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Volumn 90, Issue 24, 2016, Pages 11062-11074

Antagonism of BST-2/tetherin is a conserved function of the Env glycoprotein of primary HIV-2 isolates

Author keywords

[No Author keywords available]

Indexed keywords

BST 2 PROTEIN; ROD10 PROTEIN; ROD14 PROTEIN; TETHERIN; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; BST2 PROTEIN, HUMAN; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; LEUKOCYTE ANTIGEN; VIRUS ENVELOPE PROTEIN;

EID: 85001093586     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01451-16     Document Type: Article
Times cited : (12)

References (55)
  • 4
    • 84890125460 scopus 로고    scopus 로고
    • HIV accessory proteins versus host restriction factors
    • Strebel K. 2013. HIV accessory proteins versus host restriction factors. Curr Opin Virol 3:692-699. http://dx.doi.org/10.1016/j.coviro.2013.08.004.
    • (2013) Curr Opin Virol , vol.3 , pp. 692-699
    • Strebel, K.1
  • 5
    • 0025733252 scopus 로고
    • Serine phosphorylation-independent downregulation of cell-surface CD4 by nef
    • Garcia JV, Miller AD. 1991. Serine phosphorylation-independent downregulation of cell-surface CD4 by nef. Nature 350:508-511. http://dx.doi.org/10.1038/350508a0.
    • (1991) Nature , vol.350 , pp. 508-511
    • Garcia, J.V.1    Miller, A.D.2
  • 6
    • 0026452726 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4
    • Willey RL, Maldarelli F, Martin MA, Strebel K. 1992. Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4. J Virol 66:7193-7200.
    • (1992) J Virol , vol.66 , pp. 7193-7200
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 7
    • 0026572801 scopus 로고
    • Kinetics of HIV-1 interactions with sCD4 and CD4+ cells: implications for inhibition of virus infection and initial steps of virus entry into cells
    • Dimitrov DS, Willey RL, Martin MA, Blumenthal R. 1992. Kinetics of HIV-1 interactions with sCD4 and CD4+ cells: implications for inhibition of virus infection and initial steps of virus entry into cells. Virology 187:398-406. http://dx.doi.org/10.1016/0042-6822(92)90441-Q.
    • (1992) Virology , vol.187 , pp. 398-406
    • Dimitrov, D.S.1    Willey, R.L.2    Martin, M.A.3    Blumenthal, R.4
  • 8
    • 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, Strebel K. 1996. The envelope glycoprotein of human immunodeficiency virus type 2 enhances viral particle release: a Vpu-like factor? J Virol 70:820-829.
    • (1996) J Virol , vol.70 , pp. 820-829
    • Bour, S.1    Schubert, U.2    Peden, K.3    Strebel, K.4
  • 9
    • 0029956763 scopus 로고    scopus 로고
    • The human immunodeficiency virus (HIV) type 2 envelope protein is a functional complement to HIV type 1 Vpu that enhances particle release of heterologous retroviruses
    • Bour S, Strebel K. 1996. The human immunodeficiency virus (HIV) type 2 envelope protein is a functional complement to HIV type 1 Vpu that enhances particle release of heterologous retroviruses. J Virol 70:8285-8300.
    • (1996) J Virol , vol.70 , pp. 8285-8300
    • Bour, S.1    Strebel, K.2
  • 13
    • 84884769542 scopus 로고    scopus 로고
    • Tetherin/ BST-2 antagonism by Nef depends on a direct physical interaction between Nef and tetherin, and on clathrin-mediated endocytosis
    • Serra-Moreno R, Zimmermann K, Stern LJ, Evans DT. 2013. Tetherin/ BST-2 antagonism by Nef depends on a direct physical interaction between Nef and tetherin, and on clathrin-mediated endocytosis. PLoS Pathog 9:e1003487. http://dx.doi.org/10.1371/journal.ppat.1003487.
    • (2013) PLoS Pathog , vol.9
    • Serra-Moreno, R.1    Zimmermann, K.2    Stern, L.J.3    Evans, D.T.4
  • 14
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil SJ, Zang T, Bieniasz PD. 2008. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451:425-430. http://dx.doi.org /10.1038/nature06553.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.1    Zang, T.2    Bieniasz, P.D.3
  • 15
    • 41849116366 scopus 로고    scopus 로고
    • The interferon-induced 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, Jorgenson RL, Mitchell R, Johnson MC, Stephens EB, Guatelli J. 2008. The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein. Cell Host Microbe 3:245-252. http://dx.doi.org /10.1016/j.chom.2008.03.001.
    • (2008) Cell Host Microbe , vol.3 , pp. 245-252
    • Van Damme, N.1    Goff, D.2    Katsura, C.3    Jorgenson, R.L.4    Mitchell, R.5    Johnson, M.C.6    Stephens, E.B.7    Guatelli, J.8
  • 16
    • 0029918147 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 2 glycoprotein enhancement of particle budding: role of the cytoplasmic domain
    • Ritter GD, Yamshchikov G, Cohen SJ, Mulligan MJ. 1996. Human immunodeficiency virus type 2 glycoprotein enhancement of particle budding: role of the cytoplasmic domain. J Virol 70:2669-2673.
    • (1996) J Virol , vol.70 , pp. 2669-2673
    • Ritter, G.D.1    Yamshchikov, G.2    Cohen, S.J.3    Mulligan, M.J.4
  • 17
    • 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, Cannon PM. 2005. Functional domains within the human immunodeficiency virus type 2 envelope protein required to enhance virus production. J Virol 79:3627-3638. http://dx.doi.org/10.1128 /JVI.79.6.3627-3638.2005.
    • (2005) J Virol , vol.79 , pp. 3627-3638
    • Abada, P.1    Noble, B.2    Cannon, P.M.3
  • 18
    • 70350266393 scopus 로고    scopus 로고
    • Antagonism to and intracellular sequestration of human tetherin by the human immunodeficiency virus type 2 envelope glycoprotein
    • Le Tortorec A, Neil SJ. 2009. Antagonism to and intracellular sequestration of human tetherin by the human immunodeficiency virus type 2 envelope glycoprotein. J Virol 83:11966-11978. http://dx.doi.org/10.1128 /JVI.01515-09.
    • (2009) J Virol , vol.83 , pp. 11966-11978
    • Le Tortorec, A.1    Neil, S.J.2
  • 21
    • 78751505454 scopus 로고    scopus 로고
    • Compensatory changes in the cytoplasmic tail of gp41 confer resistance to tetherin/ BST-2 in a pathogenic nef-deleted SIV
    • Serra-Moreno R, Jia B, Breed M, Alvarez X, Evans DT. 2011. Compensatory changes in the cytoplasmic tail of gp41 confer resistance to tetherin/ BST-2 in a pathogenic nef-deleted SIV. Cell Host Microbe 9:46-57. http: //dx.doi.org/10.1016/j.chom.2010.12.005.
    • (2011) Cell Host Microbe , vol.9 , pp. 46-57
    • Serra-Moreno, R.1    Jia, B.2    Breed, M.3    Alvarez, X.4    Evans, D.T.5
  • 22
    • 77953736161 scopus 로고    scopus 로고
    • Ebola virus glycoprotein counteracts BST-2/Tetherin restriction in a sequence-independent manner that does not require tetherin surface removal
    • Lopez LA, Yang SJ, Hauser H, Exline CM, Haworth KG, Oldenburg J, Cannon PM. 2010. Ebola virus glycoprotein counteracts BST-2/Tetherin restriction in a sequence-independent manner that does not require tetherin surface removal. J Virol 84:7243-7255. http://dx.doi.org/10.1128/JVI.02636-09.
    • (2010) J Virol , vol.84 , pp. 7243-7255
    • Lopez, L.A.1    Yang, S.J.2    Hauser, H.3    Exline, C.M.4    Haworth, K.G.5    Oldenburg, J.6    Cannon, P.M.7
  • 23
    • 33644756661 scopus 로고    scopus 로고
    • Recruitment of the adaptor protein 2 complex by the human immunodeficiency virus type 2 envelope protein is necessary for high levels of virus release
    • Noble B, Abada P, Nunez-Iglesias J, Cannon PM. 2006. Recruitment of the adaptor protein 2 complex by the human immunodeficiency virus type 2 envelope protein is necessary for high levels of virus release. J Virol 80:2924-2932. http://dx.doi.org/10.1128/JVI.80.6.2924-2932.2006.
    • (2006) J Virol , vol.80 , pp. 2924-2932
    • Noble, B.1    Abada, P.2    Nunez-Iglesias, J.3    Cannon, P.M.4
  • 24
    • 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, Strebel K. 2003. Naturally occurring amino acid substitutions in the HIV-2 ROD envelope glycoprotein regulate its ability to augment viral particle release. Virology 309:85-98. http://dx.doi.org/10.1016/S0042-6822(02)00128-9.
    • (2003) Virology , vol.309 , pp. 85-98
    • Bour, S.1    Akari, H.2    Miyagi, E.3    Strebel, K.4
  • 25
    • 78049524372 scopus 로고    scopus 로고
    • Potent and broadly reactive HIV-2 neutralizing antibodies elicited by a vaccinia virus vector prime-C2V3C3 polypeptide boost immunization strategy
    • Marcelino JM, Borrego P, Rocha C, Barroso H, Quintas A, Novo C, Taveira N. 2010. Potent and broadly reactive HIV-2 neutralizing antibodies elicited by a vaccinia virus vector prime-C2V3C3 polypeptide boost immunization strategy. J Virol 84:12429-12436. http://dx.doi.org/10.1128/JVI.01102-10.
    • (2010) J Virol , vol.84 , pp. 12429-12436
    • Marcelino, J.M.1    Borrego, P.2    Rocha, C.3    Barroso, H.4    Quintas, A.5    Novo, C.6    Taveira, N.7
  • 27
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797. http://dx.doi.org/10.1093/nar/gkh340.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 28
    • 84890330527 scopus 로고    scopus 로고
    • MEGA6: molecular evolutionary genetics analysis version 6.0
    • Tamura K, Stecher G, Peterson D, Filipski A, Kumar S. 2013. MEGA6: molecular evolutionary genetics analysis version 6.0. Mol Biol Evol 30: 2725-2729. http://dx.doi.org/10.1093/molbev/mst197.
    • (2013) Mol Biol Evol , vol.30 , pp. 2725-2729
    • Tamura, K.1    Stecher, G.2    Peterson, D.3    Filipski, A.4    Kumar, S.5
  • 29
    • 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, Orenstein JM. 1990. The human immunodeficiency virus type 1-specific protein vpu is required for efficient virus maturation and release. J Virol 64:621-629.
    • (1990) J Virol , vol.64 , pp. 621-629
    • Klimkait, T.1    Strebel, K.2    Hoggan, M.D.3    Martin, M.A.4    Orenstein, J.M.5
  • 30
    • 0023930757 scopus 로고
    • In vitro mutagenesis identifies a region within the envelope gene of the human immunodeficiency virus that is critical for infectivity
    • Willey RL, Smith DH, Lasky LA, Theodore TS, Earl PL, Moss B, Capon DJ, Martin MA. 1988. In vitro mutagenesis identifies a region within the envelope gene of the human immunodeficiency virus that is critical for infectivity. J Virol 62:139-147.
    • (1988) J Virol , vol.62 , pp. 139-147
    • Willey, R.L.1    Smith, D.H.2    Lasky, L.A.3    Theodore, T.S.4    Earl, P.L.5    Moss, B.6    Capon, D.J.7    Martin, M.A.8
  • 31
    • 34548392739 scopus 로고    scopus 로고
    • An interferonalpha-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, Bieniasz PD. 2007. An interferonalpha-induced tethering mechanism inhibits HIV-1 and Ebola virus particle release but is counteracted by the HIV-1 Vpu protein. Cell Host Microbe 2:193-203. http://dx.doi.org/10.1016/j.chom.2007.08.001.
    • (2007) Cell Host Microbe , vol.2 , pp. 193-203
    • Neil, S.J.1    Sandrin, V.2    Sundquist, W.I.3    Bieniasz, P.D.4
  • 32
    • 62449325310 scopus 로고    scopus 로고
    • Vpu enhances HIV-1 virus release in the absence of Bst-2 cell surface down-modulation and intracellular depletion
    • Miyagi E, Andrew AJ, Kao S, Strebel K. 2009. Vpu enhances HIV-1 virus release in the absence of Bst-2 cell surface down-modulation and intracellular depletion. Proc Natl Acad Sci U S A 106:2868-2873. http://dx.doi.org/10.1073/pnas.0813223106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2868-2873
    • Miyagi, E.1    Andrew, A.J.2    Kao, S.3    Strebel, K.4
  • 34
    • 84899669327 scopus 로고    scopus 로고
    • HIV-1 Vpu antagonism of tetherin inhibits antibody-dependent cellular cytotoxic responses by natural killer cells
    • Alvarez RA, Hamlin RE, Monroe A, Moldt B, Hotta MT, Rodriguez Caprio G, Fierer DS, Simon V, Chen BK. 2014. HIV-1 Vpu antagonism of tetherin inhibits antibody-dependent cellular cytotoxic responses by natural killer cells. J Virol 88:6031-6046. http://dx.doi.org/10.1128/JVI.00449-14.
    • (2014) J Virol , vol.88 , pp. 6031-6046
    • Alvarez, R.A.1    Hamlin, R.E.2    Monroe, A.3    Moldt, B.4    Hotta, M.T.5    Rodriguez Caprio, G.6    Fierer, D.S.7    Simon, V.8    Chen, B.K.9
  • 36
    • 84894234563 scopus 로고    scopus 로고
    • HIV Nef and Vpu protect HIV-infected CD4+ T cells from antibody-mediated cell lysis through down-modulation of CD4 and BST2
    • Pham TN, Lukhele S, Hajjar F, Routy JP, Cohen EA. 2014. HIV Nef and Vpu protect HIV-infected CD4+ T cells from antibody-mediated cell lysis through down-modulation of CD4 and BST2. Retrovirology 11:15. http: //dx.doi.org/10.1186/1742-4690-11-15.
    • (2014) Retrovirology , vol.11 , pp. 15
    • Pham, T.N.1    Lukhele, S.2    Hajjar, F.3    Routy, J.P.4    Cohen, E.A.5
  • 37
    • 78651486929 scopus 로고    scopus 로고
    • The interferon-inducible host factor bone marrow stromal antigen 2/tetherin restricts virion release, but is it actually a viral restriction factor?
    • Andrew A, Strebel K. 2011. The interferon-inducible host factor bone marrow stromal antigen 2/tetherin restricts virion release, but is it actually a viral restriction factor? J Interferon Cytokine Res 31:137-144. http://dx.doi.org/10.1089/jir.2010.0108.
    • (2011) J Interferon Cytokine Res , vol.31 , pp. 137-144
    • Andrew, A.1    Strebel, K.2
  • 39
    • 84894577734 scopus 로고    scopus 로고
    • Feline immunodeficiency virus envelope glycoproteins antagonize tetherin through a distinctive mechanism that requires virion incorporation
    • Morrison JH, Guevara RB, Marcano AC, Saenz DT, Fadel HJ, Rogstad DK, Poeschla EM. 2014. Feline immunodeficiency virus envelope glycoproteins antagonize tetherin through a distinctive mechanism that requires virion incorporation. J Virol 88:3255-3272. http://dx.doi.org/10.1128/JVI.03814-13.
    • (2014) J Virol , vol.88 , pp. 3255-3272
    • Morrison, J.H.1    Guevara, R.B.2    Marcano, A.C.3    Saenz, D.T.4    Fadel, H.J.5    Rogstad, D.K.6    Poeschla, E.M.7
  • 40
    • 84891705762 scopus 로고    scopus 로고
    • Equine tetherin blocks retrovirus release and its activity is antagonized by equine infectious anemia virus envelope protein
    • Yin X, Hu Z, Gu Q, Wu X, Zheng Y-H, Wei P, Wang X. 2014. Equine tetherin blocks retrovirus release and its activity is antagonized by equine infectious anemia virus envelope protein. J Virol 88:1259-1270. http://dx.doi.org/10.1128/JVI.03148-13.
    • (2014) J Virol , vol.88 , pp. 1259-1270
    • Yin, X.1    Hu, Z.2    Gu, Q.3    Wu, X.4    Zheng, Y.-H.5    Wei, P.6    Wang, X.7
  • 41
    • 80053957184 scopus 로고    scopus 로고
    • Some human immunodeficiency virus type 1 Vpu proteins are able to antagonize macaque BST-2 in vitro and in vivo: Vpu-negative simian-human immunodeficiency viruses are attenuated in vivo
    • Shingai M, Yoshida T, Martin MA, Strebel K. 2011. Some human immunodeficiency virus type 1 Vpu proteins are able to antagonize macaque BST-2 in vitro and in vivo: Vpu-negative simian-human immunodeficiency viruses are attenuated in vivo. J Virol 85:9708-9715. http://dx.doi.org/10.1128/JVI.00626-11.
    • (2011) J Virol , vol.85 , pp. 9708-9715
    • Shingai, M.1    Yoshida, T.2    Martin, M.A.3    Strebel, K.4
  • 42
    • 80053966922 scopus 로고    scopus 로고
    • Identification of residues in the BST-2 TM domain important for antagonism by HIV-1 Vpu using a gain-offunction approach
    • Yoshida T, Kao S, Strebel K. 2011. Identification of residues in the BST-2 TM domain important for antagonism by HIV-1 Vpu using a gain-offunction approach. Front Microbiol 2:1.
    • (2011) Front Microbiol , vol.2 , pp. 1
    • Yoshida, T.1    Kao, S.2    Strebel, K.3
  • 43
    • 78650636704 scopus 로고    scopus 로고
    • Identification of amino acids in the human tetherin transmembrane domain responsible for HIV-1 Vpu interaction and susceptibility
    • Kobayashi T, Ode H, Yoshida T, Sato K, Gee P, Yamamoto SP, Ebina H, Strebel K, Sato H, Koyanagi Y. 2011. Identification of amino acids in the human tetherin transmembrane domain responsible for HIV-1 Vpu interaction and susceptibility. J Virol 85:932-945. http://dx.doi.org/10.1128/JVI.01668-10.
    • (2011) J Virol , vol.85 , pp. 932-945
    • Kobayashi, T.1    Ode, H.2    Yoshida, T.3    Sato, K.4    Gee, P.5    Yamamoto, S.P.6    Ebina, H.7    Strebel, K.8    Sato, H.9    Koyanagi, Y.10
  • 44
    • 67249100279 scopus 로고    scopus 로고
    • Mutation of a single residue renders human tetherin resistant to HIV-1 Vpu-mediated depletion
    • Gupta RK, Hue S, Schaller T, Verschoor E, Pillay D, Towers GJ. 2009. Mutation of a single residue renders human tetherin resistant to HIV-1 Vpu-mediated depletion. PLoS Pathog 5:e1000443. http://dx.doi.org/10.1371/journal.ppat.1000443.
    • (2009) PLoS Pathog , vol.5
    • Gupta, R.K.1    Hue, S.2    Schaller, T.3    Verschoor, E.4    Pillay, D.5    Towers, G.J.6
  • 46
    • 71749086904 scopus 로고    scopus 로고
    • HIV-1 accessory protein Vpu internalizes cellsurface BST-2/tetherin through transmembrane interactions leading to lysosomes
    • Iwabu Y, Fujita H, Kinomoto M, Kaneko K, Ishizaka Y, Tanaka Y, Sata T, Tokunaga K. 2009. HIV-1 accessory protein Vpu internalizes cellsurface BST-2/tetherin through transmembrane interactions leading to lysosomes. J Biol Chem 284:35060-35072. http://dx.doi.org/10.1074/jbc.M109.058305.
    • (2009) J Biol Chem , vol.284 , pp. 35060-35072
    • Iwabu, Y.1    Fujita, H.2    Kinomoto, M.3    Kaneko, K.4    Ishizaka, Y.5    Tanaka, Y.6    Sata, T.7    Tokunaga, K.8
  • 47
    • 84855272482 scopus 로고    scopus 로고
    • HIV-1 Vpu protein antagonizes innate restriction factor BST-2 via lipid-embedded helix-helix interactions
    • Skasko M, Wang Y, Tian Y, Tokarev A, Munguia J, Ruiz A, Stephens EB, Opella SJ, Guatelli J. 2012. HIV-1 Vpu protein antagonizes innate restriction factor BST-2 via lipid-embedded helix-helix interactions. J Biol Chem 287:58-67. http://dx.doi.org/10.1074/jbc.M111.296772.
    • (2012) J Biol Chem , vol.287 , pp. 58-67
    • Skasko, M.1    Wang, Y.2    Tian, Y.3    Tokarev, A.4    Munguia, J.5    Ruiz, A.6    Stephens, E.B.7    Opella, S.J.8    Guatelli, J.9
  • 48
    • 84899819636 scopus 로고    scopus 로고
    • Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1
    • Jia X, Weber E, Tokarev A, Lewinski M, Rizk M, Suarez M, Guatelli J, Xiong Y. 2014. Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1. eLife 3:e02362.
    • (2014) ELife , vol.3
    • Jia, X.1    Weber, E.2    Tokarev, A.3    Lewinski, M.4    Rizk, M.5    Suarez, M.6    Guatelli, J.7    Xiong, Y.8
  • 49
    • 84861209115 scopus 로고    scopus 로고
    • A cytoplasmic tail determinant in HIV-1 Vpu mediates targeting of tetherin for endosomal degradation and counteracts interferon-induced restriction
    • Kueck T, Neil SJD. 2012. A cytoplasmic tail determinant in HIV-1 Vpu mediates targeting of tetherin for endosomal degradation and counteracts interferon-induced restriction. PLoS Pathog 8:e1002609. http://dx.doi.org/10.1371/journal.ppat.1002609.
    • (2012) PLoS Pathog , vol.8
    • Kueck, T.1    Neil, S.J.D.2
  • 50
    • 80054000378 scopus 로고    scopus 로고
    • Role of the endocytic pathway in the counteraction of BST-2 by human lentiviral pathogens
    • Lau D, Kwan W, Guatelli J. 2011. Role of the endocytic pathway in the counteraction of BST-2 by human lentiviral pathogens. J Virol 85:9834-9846 http://dx.doi.org/10.1128/JVI.02633-10.
    • (2011) J Virol , vol.85 , pp. 9834-9846
    • Lau, D.1    Kwan, W.2    Guatelli, J.3
  • 52
    • 47749137744 scopus 로고    scopus 로고
    • Requirements of the membrane proximal tyrosine and dileucine-based sorting signals for efficient transport of the subtype C Vpu protein to the plasma membrane and in virus release
    • Ruiz A, Hill MS, Schmitt K, Guatelli J, Stephens EB. 2008. Requirements of the membrane proximal tyrosine and dileucine-based sorting signals for efficient transport of the subtype C Vpu protein to the plasma membrane and in virus release. Virology 378:58-68. http://dx.doi.org/10.1016/j.virol.2008.05.022.
    • (2008) Virology , vol.378 , pp. 58-68
    • Ruiz, A.1    Hill, M.S.2    Schmitt, K.3    Guatelli, J.4    Stephens, E.B.5
  • 53
    • 84899670501 scopus 로고    scopus 로고
    • Counteraction of the multifunctional restriction factor tetherin
    • Sauter D. 2014. Counteraction of the multifunctional restriction factor tetherin. Front Microbiol 5:163.
    • (2014) Front Microbiol , vol.5 , pp. 163
    • Sauter, D.1
  • 54
    • 80655146209 scopus 로고    scopus 로고
    • Antibodymediated enhancement of HIV-1 and HIV-2 production from BST-2/ tetherin+ cells
    • Miyagi E, Andrew A, Kao S, Yoshida T, Strebel K. 2011. Antibodymediated enhancement of HIV-1 and HIV-2 production from BST-2/ tetherin+ cells. J Virol 85:11981-11994. http://dx.doi.org/10.1128/JVI.05176-11.
    • (2011) J Virol , vol.85 , pp. 11981-11994
    • Miyagi, E.1    Andrew, A.2    Kao, S.3    Yoshida, T.4    Strebel, K.5
  • 55
    • 0026785547 scopus 로고
    • Identification and characterization of fusion and processing domains of the human immunodeficiency virus type 2 envelope glycoprotein
    • Freed EO, Myers DJ. 1992. Identification and characterization of fusion and processing domains of the human immunodeficiency virus type 2 envelope glycoprotein. J Virol 66:5472-5478.
    • (1992) J Virol , vol.66 , pp. 5472-5478
    • Freed, E.O.1    Myers, D.J.2


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