메뉴 건너뛰기




Volumn 25, Issue 12, 2009, Pages 1197-1210

Antiviral activity of the interferon-induced cellular protein BST-2/tetherin

Author keywords

[No Author keywords available]

Indexed keywords

ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; BONE MARROW STROMAL ANTIGEN 2; INTERFERON; MEMBRANE PROTEIN; NEF PROTEIN; TETHERIN; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; VIRUS PROTEIN; VPU PROTEIN; VPU PROTEIN INHIBITOR;

EID: 73149087722     PISSN: 08892229     EISSN: None     Source Type: Journal    
DOI: 10.1089/aid.2009.0253     Document Type: Review
Times cited : (79)

References (77)
  • 1
    • 0023677668 scopus 로고
    • A novel gene of HIV- 1, vpu, and its 16-kilodalton product
    • Strebel K, Klimkait T, and Martin MA: A novel gene of HIV- 1, vpu, and its 16-kilodalton product. Science 1988;241:1221-1223.
    • (1988) Science , vol.241 , pp. 1221-1223
    • Strebel, K.1    Klimkait, T.2    Martin, M.A.3
  • 3
    • 0025139857 scopus 로고
    • The human immunodeficiency virus type 1-specific protein vpu is required for efficient virus maturation and release
    • Klimkait T, Strebel K, Hoggan MD, Martin MA, and Orenstein JM: The human immunodeficiency virus type 1-specific protein vpu is required for efficient virus maturation and release. J Virol 1990;64(2):621-629.
    • (1990) J Virol , vol.64 , Issue.2 , pp. 621-629
    • Klimkait, T.1    Strebel, K.2    Hoggan, M.D.3    Martin, M.A.4    Orenstein, J.M.5
  • 4
    • 0028863722 scopus 로고
    • Function of human immunodeficiency virus type 1 Vpu protein in various cell types
    • Sakai H, Tokunaga K, Kawamura M, and Adachi A: Function of human immunodeficiency virus type 1 Vpu protein in various cell types. J Gen Virol 1995;76( Pt 11): 2717-2722.
    • (1995) J Gen Virol , vol.76 , Issue.PART 11 , pp. 2717-2722
    • Sakai, H.1    Tokunaga, K.2    Kawamura, M.3    Adachi, A.4
  • 5
    • 0025000834 scopus 로고
    • Interferon-α treatment leads to accumulation of virus particles on the surface of cells persistently infected with the human immunodeficiency virus type 1
    • Yasuda Y, Miyake S, Kato S, et al.: Interferon-alpha treatment leads to accumulation of virus particles on the surface of cells persistently infected with the human immunodeficiency virus type 1. J Acquir Immune Defic Syndr 1990;3(11): 1046-1051. (Pubitemid 20373632)
    • (1990) Journal of Acquired Immune Deficiency Syndromes , vol.3 , Issue.11 , pp. 1046-1051
    • Yasuda, Y.1    Miyake, S.2    Kato, S.3    Kita, M.4    Kishida, T.5    Kimura, T.6    Ikuta, K.7
  • 6
    • 0032130973 scopus 로고    scopus 로고
    • Effects of IFN alpha on late stages of HIV-1 replication cycle
    • Dianzani F, Castilletti C, Gentile M, et al.: Effects of IFN alpha on late stages of HIV-1 replication cycle. Biochimie 1998;80(8-9):745-754.
    • (1998) Biochimie , vol.80 , Issue.8-9 , pp. 745-754
    • Dianzani, F.1    Castilletti, C.2    Gentile, M.3
  • 7
    • 0027306176 scopus 로고
    • Vpu protein of human immunodeficiency virus type 1 enhances the release of capsids produced by gag gene constructs of widely divergent retroviruses
    • Gottlinger HG, Dorfman T, Cohen EA, and Haseltine WA: Vpu protein of human immunodeficiency virus type 1 enhances the release of capsids produced by gag gene constructs of widely divergent retroviruses. Proc Natl Acad Sci USA 1993;90(15):7381-7385.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.15 , pp. 7381-7385
    • Gottlinger, H.G.1    Dorfman, T.2    Cohen, E.A.3    Haseltine, W.A.4
  • 8
    • 0344303622 scopus 로고    scopus 로고
    • Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production
    • Varthakavi V, Smith RM, Bour SP, Strebel K, and Spearman P: Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production. Proc Natl Acad Sci USA 2003;100(25):15154-15159.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.25 , pp. 15154-15159
    • Varthakavi, V.1    Smith, R.M.2    Bour, S.P.3    Strebel, K.4    Spearman, P.5
  • 9
    • 33646921736 scopus 로고    scopus 로고
    • HIV-1 Vpu promotes release and prevents endocytosis of nascent retrovirus particles from the plasma membrane
    • Neil SJ, Eastman SW, Jouvenet N, and Bieniasz PD: HIV-1 Vpu promotes release and prevents endocytosis of nascent retrovirus particles from the plasma membrane. PLoS Pathog 2006;2(5):e39.
    • (2006) PLoS Pathog , vol.2 , Issue.5
    • Neil, S.J.1    Eastman, S.W.2    Jouvenet, N.3    Bieniasz, P.D.4
  • 10
    • 34548392739 scopus 로고    scopus 로고
    • An interferon-alpha-induced tethering mechanism inhibits HIV-1 and Ebola virus particle release but is counteracted by the HIV-1 Vpu protein
    • Neil SJ, Sandrin V, Sundquist WI, and Bieniasz PD: An interferon-alpha-induced tethering mechanism inhibits HIV-1 and Ebola virus particle release but is counteracted by the HIV-1 Vpu protein. Cell Host Microbe 2007;2(3):193-203.
    • (2007) Cell Host Microbe , vol.2 , Issue.3 , pp. 193-203
    • Neil, S.J.1    Sandrin, V.2    Sundquist, W.I.3    Bieniasz, P.D.4
  • 11
    • 33750470785 scopus 로고    scopus 로고
    • Quantitative membrane proteomics reveals new cellular targets of viral immune modulators
    • Bartee E, McCormack A, and Fruh K: Quantitative membrane proteomics reveals new cellular targets of viral immune modulators. PLoS Pathog 2006;2(10):e107.
    • (2006) PLoS Pathog , vol.2 , Issue.10
    • Bartee, E.1    McCormack, A.2    Fruh, K.3
  • 12
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • Margottin F, Bour SP, Durand H, et al.: A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol Cell 1998;1(4):565-574.
    • (1998) Mol Cell , vol.1 , Issue.4 , pp. 565-574
    • Margottin, F.1    Bour, S.P.2    Durand, H.3
  • 13
    • 33747803946 scopus 로고    scopus 로고
    • Bone marrow stromal cell antigen 2 is a specific marker of type i IFN-producing cells in the naive mouse, but a promiscuous cell surface antigen following IFN stimulation
    • Blasius AL, Giurisato E, Cella M, et al.: Bone marrow stromal cell antigen 2 is a specific marker of type I IFN-producing cells in the naive mouse, but a promiscuous cell surface antigen following IFN stimulation. J Immunol 2006;177(5): 3260-3265.
    • (2006) J Immunol , vol.177 , Issue.5 , pp. 3260-3265
    • Blasius, A.L.1    Giurisato, E.2    Cella, M.3
  • 14
    • 28844451507 scopus 로고    scopus 로고
    • Characterization of antibodies submitted to the B cell section of the 8th Human Leukocyte Differentiation Antigens Workshop by flow cytometry and immunohistochemistry
    • Vidal-Laliena M, Romero X, March S, et al.: Characterization of antibodies submitted to the B cell section of the 8th Human Leukocyte Differentiation Antigens Workshop by flow cytometry and immunohistochemistry. Cell Immunol 2005;236(1-2):6-16.
    • (2005) Cell Immunol , vol.236 , Issue.1-2 , pp. 6-16
    • Vidal-Laliena, M.1    Romero, X.2    March, S.3
  • 15
    • 0141494290 scopus 로고    scopus 로고
    • Bst-2=HM1.24 is a raft-associated apical membrane protein with an unusual topology
    • Kupzig S, Korolchuk V, Rollason R, et al.: Bst-2=HM1.24 is a raft-associated apical membrane protein with an unusual topology. Traffic 2003;4(10):694-709.
    • (2003) Traffic , vol.4 , Issue.10 , pp. 694-709
    • Kupzig, S.1    Korolchuk, V.2    Rollason, R.3
  • 16
    • 41849116366 scopus 로고    scopus 로고
    • The interferoninduced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein
    • Van Damme N, Goff D, Katsura C, et al.: The interferoninduced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein. Cell Host Microbe 2008;3(4):245-252.
    • (2008) Cell Host Microbe , vol.3 , Issue.4 , pp. 245-252
    • Van Damme, N.1    Goff, D.2    Katsura, C.3
  • 17
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil SJ, Zang T, and Bieniasz PD: Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 2008; 451(7177):425-430.
    • (2008) Nature , vol.451 , Issue.7177 , pp. 425-430
    • Neil, S.J.1    Zang, T.2    Bieniasz, P.D.3
  • 18
    • 0033583795 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a surface antigen preferentially overexpressed on multiple myeloma cells
    • Ohtomo T, Sugamata Y, Ozaki Y, et al.: Molecular cloning and characterization of a surface antigen preferentially overexpressed on multiple myeloma cells. Biochem Biophys Res Commun 1999;258(3):583-591.
    • (1999) Biochem Biophys Res Commun , vol.258 , Issue.3 , pp. 583-591
    • Ohtomo, T.1    Sugamata, Y.2    Ozaki, Y.3
  • 19
    • 36549052593 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis of a lipid-raft-associated protein is mediated through a dual tyrosine motif
    • Rollason R, Korolchuk V, Hamilton C, Schu P, and Banting G: Clathrin-mediated endocytosis of a lipid-raft-associated protein is mediated through a dual tyrosine motif. J Cell Sci 2007;120(Pt 21):3850-3858.
    • (2007) J Cell Sci , vol.120 , Issue.PART 21 , pp. 3850-3858
    • Rollason, R.1    Korolchuk, V.2    Hamilton, C.3    Schu, P.4    Banting, G.5
  • 20
    • 67650120099 scopus 로고    scopus 로고
    • HM1.24 is internalized from lipid rafts by clathrin-mediated endocytosis through interaction with alpha-adaptin
    • Masuyama N, Kuronita T, Tanaka R, et al.: HM1.24 is internalized from lipid rafts by clathrin-mediated endocytosis through interaction with alpha-adaptin. J Biol Chem 2009; 284(23):15927-15941.
    • (2009) J Biol Chem , vol.284 , Issue.23 , pp. 15927-15941
    • Masuyama, N.1    Kuronita, T.2    Tanaka, R.3
  • 21
    • 70349267563 scopus 로고    scopus 로고
    • Molecular mechanism of BST2=tetherin downregulation by K5=MIR2 of Kaposi's sarcoma-associated herpesvirus
    • Mansouri M, Viswanathan K, Douglas JL, et al.: Molecular mechanism of BST2=tetherin downregulation by K5=MIR2 of Kaposi's sarcoma-associated herpesvirus. J Virol 2009; 83(19):9672-9681.
    • (2009) J Virol , vol.83 , Issue.19 , pp. 9672-9681
    • Mansouri, M.1    Viswanathan, K.2    Douglas, J.L.3
  • 22
    • 67249114758 scopus 로고    scopus 로고
    • Species-specific activity of SIV Nef and HIV-1 Vpu in overcoming restriction by tetherin=BST2
    • Jia B, Serra-Moreno R, Neidermyer W, et al.: Species-specific activity of SIV Nef and HIV-1 Vpu in overcoming restriction by tetherin=BST2. PLoS Pathog 2009;5(5):e1000429.
    • (2009) PLoS Pathog , vol.5 , Issue.5
    • Jia, B.1    Serra-Moreno, R.2    Neidermyer, W.3
  • 23
    • 67651111833 scopus 로고    scopus 로고
    • Nef proteins from simian immunodeficiency viruses are tetherin antagonists
    • Zhang F, Wilson SJ, Landford WC, et al.: Nef proteins from simian immunodeficiency viruses are tetherin antagonists. Cell Host Microbe 2009;6(1):54-67.
    • (2009) Cell Host Microbe , vol.6 , Issue.1 , pp. 54-67
    • Zhang, F.1    Wilson, S.J.2    Landford, W.C.3
  • 24
    • 66149099203 scopus 로고    scopus 로고
    • Suppression of tetherin-restricting activity upon human immunodeficiency virus type 1 particle release correlates with localization of Vpu in the trans-Golgi network
    • Dube M, Roy BB, Guiot-Guillain P, et al.: Suppression of tetherin-restricting activity upon human immunodeficiency virus type 1 particle release correlates with localization of Vpu in the trans-Golgi network. J Virol 2009;83(9):4574-4590.
    • (2009) J Virol , vol.83 , Issue.9 , pp. 4574-4590
    • Dube, M.1    Roy, B.B.2    Guiot-Guillain, P.3
  • 25
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • Aloia RC, Tian H, and Jensen FC: Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc Natl Acad Sci USA 1993;90(11):5181-5185.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.11 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.2    Jensen, F.C.3
  • 26
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • Nguyen DH and Hildreth JEK: 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.K.2
  • 27
    • 0346734116 scopus 로고    scopus 로고
    • In vivo oligomerization and raft localization of Ebola virus protein VP40 during vesicular budding
    • Panchal RG, Ruthel G, Kenny TA, et al.: In vivo oligomerization and raft localization of Ebola virus protein VP40 during vesicular budding. Proc Natl Acad Sci USA 2003; 100(26):15936-15941.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.26 , pp. 15936-15941
    • Panchal, R.G.1    Ruthel, G.2    Kenny, T.A.3
  • 28
    • 60049094369 scopus 로고    scopus 로고
    • Inhibition of Lassa and Marburg virus production by tetherin
    • Sakuma T, Noda T, Urata S, Kawaoka Y, and Yasuda J: Inhibition of Lassa and Marburg virus production by tetherin. J Virol 2009;83(5):2382-2385.
    • (2009) J Virol , vol.83 , Issue.5 , pp. 2382-2385
    • Sakuma, T.1    Noda, T.2    Urata, S.3    Kawaoka, Y.4    Yasuda, J.5
  • 29
    • 70349935302 scopus 로고    scopus 로고
    • The formation of cysteine-linked dimers of BST-2=tetherin is important for inhibition of HIV-1 virus release but not for sensitivity to Vpu
    • Andrew AJ, Miyagi E, Kao S, and Strebel K: The formation of cysteine-linked dimers of BST-2=tetherin is important for inhibition of HIV-1 virus release but not for sensitivity to Vpu. Retrovirology 2009;6(1):80.
    • (2009) Retrovirology , vol.6 , Issue.1 , pp. 80
    • Andrew, A.J.1    Miyagi, E.2    Kao, S.3    Strebel, K.4
  • 30
    • 70349125041 scopus 로고    scopus 로고
    • Dimerization of tetherin is not essential for its antiviral activity against Lassa and Marburg viruses
    • Sakuma T, Sakurai A, and Yasuda J: Dimerization of tetherin is not essential for its antiviral activity against Lassa and Marburg viruses. PLoS One 2009;4(9):e6934.
    • (2009) PLoS One , vol.4 , Issue.9
    • Sakuma, T.1    Sakurai, A.2    Yasuda, J.3
  • 31
    • 62449106199 scopus 로고    scopus 로고
    • Tetherin-mediated restriction of filovirus budding is antagonized by the Ebola glycoprotein
    • Kaletsky RL, Francica JR, grawal-Gamse C, and Bates P: Tetherin-mediated restriction of filovirus budding is antagonized by the Ebola glycoprotein. Proc Natl Acad Sci U S A 2009;106(8):2886-2891.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.8 , pp. 2886-2891
    • Kaletsky, R.L.1    Francica, J.R.2    Grawal-Gamse, C.3    Bates, P.4
  • 32
    • 60049094369 scopus 로고    scopus 로고
    • Inhibition of Lassa and Marburg virus production by tetherin
    • Sakuma T, Noda T, Urata S, Kawaoka Y, and Yasuda J: Inhibition of Lassa and Marburg virus production by tetherin. J Virol 2008;83(5):2382-2385.
    • (2008) J Virol , vol.83 , Issue.5 , pp. 2382-2385
    • Sakuma, T.1    Noda, T.2    Urata, S.3    Kawaoka, Y.4    Yasuda, J.5
  • 33
    • 59649124256 scopus 로고    scopus 로고
    • Broad-spectrum inhibition of retroviral and filoviral particle release by tetherin
    • Jouvenet N, Neil SJ, Zhadina M, et al.: Broad-spectrum inhibition of retroviral and filoviral particle release by tetherin. J Virol 2009;83(4):1837-1844.
    • (2009) J Virol , vol.83 , Issue.4 , pp. 1837-1844
    • Jouvenet, N.1    Neil, S.J.2    Zhadina, M.3
  • 34
    • 67249157032 scopus 로고    scopus 로고
    • Vpu antagonizes BST-2-mediated restriction ofHIV-1 release via beta-TrCP and endo-lysosomal trafficking
    • Mitchell RS, Katsura C, Skasko MA, et al.: Vpu antagonizes BST-2-mediated restriction ofHIV-1 release via beta-TrCP and endo-lysosomal trafficking. PLoS Pathog 2009;5(5):e1000450.
    • (2009) PLoS Pathog , vol.5 , Issue.5
    • Mitchell, R.S.1    Katsura, C.2    Skasko, M.A.3
  • 35
    • 77950424913 scopus 로고    scopus 로고
    • Direct restriction of virus release and incorporation of the interferon-induced protein BST-2 into HIV-1 particles
    • in press
    • Fitzpatrick K, SkaskoM, Deerinck T, et al.: Direct restriction of virus release and incorporation of the interferon-induced protein BST-2 into HIV-1 particles. PLoS Pathog 2009, in press.
    • (2009) PLoS Pathog
    • Fitzpatrick, K.1    Skaskom Deerinck, T.2
  • 36
    • 70350348675 scopus 로고    scopus 로고
    • Tetherin inhibits HIV-1 release by directly tethering virions to cells
    • Perez-Caballero D, Zang T, Ebrahimi A, et al.: Tetherin inhibits HIV-1 release by directly tethering virions to cells. Cell 2009;139:499-511.
    • (2009) Cell , vol.139 , pp. 499-511
    • Perez-Caballero, D.1    Zang, T.2    Ebrahimi, A.3
  • 37
    • 67650077552 scopus 로고    scopus 로고
    • Comparative study on the effect of human BST-2=tetherin on HIV-1 release in cells of various species
    • Sato K, Yamamoto SP, Misawa N, et al.: Comparative study on the effect of human BST-2=tetherin on HIV-1 release in cells of various species. Retrovirology 2009;6:53.
    • (2009) Retrovirology , vol.6 , pp. 53
    • Sato, K.1    Yamamoto, S.P.2    Misawa, N.3
  • 38
    • 44649139364 scopus 로고    scopus 로고
    • HIV-1 accessory proteins- ensuring viral survival in a hostile environment
    • Malim MH and Emerman M: HIV-1 accessory proteins- ensuring viral survival in a hostile environment. Cell Host Microbe 2008;3(6):388-398.
    • (2008) Cell Host Microbe , vol.3 , Issue.6 , pp. 388-398
    • Malim, M.H.1    Emerman, M.2
  • 39
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys
    • Stremlau M, Owens CM, Perron MJ, et al.: The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature 2004;427(6977):848-853.
    • (2004) Nature , vol.427 , Issue.6977 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3
  • 40
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu X, Yu Y, Liu B, et al.: Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 2003;302(5647):1056-1060.
    • (2003) Science , vol.302 , Issue.5647 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3
  • 41
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle A, Strack B, Ancuta P, et al.: Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J Biol Chem 2004; 279(9):7792-7798.
    • (2004) J Biol Chem , vol.279 , Issue.9 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3
  • 42
    • 33744797119 scopus 로고    scopus 로고
    • Viral modulators of cullin RING ubiquitin ligases: Culling the host defense
    • Barry M and Fruh K: Viral modulators of cullin RING ubiquitin ligases: Culling the host defense. Sci STKE 2006; 2006(335):e21.
    • (2006) Sci STKE , vol.2006 , Issue.335
    • Barry, M.1    Fruh, K.2
  • 43
    • 70350266393 scopus 로고    scopus 로고
    • Antagonism and intracellular sequestration of human tetherin by the HIV-2 envelope glycoprotein
    • Le Tortorec A and Neil SJ: Antagonism and intracellular sequestration of human tetherin by the HIV-2 envelope glycoprotein. J Virol 2009;83:11966-11978.
    • (2009) J Virol , vol.83 , pp. 11966-11978
    • Le Tortorec, A.1    Neil, S.J.2
  • 44
    • 73949107791 scopus 로고    scopus 로고
    • Simian immunodeficiency virus envelope glycoprotein counteracts tetherin=BST-2=CD317 by intracellular sequestration
    • epub
    • Gupta RK, Mlcochova P, Pelchen-Matthews A, et al.: Simian immunodeficiency virus envelope glycoprotein counteracts tetherin=BST-2=CD317 by intracellular sequestration. Proc Natl Acad Sci USA 2009 epub.
    • (2009) Proc Natl Acad Sci USA
    • Gupta, R.K.1    Mlcochova, P.2    Pelchen-Matthews, A.3
  • 45
    • 67249100279 scopus 로고    scopus 로고
    • Mutation of a single residue renders human tetherin resistant to HIV-1 Vpumediated depletion
    • Gupta RK, Hue S, Schaller T, et al.: Mutation of a single residue renders human tetherin resistant to HIV-1 Vpumediated depletion. PLoS Pathog 2009;5(5):e1000443.
    • (2009) PLoS Pathog , vol.5 , Issue.5
    • Gupta, R.K.1    Hue, S.2    Schaller, T.3
  • 46
    • 61849183569 scopus 로고    scopus 로고
    • HIV-1 antagonism of CD317 is species specific and involves Vpu-mediated proteasomal degradation of the restriction factor
    • Goffinet C, Allespach I, Homann S, et al.: HIV-1 antagonism of CD317 is species specific and involves Vpu-mediated proteasomal degradation of the restriction factor. Cell Host Microbe 2009;5(3):285-297.
    • (2009) Cell Host Microbe , vol.5 , Issue.3 , pp. 285-297
    • Goffinet, C.1    Allespach, I.2    Homann, S.3
  • 47
    • 33644654306 scopus 로고    scopus 로고
    • The pericentriolar recycling endosome plays a key role in Vpu-mediated enhancement of HIV-1 particle release
    • Varthakavi V, Smith RM, Martin KL, et al.: The pericentriolar recycling endosome plays a key role in Vpu-mediated enhancement of HIV-1 particle release. Traffic 2006;7(3):298-307.
    • (2006) Traffic , vol.7 , Issue.3 , pp. 298-307
    • Varthakavi, V.1    Smith, R.M.2    Martin, K.L.3
  • 48
    • 42149092583 scopus 로고    scopus 로고
    • HIV-1 Vpu inhibits accumulation of the envelope glycoprotein within clathrincoated, Gag-containing endosomes
    • Van Damme N and Guatelli J: HIV-1 Vpu inhibits accumulation of the envelope glycoprotein within clathrincoated, Gag-containing endosomes. Cell Microbiol 2007;10: 1040-1057.
    • (2007) Cell Microbiol , vol.10 , pp. 1040-1057
    • Van Damme, N.1    Guatelli, J.2
  • 49
    • 67650860393 scopus 로고    scopus 로고
    • The transmembrane domain of BST-2 determines its sensitivity to down-modulation by human immunodeficiency virus type 1 Vpu
    • Rong L, Zhang J, Lu J, et al.: The transmembrane domain of BST-2 determines its sensitivity to down-modulation by human immunodeficiency virus type 1 Vpu. J Virol 2009; 83(15):7536-7546.
    • (2009) J Virol , vol.83 , Issue.15 , pp. 7536-7546
    • Rong, L.1    Zhang, J.2    Lu, J.3
  • 50
    • 67749095196 scopus 로고    scopus 로고
    • Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2=tetherin via a {beta}TrCP-dependent mechanism
    • Douglas JL, Viswanathan K, McCarroll MN, et al.: Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2=tetherin via a {beta}TrCP-dependent mechanism. J Virol 2009;83(16):7931-7947.
    • (2009) J Virol , vol.83 , Issue.16 , pp. 7931-7947
    • Douglas, J.L.1    Viswanathan, K.2    McCarroll, M.N.3
  • 51
    • 70349663496 scopus 로고    scopus 로고
    • HIV-1 Vpu neutralizes the antiviral factor tetherin=BST-2 by binding it and directing its beta-TrCP2-dependent degradation
    • Mangeat B, Gers-Huber G, Lehmann M, et al.: HIV-1 Vpu neutralizes the antiviral factor tetherin=BST-2 by binding it and directing its beta-TrCP2-dependent degradation. PLoS Pathog 2009;5(9):e1000574.
    • (2009) PLoS Pathog , vol.5 , Issue.9
    • Mangeat, B.1    Gers-Huber, G.2    Lehmann, M.3
  • 52
    • 62449325310 scopus 로고    scopus 로고
    • Vpu enhances HIV-1 virus release in the absence of Bst-2 cell surface downmodulation and intracellular depletion
    • Miyagi E, Andrew AJ, Kao S, and Strebel K: Vpu enhances HIV-1 virus release in the absence of Bst-2 cell surface downmodulation and intracellular depletion. Proc Natl Acad Sci USA 2009;106(8):2868-2873.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.8 , pp. 2868-2873
    • Miyagi, E.1    Andrew, A.J.2    Kao, S.3    Strebel, K.4
  • 53
    • 70350278891 scopus 로고    scopus 로고
    • Simian immunodeficiency virus from African green monkeys (SIVagm) does not antagonize endogenous levels of African green monkey tetherin=BST-2
    • Lim E and Emerman M: Simian immunodeficiency virus from African green monkeys (SIVagm) does not antagonize endogenous levels of African green monkey tetherin=BST-2. J Virol 2009;83(22):11673-11681.
    • (2009) J Virol , vol.83 , Issue.22 , pp. 11673-11681
    • Lim, E.1    Emerman, M.2
  • 54
    • 71749086904 scopus 로고    scopus 로고
    • HIV-1 accessory protein Vpu internalizes cell-surface BST-2=tetherin through transmembrane interactions leading to lysosomes
    • epub
    • Iwabu Y, Fujita H, Kinomoto M, et al.: HIV-1 accessory protein Vpu internalizes cell-surface BST-2=tetherin through transmembrane interactions leading to lysosomes. J Biol Chem 2009 epub.
    • (2009) J Biol Chem
    • Iwabu, Y.1    Fujita, H.2    Kinomoto, M.3
  • 55
    • 0030052467 scopus 로고    scopus 로고
    • The envelope glycoprotein of human immunodeficiency virus type 2 enhances viral particle release: A Vpu-like factor?
    • Bour S, Schubert U, Peden K, and Strebel K: The envelope glycoprotein of human immunodeficiency virus type 2 enhances viral particle release: A Vpu-like factor? J Virol 1996;70(2):820-829.
    • (1996) J Virol , vol.70 , Issue.2 , pp. 820-829
    • Bour, S.1    Schubert, U.2    Peden, K.3    Strebel, K.4
  • 56
    • 14744281049 scopus 로고    scopus 로고
    • Functional domains within the human immunodeficiency virus type 2 envelope protein required to enhance virus production
    • Abada P, Noble B, and Cannon PM: Functional domains within the human immunodeficiency virus type 2 envelope protein required to enhance virus production. J Virol 2005; 79(6):3627-3638.
    • (2005) J Virol , vol.79 , Issue.6 , pp. 3627-3638
    • Abada, P.1    Noble, B.2    Cannon, P.M.3
  • 58
    • 61449243774 scopus 로고    scopus 로고
    • Species-specific activity of HIV-1 Vpu and positive selection of tetherin transmembrane domain variants
    • McNatt MW, Zang T, Hatziioannou T, et al.: Species-specific activity of HIV-1 Vpu and positive selection of tetherin transmembrane domain variants. PLoS Pathog 2009;5(2): e1000300.
    • (2009) PLoS Pathog , vol.5 , Issue.2
    • McNatt, M.W.1    Zang, T.2    Hatziioannou, T.3
  • 59
    • 0030069139 scopus 로고    scopus 로고
    • The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains
    • Schubert U, Bour S, Ferrer-Montiel AV, et al.: The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains. J Virol 1996;70(2):809-819.
    • (1996) J Virol , vol.70 , Issue.2 , pp. 809-819
    • Schubert, U.1    Bour, S.2    Ferrer-Montiel, A.V.3
  • 60
    • 0034469259 scopus 로고    scopus 로고
    • An in vitro rapid-turnover assay for human immunodeficiency virus type 1 replication selects for cell-to-cell spread of virus
    • Gummuluru S, Kinsey CM, and Emerman M: An in vitro rapid-turnover assay for human immunodeficiency virus type 1 replication selects for cell-to-cell spread of virus. J Virol 2000;74(23):10882-10891.
    • (2000) J Virol , vol.74 , Issue.23 , pp. 10882-10891
    • Gummuluru, S.1    Kinsey, C.M.2    Emerman, M.3
  • 61
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamindependent fusion with endosomes
    • Miyauchi K, Kim Y, Latinovic O, Morozov V, and Melikyan GB: HIV enters cells via endocytosis and dynamindependent fusion with endosomes. Cell 2009:137(3):433-444.
    • (2009) Cell , vol.137 , Issue.3 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 62
    • 73149102228 scopus 로고    scopus 로고
    • BCA2=Rabring7 promotes tetherin-dependent HIV-1 restriction
    • in press
    • Miyakawa K, Ryo A, Murakami T, et al.: BCA2=Rabring7 promotes tetherin-dependent HIV-1 restriction. PLoS Pathog 2009, in press.
    • (2009) PLoS Pathog
    • Miyakawa, K.1    Ryo, A.2    Murakami, T.3
  • 63
    • 0030602182 scopus 로고    scopus 로고
    • Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells
    • Schubert U, Ferrer-Montiel AV, Oblatt-Montal M, et al.: Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells. FEBS Lett 1996; 398(1):12-18.
    • (1996) FEBS Lett , vol.398 , Issue.1 , pp. 12-18
    • Schubert, U.1    Ferrer-Montiel, A.V.2    Oblatt-Montal, M.3
  • 64
    • 0036708437 scopus 로고    scopus 로고
    • Molecular dynamics investigation of membrane-bound bundles of the channel-forming transmembrane domain of viral protein U from the human immunodeficiency virus HIV-1
    • Lopez CF, Montal M, Blasie JK, Klein ML, and Moore PB: Molecular dynamics investigation of membrane-bound bundles of the channel-forming transmembrane domain of viral protein U from the human immunodeficiency virus HIV-1. Biophys J 2002;83(3):1259-1267.
    • (2002) Biophys J , vol.83 , Issue.3 , pp. 1259-1267
    • Lopez, C.F.1    Montal, M.2    Blasie, J.K.3    Klein, M.L.4    Moore, P.B.5
  • 65
    • 33749511249 scopus 로고    scopus 로고
    • Three-dimensional structure of the transmembrane domain of Vpu from HIV-1 in aligned phospholipid bicelles
    • Park SH, De Angelis AA, Nevzorov AA, Wu CH, and Opella SJ: Three-dimensional structure of the transmembrane domain of Vpu from HIV-1 in aligned phospholipid bicelles. Biophys J 2006;91(8):3032-3042.
    • (2006) Biophys J , vol.91 , Issue.8 , pp. 3032-3042
    • Park, S.H.1    De Angelis, A.A.2    Nevzorov, A.A.3    Wu, C.H.4    Opella, S.J.5
  • 66
    • 67249093700 scopus 로고    scopus 로고
    • Vpu matchmakers as a therapeutic strategy for HIV infection
    • Montal M: Vpu matchmakers as a therapeutic strategy for HIV infection. PLoS Pathog 2009;5(5):e1000246.
    • (2009) PLoS Pathog , vol.5 , Issue.5
    • Montal, M.1
  • 67
    • 1942502838 scopus 로고    scopus 로고
    • Mutual functional destruction of HIV-1 Vpu and host TASK- 1 channel
    • Hsu K, Seharaseyon J, Dong P, Bour S, and Marban E: Mutual functional destruction of HIV-1 Vpu and host TASK- 1 channel. Mol Cell 2004;14(2):259-267.
    • (2004) Mol Cell , vol.14 , Issue.2 , pp. 259-267
    • Hsu, K.1    Seharaseyon, J.2    Dong, P.3    Bour, S.4    Marban, E.5
  • 69
    • 69249222743 scopus 로고    scopus 로고
    • A New World primate deficient in tetherin-mediated restriction of human immunodeficiency virus type 1
    • Wong SK, Connole M, Sullivan JS, et al.: A New World primate deficient in tetherin-mediated restriction of human immunodeficiency virus type 1. J Virol 2009;83(17):8771-8780.
    • (2009) J Virol , vol.83 , Issue.17 , pp. 8771-8780
    • Wong, S.K.1    Connole, M.2    Sullivan, J.S.3
  • 70
    • 0038279871 scopus 로고    scopus 로고
    • Characterization of a novel simian immunodeficiency virus (SIVmonNG1) genome sequence from a mona monkey (Cercopithecus mona)
    • Barlow KL, Ajao AO, and Clewley JP: Characterization of a novel simian immunodeficiency virus (SIVmonNG1) genome sequence from a mona monkey (Cercopithecus mona). J Virol 2003;77(12):6879-6888.
    • (2003) J Virol , vol.77 , Issue.12 , pp. 6879-6888
    • Barlow, K.L.1    Ajao, A.O.2    Clewley, J.P.3
  • 71
    • 0036319292 scopus 로고    scopus 로고
    • Characterization of a novel simian immunodeficiency virus with a vpu gene from greater spot-nosed monkeys (Cercopithecus nictitans) provides new insights into simian=human immunodeficiency virus phylogeny
    • Courgnaud V, Salemi M, Pourrut X, et al.: Characterization of a novel simian immunodeficiency virus with a vpu gene from greater spot-nosed monkeys (Cercopithecus nictitans) provides new insights into simian=human immunodeficiency virus phylogeny. J Virol 2002;76(16):8298-8309.
    • (2002) J Virol , vol.76 , Issue.16 , pp. 8298-8309
    • Courgnaud, V.1    Salemi, M.2    Pourrut, X.3
  • 72
    • 20744440450 scopus 로고    scopus 로고
    • Characterization of a novel vpu-harboring simian immunodeficiency virus from a Dent's Mona monkey (Cercopithecus mona denti)
    • Dazza MC, Ekwalanga M, Nende M, et al.: Characterization of a novel vpu-harboring simian immunodeficiency virus from a Dent's Mona monkey (Cercopithecus mona denti). J Virol 2005;79(13):8560-8571.
    • (2005) J Virol , vol.79 , Issue.13 , pp. 8560-8571
    • Dazza, M.C.1    Ekwalanga, M.2    Nende, M.3
  • 73
    • 0038047665 scopus 로고    scopus 로고
    • Hybrid origin of SIV in chimpanzees
    • Bailes E, Gao F, Bibollet-Ruche F, et al.: Hybrid origin of SIV in chimpanzees. Science 2003;300(5626):1713.
    • (2003) Science , vol.300 , Issue.5626 , pp. 1713
    • Bailes, E.1    Gao, F.2    Bibollet-Ruche, F.3
  • 74
    • 0036059017 scopus 로고    scopus 로고
    • Deletion of the vpu sequences prior to the Env in a simian-human immunodeficiency virus results in enhanced Env precursor synthesis but is less pathogenic for pig-tailed macaques
    • Stephens EB, McCormick C, Pacyniak E, et al.: Deletion of the vpu sequences prior to the Env in a simian-human immunodeficiency virus results in enhanced Env precursor synthesis but is less pathogenic for pig-tailed macaques. Virology 2002;293(2):252-261.
    • (2002) Virology , vol.293 , Issue.2 , pp. 252-261
    • Stephens, E.B.1    McCormick, C.2    Pacyniak, E.3
  • 75
    • 0037466524 scopus 로고    scopus 로고
    • Naturally occurring amino acid substitutions in the HIV-2 ROD envelope glycoprotein regulate its ability to augment viral particle release
    • Bour S, Akari H, Miyagi E, and Strebel K: Naturally occurring amino acid substitutions in the HIV-2 ROD envelope glycoprotein regulate its ability to augment viral particle release. Virology 2003;309(1):85-98.
    • (2003) Virology , vol.309 , Issue.1 , pp. 85-98
    • Bour, S.1    Akari, H.2    Miyagi, E.3    Strebel, K.4
  • 76
    • 67650507029 scopus 로고    scopus 로고
    • Regulation of TLR7=9 responses in plasmacytoid dendritic cells by BST2 and ILT7 receptor interaction
    • Cao W, Bover L, Cho M, et al.: Regulation of TLR7=9 responses in plasmacytoid dendritic cells by BST2 and ILT7 receptor interaction. J Exp Med 2009;206(7):1603-1614.
    • (2009) J Exp Med , vol.206 , Issue.7 , pp. 1603-1614
    • Cao, W.1    Bover, L.2    Cho, M.3
  • 77
    • 0242362161 scopus 로고    scopus 로고
    • Combining localstructure, fold-recognition, and new fold methods for protein structure prediction
    • Karplus K, Karchin R, Draper J, et al.: Combining localstructure, fold-recognition, and new fold methods for protein structure prediction. Proteins 2003;53(Suppl 6):491-496.
    • (2003) Proteins , vol.53 , Issue.SUPPL. 6 , pp. 491-496
    • Karplus, K.1    Karchin, R.2    Draper, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.