter, E.2
  • 5
    • 0036568729 scopus 로고    scopus 로고
    • Tsg101: HIV-1's ticket to ride
    • Carter CA. Tsg101: HIV-1's ticket to ride. Trends Microbiol 2002;10:203-205.
    • (2002) Trends Microbiol. , vol.10 , pp. 203-205
    • Carter, C.A.1
  • 6
    • 0036239363 scopus 로고    scopus 로고
    • Viral late domains
    • Freed EO. Viral late domains. J Virol 2002;76:4679-4687.
    • (2002) J. Virol. , vol.76 , pp. 4679-4687
    • Freed, E.O.1
  • 7
    • 0034700119 scopus 로고    scopus 로고
    • Ubiquitin in retrovirus assembly: Actor or bystander?
    • Vogt VM. Ubiquitin in retrovirus assembly: actor or bystander? Proc Natl Acad Sci USA 2000;97:12945-12947.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12945-12947
    • Vogt, V.M.1
  • 9
    • 0026317877 scopus 로고
    • Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
    • Gottlinger HG, Dorfman T, Sodroski JG, Haseltine WA. Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release. Proc Natl Acad Sci USA 1991;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
  • 12
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann DJ, Babst M, Emr SD. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 2001;106:145-155.
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 13
    • 0036829172 scopus 로고    scopus 로고
    • Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
    • Pornillos O, Alam SL, Davis DR, Sundquist WI. Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein. Nat Struct Biol 2002;9:812-817.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 812-817
    • Pornillos, O.1    Alam, S.L.2    Davis, D.R.3    Sundquist, W.I.4
  • 14
    • 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 RN, Brown ME, Wang G, Huibregtse J, Hayes FP. 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 2000;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
  • 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, Bouamr F, Vana ML, Xiang Y, Aiyar A, Carter C, Leis J. 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 2001;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
  • 17
    • 0034700146 scopus 로고    scopus 로고
    • Ubiquitin is part of the retrovirus budding machinery
    • Patnaik A, Chau V, Wills JW. Ubiquitin is part of the retrovirus budding machinery. Proc Natl Acad Sci USA 2000;97:13069-13074.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13069-13074
    • Patnaik, A.1    Chau, V.2    Wills, J.W.3
  • 18
    • 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, Zang T, Bieniasz PD. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat Med 2001;7:1313-1319.
    • (2001) Nat. Med. , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 19
    • 0023678515 scopus 로고
    • Cytoplasmic assembly and accumulation of human immunodeficiency virus types 1 and 2 in recombinant human colony-stimulating factor-1-treated human monocytes: An ultrastructural study
    • Orenstein JM, Meltzer MS, Phipps T, Gendelman HE. Cytoplasmic assembly and accumulation of human immunodeficiency virus types 1 and 2 in recombinant human colony-stimulating factor-1-treated human monocytes: an ultrastructural study. J Virol 1988;62:2578-2586.
    • (1988) J. Virol. , vol.62 , pp. 2578-2586
    • Orenstein, J.M.1    Meltzer, M.S.2    Phipps, T.3    Gendelman, H.E.4
  • 21
    • 0035838984 scopus 로고    scopus 로고
    • Dendritic cells: Specialized and regulated antigen processing machines
    • Mallman I, Steinman RM. Dendritic cells: specialized and regulated antigen processing machines. Cell 2001;106:255-258.
    • (2001) Cell , vol.106 , pp. 255-258
    • Mallman, I.1    Steinman, R.M.2
  • 23
    • 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, Resh MD. Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging. J Virol 2000;74:8670-8679.
    • (2000) J. Virol. , vol.74 , pp. 8670-8679
    • Hermida-Matsumoto, L.1    Resh, M.D.2
  • 24
    • 0031949314 scopus 로고    scopus 로고
    • The I domain is required for efficient plasma membrane binding of human immunodeficiency virus type 1 Pr55Gag
    • Sandefur S, Varthakavi V, Spearman P. The I domain is required for efficient plasma membrane binding of human immunodeficiency virus type 1 Pr55Gag. J Virol 1998;72:2723-2732.
    • (1998) J. Virol. , vol.72 , pp. 2723-2732
    • Sandefur, S.1    Varthakavi, V.2    Spearman, P.3
  • 25
    • 0001602245 scopus 로고    scopus 로고
    • Retroviral pathogenesis
    • Coffin JM, Hughes SH, Varmus HE, eds. Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press
    • Rosenberg N, Jolicoeur P. Retroviral pathogenesis. In: Coffin JM, Hughes SH, Varmus HE, eds. Retroviruses. Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press; 1997. pp 475-586.
    • (1997) Retroviruses , pp. 475-586
    • Rosenberg, N.1    Jolicoeur, P.2
  • 26
    • 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, Li X, Goff SP. Mutations altering the Moloney murine leukemia virus p12 Gag protein affect virion production and early events of the virus life cycle, EMBO J 1999;18:4700-4710.
    • (1999) EMBO J. , vol.18 , pp. 4700-4710
    • Yuan, B.1    Li, X.2    Goff, S.P.3
  • 27
    • 0042310339 scopus 로고    scopus 로고
    • Virus assembly
    • Knipe DM, ed. Philadelphia: Lippincot Williams&Wilkins
    • Hunter E. Virus assembly. In: Knipe DM, ed. Fields Virology. Philadelphia: Lippincot Williams&Wilkins; 2001. pp 171-198.
    • (2001) Fields Virology , pp. 171-198
    • Hunter, E.1
  • 28
    • 0033862233 scopus 로고    scopus 로고
    • Mapping and characterization of the N-terminal I domain of human immunodeficiency virus type 1 Pr55 (Gag)
    • Sandefur S, Smith RM, Varthakavi V, Spearman P. Mapping and characterization of the N-terminal I domain of human immunodeficiency virus type 1 Pr55 (Gag). J Virol 2000;74:7238-7249.
    • (2000) J. Virol. , vol.74 , pp. 7238-7249
    • Sandefur, S.1    Smith, R.M.2    Varthakavi, V.3    Spearman, P.4
  • 29
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 gag proteins: Diverse functions in the virus life cycle
    • Freed EO. HIV-1 gag proteins: diverse functions in the virus life cycle. Virology 1998;251:1-15.
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 30
    • 0032493658 scopus 로고    scopus 로고
    • Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes
    • Escola JM, Kleijmeer MJ, Stoorvogel W, Griffith JM, Yoshie O, Geuze HJ. Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes. J Biol Chem 1998;273:20121-20127.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20121-20127
    • Escola, J.M.1    Kleijmeer, M.J.2    Stoorvogel, W.3    Griffith, J.M.4    Yoshie, O.5    Geuze, H.J.6
  • 31
    • 0036150019 scopus 로고    scopus 로고
    • VP40, the matrix protein of Marburg virus, is associated with membranes of the late endosomal compartment
    • Kolesnikova L, Bugany H, Klenk HD, Becker S. VP40, the matrix protein of Marburg virus, is associated with membranes of the late endosomal compartment. J Virol 2002;76:1825-1838.
    • (2002) J. Virol. , vol.76 , pp. 1825-1838
    • Kolesnikova, L.1    Bugany, H.2    Klenk, H.D.3    Becker, S.4
  • 32
    • 0036166924 scopus 로고    scopus 로고
    • A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies
    • Reggiori F, Pelham HR. A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies. Nat Cell Biol 2002;4:117-123.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 117-123
    • Reggiori, F.1    Pelham, H.R.2
  • 33
    • 0027177935 scopus 로고
    • A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects virus particle assembly from the plasma membrane to the endoplasmic reticulum
    • Facke M, Janetzko A, Shoeman RL, Krausslich HG. A large deletion in the matrix domain of the human immunodeficiency virus gag gene redirects virus particle assembly from the plasma membrane to the endoplasmic reticulum. J Virol 1993;67:4972-4980.
    • (1993) J. Virol. , vol.67 , pp. 4972-4980
    • Facke, M.1    Janetzko, A.2    Shoeman, R.L.3    Krausslich, H.G.4
  • 35
    • 0037194733 scopus 로고    scopus 로고
    • Dendritic cell maturation triggers retrograde MHC class II transport from lysosomes to the plasma membrane
    • Chow A, Toomre D, Garrett W, Mellman I. Dendritic cell maturation triggers retrograde MHC class II transport from lysosomes to the plasma membrane. Nature 2002;418:988-994.
    • (2002) Nature , vol.418 , pp. 988-994
    • Chow, A.1    Toomre, D.2    Garrett, W.3    Mellman, I.4
  • 39
    • 0036385503 scopus 로고    scopus 로고
    • HIV-1 Gag polyprotein rescues HLA-DR intracellular transport in a human CD4 (+) cell line
    • Gluschankof P, Suzan M. HIV-1 Gag polyprotein rescues HLA-DR intracellular transport in a human CD4 (+) cell line. Virology 2002; 300:160-169.
    • (2002) Virology , vol.300 , pp. 160-169
    • Gluschankof, P.1    Suzan, M.2
  • 41
    • 0032577581 scopus 로고    scopus 로고
    • Chemokine receptors: Keys to AIDS pathogenesis?
    • Littman DR. Chemokine receptors: keys to AIDS pathogenesis? Cell 1998;93:677-680.
    • (1998) Cell , vol.93 , pp. 677-680
    • Littman, D.R.1
  • 42
    • 0242280995 scopus 로고    scopus 로고
    • Immune response to murine and feline retroviruses
    • Pantaleo G, Walker BD, eds. Totowa: N.J. Humana Press
    • Finke D, Acha-Orbea H. Immune response to murine and feline retroviruses. In: Pantaleo G, Walker BD, eds. Retroviral Immunology. Totowa: N.J. Humana Press, 2001. pp 125-157.
    • (2001) Retroviral Immunology , pp. 125-157
    • Finke, D.1    Acha-Orbea, H.2
  • 45
    • 0036172314 scopus 로고    scopus 로고
    • DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection
    • Kwon DS, Gregorio G, Bitton N, Hendrickson WA, Littman DR. DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection. Immunity 2002;16:135-144.
    • (2002) Immunity , vol.16 , pp. 135-144
    • Kwon, D.S.1    Gregorio, G.2    Bitton, N.3    Hendrickson, W.A.4    Littman, D.R.5
  • 47
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • Pelchen-Matthews A, Kramer B, Marsh M. Infectious HIV-1 assembles in late endosomes in primary macrophages. J Cell Biol 2003;162:443-455.
    • (2003) J. Cell Biol. , vol.162 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 49
    • 0033019820 scopus 로고    scopus 로고
    • The hypervariable domain of the murine leukemia virus surface protein tolerates large insertions and deletions, enabling development of a retroviral particle display system
    • Kayman SC, Park H, Saxon M, Pinter A. The hypervariable domain of the murine leukemia virus surface protein tolerates large insertions and deletions, enabling development of a retroviral particle display system. J Virol 1999;73:1802-1808.
    • (1999) J. Virol. , vol.73 , pp. 1802-1808
    • Kayman, S.C.1    Park, H.2    Saxon, M.3    Pinter, A.4
  • 50
    • 0032875453 scopus 로고    scopus 로고
    • Analysis of receptor usage by ecotropic murine retroviruses, using green fluorescent protein-tagged cationic amino acid transporters
    • Masuda M, Kakushima N, Wilt SG, Ruscetti SK, Hoffman PM, Iwamoto A. Analysis of receptor usage by ecotropic murine retroviruses, using green fluorescent protein-tagged cationic amino acid transporters. J Virol 1999;73:8623-8629.
    • (1999) J. Virol. , vol.73 , pp. 8623-8629
    • Masuda, M.1    Kakushima, N.2    Wilt, S.G.3    Ruscetti, S.K.4    Hoffman, P.M.5    Iwamoto, A.6
  • 52
    • 0037017395 scopus 로고    scopus 로고
    • Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells
    • Barbero P, Bittova L, Pfeffer SR. Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells. J Cell Biol 2002;156:511-518.
    • (2002) J. Cell Biol. , vol.156 , pp. 511-518
    • Barbero, P.1    Bittova, L.2    Pfeffer, S.R.3
  • 53
    • 0034927311 scopus 로고    scopus 로고
    • Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail
    • Blott EJ, Bossi G, Clark R, Zvelebil M, Griffiths GM. Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail. J Cell Sci 2001;114:2405-2416.
    • (2001) J. Cell Sci. , vol.114 , pp. 2405-2416
    • Blott, E.J.1    Bossi, G.2    Clark, R.3    Zvelebil, M.4    Griffiths, G.M.5
  • 55
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • Sonnichsen B, De Renzis S, Nielsen E, Rietdorf J, Zerial M. Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J Cell Biol 2000;149:901-914.
    • (2000) J. Cell Biol. , vol.149 , pp. 901-914
    • Sonnichsen, B.1    De Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 56
    • 0030451424 scopus 로고    scopus 로고
    • TGN38-green fluorescent protein hybrid proteins expressed in stably transfected eukaryotic cells provide a tool for the real-time, in vivo study of membrane traffic pathways and suggest a possible role for ratTGN38
    • Girotti M, Banting G. TGN38-green fluorescent protein hybrid proteins expressed in stably transfected eukaryotic cells provide a tool for the real-time, in vivo study of membrane traffic pathways and suggest a possible role for ratTGN38. J Cell Sci 1996;109:2915-2926.
    • (1996) J. Cell Sci. , vol.109 , pp. 2915-2926
    • Girotti, M.1    Banting, G.2
  • 57
    • 0035038392 scopus 로고    scopus 로고
    • Adaptation of chimeric retroviruses in vitro and in vivo: Isolation of avian retroviral vectors with extended host range
    • Barsov EV, Payne WS, Hughes SH. Adaptation of chimeric retroviruses in vitro and in vivo: isolation of avian retroviral vectors with extended host range. J Virol 2001;75:4973-4983.
    • (2001) J. Virol. , vol.75 , pp. 4973-4983
    • Barsov, E.V.1    Payne, W.S.2    Hughes, S.H.3
  • 58
    • 0037302292 scopus 로고    scopus 로고
    • Phosphorylated serine residues and an arginine-rich domain of the Moloney murine leukemia virus p12 protein are required for early events of viral infection
    • Yueh A, Goff SP. Phosphorylated serine residues and an arginine-rich domain of the Moloney murine leukemia virus p12 protein are required for early events of viral infection. J Virol 2003;77:1820-1829.
    • (2003) J. Virol. , vol.77 , pp. 1820-1829
    • Yueh, A.1    Goff, S.P.2
  • 59
    • 0035809211 scopus 로고    scopus 로고
    • Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells
    • Folsch H, Pypaert M, Schu P, Mellman I. Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells. J Cell Biol 2001;152:595-606.
    • (2001) J. Cell Biol. , vol.152 , pp. 595-606
    • Folsch, H.1    Pypaert, M.2    Schu, P.3    Mellman, I.4
  • 60
    • 0037956030 scopus 로고    scopus 로고
    • Biochemical sub-fractionation of the mammalian Golgi apparatus
    • Taguchi T, Pypaert M, Warren G. Biochemical sub-fractionation of the mammalian Golgi apparatus. Traffic 2003;4:344-352.
    • (2003) Traffic , vol.4 , pp. 344-352
    • Taguchi, T.1    Pypaert, M.2    Warren, G.3
  • 61
    • 0037309056 scopus 로고    scopus 로고
    • The proline-rich region of the ecotropic Moloney murine leukaemia virus envelope protein tolerates the insertion of the green fluorescent protein and allows the generation of replication-competent virus
    • Erlwein O, Buchholz CJ, Schnierle BS. The proline-rich region of the ecotropic Moloney murine leukaemia virus envelope protein tolerates the insertion of the green fluorescent protein and allows the generation of replication-competent virus. J Gen Virol 2003;84:369-373.
    • (2003) J. Gen. Virol. , vol.84 , pp. 369-373
    • Erlwein, O.1    Buchholz, C.J.2    Schnierle, B.S.3


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