메뉴 건너뛰기




Volumn 4, Issue 12, 2003, Pages 902-910

HIV-1 egress is gated through late endosomal membranes

Author keywords

Human immunodeficiency virus type 1 (HIV 1); Late endosome; Multivesicular body (MVB); Retroviral assembly and release

Indexed keywords

GAG PROTEIN; STRUCTURAL PROTEIN;

EID: 0346937486     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1600-0854.2003.00145.x     Document Type: Article
Times cited : (155)

References (55)
  • 1
    • 0036437319 scopus 로고    scopus 로고
    • Break ins and break outs: Viral interactions with the cytoskeleton of mammalian cells
    • Smith GA, Enquist LW. Break ins and break outs: viral interactions with the cytoskeleton of mammalian cells. Annu Rev Cell Dev Biol 2002;18:135-161.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 135-161
    • Smith, G.A.1    Enquist, L.W.2
  • 2
    • 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
  • 4
    • 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
  • 5
    • 0035490884 scopus 로고    scopus 로고
    • The endocytic pathway. a mosaic of domains
    • Gruenberg J. The endocytic pathway. a mosaic of domains. Nat Rev Mol Cell Biol 2001;2:721-730.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 721-730
    • Gruenberg, J.1
  • 11
    • 0001118596 scopus 로고    scopus 로고
    • Wills 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 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
  • 12
    • 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
  • 13
    • 0033102128 scopus 로고    scopus 로고
    • Tagging the human immunodeficiency virus gag protein with green fluorescent protein. Minimal evidence for colocalisation with actin
    • Perrin-Tricaud C, Davoust J, Jones IM. Tagging the human immunodeficiency virus gag protein with green fluorescent protein. Minimal evidence for colocalisation with actin. Virology 1999;255:20-25.
    • (1999) Virology , vol.255 , pp. 20-25
    • Perrin-Tricaud, C.1    Davoust, J.2    Jones, I.M.3
  • 14
    • 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
  • 17
    • 0033981633 scopus 로고    scopus 로고
    • Rab GTPases coordinate endocytosis
    • Somsel Rodman J, Wandinger-Ness A. Rab GTPases coordinate endocytosis. J Cell Sci 2000;113 Part 2:183-192.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 2 , pp. 183-192
    • Somsel Rodman, J.1    Wandinger-Ness, A.2
  • 19
    • 0035865135 scopus 로고    scopus 로고
    • Rab-interacting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes
    • Cantalupo G, Alifano P, Roberti V, Bruni CB, Bucci C. Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. EMBO J 2001;20:683-693.
    • (2001) EMBO J. , vol.20 , pp. 683-693
    • Cantalupo, G.1    Alifano, P.2    Roberti, V.3    Bruni, C.B.4    Bucci, C.5
  • 21
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
    • Kobayashi T, Stang E, Fang KS, de Moerloose P, Parton RG, Gruenberg J. A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature 1998;392:193-197.
    • (1998) Nature , vol.392 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    Fang, K.S.3    de Moerloose, P.4    Parton, R.G.5    Gruenberg, J.6
  • 22
    • 0035958557 scopus 로고    scopus 로고
    • Plasma membrane repair is mediated by Ca (2+) -regulated exocytosis of lysosomes
    • Reddy A, Caler EV, Andrews NW. Plasma membrane repair is mediated by Ca (2+) -regulated exocytosis of lysosomes. Cell 2001;106:157-169.
    • (2001) Cell , vol.106 , pp. 157-169
    • Reddy, A.1    Caler, E.V.2    Andrews, N.W.3
  • 23
    • 0038316341 scopus 로고    scopus 로고
    • ER-mediated phagocytosis: A new membrane for new functions
    • Desjardins M. ER-mediated phagocytosis: a new membrane for new functions. Nat Rev Immunol 2003;3:280-291.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 280-291
    • Desjardins, M.1
  • 24
    • 0034232503 scopus 로고    scopus 로고
    • Endocytosis in viral replication
    • Marsh M, Pelchen-Matthews A. Endocytosis in viral replication. Traffic 2000;1:525-532.
    • (2000) Traffic , vol.1 , pp. 525-532
    • Marsh, M.1    Pelchen-Matthews, A.2
  • 25
    • 0037062441 scopus 로고    scopus 로고
    • Cell surface expression of the HIV-1 envelope glycoproteins is directed from intra-cellular CTLA-4-containing regulated secretory granules
    • Miranda LR, Schaefer BC, Kupfer A, Hu Z, Franzusoff A. Cell surface expression of the HIV-1 envelope glycoproteins is directed from intra-cellular CTLA-4-containing regulated secretory granules. Proc Natl Acad Sci USA 2002;99:8031-8036.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8031-8036
    • Miranda, L.R.1    Schaefer, B.C.2    Kupfer, A.3    Hu, Z.4    Franzusoff, A.5
  • 26
    • 0038618759 scopus 로고    scopus 로고
    • Targeting of the human immunodeficiency virus type 1 envelope to the trans-Golgi network through binding to TIP47 is required for env incorporation into virions and infectivity
    • Blot G, Janvier K, Le Panse S, Benarous R, Berlioz-Torrent C. Targeting of the human immunodeficiency virus type 1 envelope to the trans-Golgi network through binding to TIP47 is required for env incorporation into virions and infectivity. J Virol 2003;77:6931-6945.
    • (2003) J. Virol. , vol.77 , pp. 6931-6945
    • Blot, G.1    Janvier, K.2    Le Panse, S.3    Benarous, R.4    Berlioz-Torrent, C.5
  • 31
    • 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
  • 32
    • 0037154214 scopus 로고    scopus 로고
    • Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function
    • Demirov DG, Ono A, Orenstein JM, Freed EO. Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function. Proc Natl Aced Sci USA 2002;99:955-960.
    • (2002) Proc. Natl. Aced. Sci. USA , vol.99 , pp. 955-960
    • Demirov, D.G.1    Ono, A.2    Orenstein, J.M.3    Freed, E.O.4
  • 34
    • 0036845721 scopus 로고    scopus 로고
    • Potential roles of cellular proteins in HIV-1
    • Ott DE. Potential roles of cellular proteins in HIV-1. Rev Med Virol 2002;12:359-374.
    • (2002) Rev. Med. Virol. , vol.12 , pp. 359-374
    • Ott, D.E.1
  • 37
    • 0027332763 scopus 로고
    • Association of host cell surface adhesion receptors and other membrane proteins with HIV and SIV
    • Orentas RJ, Hildreth JE. Association of host cell surface adhesion receptors and other membrane proteins with HIV and SIV. AIDS Res Hum Retroviruses 1993;9:1157-1165.
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , pp. 1157-1165
    • Orentas, R.J.1    Hildreth, J.E.2
  • 38
    • 0031592609 scopus 로고    scopus 로고
    • Cell membrane vesicles are a major contaminant of gradient-enriched human immunodeficiency virus type-1 preparations
    • Gluschankof P, Mondor I, Gelderblom HR, Sattentau QJ. Cell membrane vesicles are a major contaminant of gradient-enriched human immunodeficiency virus type-1 preparations. Virology 1997;230:125-133.
    • (1997) Virology , vol.230 , pp. 125-133
    • Gluschankof, P.1    Mondor, I.2    Gelderblom, H.R.3    Sattentau, Q.J.4
  • 39
    • 0033999270 scopus 로고    scopus 로고
    • Role of the Gag matrix domain in targeting human immunodeficiency virus type 1 assembly
    • Ono A, Orenstein JM, Freed EO. Role of the Gag matrix domain in targeting human immunodeficiency virus type 1 assembly. J Virol 2000;74:2855-2866.
    • (2000) J. Virol. , vol.74 , pp. 2855-2866
    • Ono, A.1    Orenstein, J.M.2    Freed, E.O.3
  • 40
    • 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
  • 41
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • Aloia RC, Tian H, Jensen FC. Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc Natl Aced Sci USA 1993;90:5181-5185.
    • (1993) Proc. Natl. Aced. Sci. USA , vol.90 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.2    Jensen, F.C.3
  • 42
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in HIV-1 assembly and release
    • Ono A, Freed EO. Plasma membrane rafts play a critical role in HIV-1 assembly and release. Proc Natl Acad Sci USA 2001;98: 13925-13930.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13925-13930
    • Ono, A.1    Freed, E.O.2
  • 43
    • 0034864631 scopus 로고    scopus 로고
    • Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains
    • Lindwasser OW, Resh MD. Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains. J Virol 2001;75:7913-7924.
    • (2001) J. Virol. , vol.75 , pp. 7913-7924
    • Lindwasser, O.W.1    Resh, M.D.2
  • 44
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • Nguyen DH, Hildreth JE. Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts. J Virol 2000;74:3264-3272.
    • (2000) J. Virol. , vol.74 , pp. 3264-3272
    • Nguyen, D.H.1    Hildreth, J.E.2
  • 45
    • 0034610368 scopus 로고    scopus 로고
    • Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity
    • Rousso I, Mixon MB, Chen BK, Kim PS. Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity. Proc Natl Acad Sci USA 2000;97:13523-13525.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13523-13525
    • Rousso, I.1    Mixon, M.B.2    Chen, B.K.3    Kim, P.S.4
  • 46
    • 0037302342 scopus 로고    scopus 로고
    • Independent segregation of human immunodeficiency virus type 1 Gag protein complexes and lipid rafts
    • Ding L, Derdowski A, Wang JJ, Spearman P. Independent segregation of human immunodeficiency virus type 1 Gag protein complexes and lipid rafts. J Virol 2003;77:1916-1926.
    • (2003) J. Virol. , vol.77 , pp. 1916-1926
    • Ding, L.1    Derdowski, A.2    Wang, J.J.3    Spearman, P.4
  • 47
    • 0034529050 scopus 로고    scopus 로고
    • How cells handle cholesterol
    • Simons K, Ikonen E. How cells handle cholesterol. Science 2000; 290:1721-1726.
    • (2000) Science , vol.290 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2
  • 49
    • 0034252971 scopus 로고    scopus 로고
    • Concentration of MHC class II molecules in lipid rafts facilitates antigen presentation
    • Anderson HA, Hiltbold EM, Roche PA. Concentration of MHC class II molecules in lipid rafts facilitates antigen presentation. Nat Immunol 2000;1:156-162.
    • (2000) Nat. Immunol. , vol.1 , pp. 156-162
    • Anderson, H.A.1    Hiltbold, E.M.2    Roche, P.A.3
  • 50
    • 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
  • 51
    • 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
  • 52
    • 0037303193 scopus 로고    scopus 로고
    • Overlapping motifs (PTAP and PPEY) within the Elbola virus VP40 protein function independently as late budding domains: Involvement of host proteins TSG101 and VPS-4
    • Licata JM, Simpson-Holley M, Wright NT, Han Z, Paragas J, Harty RN. Overlapping motifs (PTAP and PPEY) within the Elbola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4. J Virol 2003;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
  • 55
    • 0029762913 scopus 로고    scopus 로고
    • Improving structural integrity of cryosections for immunogold labeling
    • Liou W, Geuze HJ, Slot JW. Improving structural integrity of cryosections for immunogold labeling. Histochem Cell Biol 1996; 106:41-58.
    • (1996) Histochem. Cell Biol. , vol.106 , pp. 41-58
    • Liou, W.1    Geuze, H.J.2    Slot, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.