메뉴 건너뛰기




Volumn 54, Issue 2, 2013, Pages 132-139

BST-2/tetherin: Structural biology, viral antagonism, and immunobiology of a potent host antiviral factor

Author keywords

Antiviral state; Innate immunity; Interferon; Plasmacytoid dendritic cells; Tetherin; Virology

Indexed keywords

PEPTIDES AND PROTEINS; PROTEIN BST2; UNCLASSIFIED DRUG;

EID: 84871648210     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2012.11.008     Document Type: Review
Times cited : (54)

References (89)
  • 1
    • 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 A.J., Miyagi E., Kao S., 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, 6:80.
    • (2009) Retrovirology , vol.6 , pp. 80
    • Andrew, A.J.1    Miyagi, E.2    Kao, S.3    Strebel, K.4
  • 3
    • 84861324358 scopus 로고    scopus 로고
    • Virus-activated interferon regulatory factor 7 upregulates expression of the interferon-regulated BST2 gene independently of interferon signaling
    • Bego M.G., Mercier J., Cohen E.A. Virus-activated interferon regulatory factor 7 upregulates expression of the interferon-regulated BST2 gene independently of interferon signaling. Journal of Virology 2012, 86:3513-3527.
    • (2012) Journal of Virology , vol.86 , pp. 3513-3527
    • Bego, M.G.1    Mercier, J.2    Cohen, E.A.3
  • 4
    • 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 A.L., Giurisato E., Cella M., Schreiber R.D., Shaw A.S., Colonna M. 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. Journal of Immunology 2006, 177:3260-3265.
    • (2006) Journal of Immunology , vol.177 , pp. 3260-3265
    • Blasius, A.L.1    Giurisato, E.2    Cella, M.3    Schreiber, R.D.4    Shaw, A.S.5    Colonna, M.6
  • 6
    • 65449186712 scopus 로고    scopus 로고
    • Up-regulation of bone marrow stromal protein 2 (BST2) in breast cancer with bone metastasis
    • Cai D., Cao J., Li Z., Zheng X., Yao Y., Li W., Yuan Z. Up-regulation of bone marrow stromal protein 2 (BST2) in breast cancer with bone metastasis. BMC Cancer 2009, 9:102.
    • (2009) BMC Cancer , vol.9 , pp. 102
    • Cai, D.1    Cao, J.2    Li, Z.3    Zheng, X.4    Yao, Y.5    Li, W.6    Yuan, Z.7
  • 9
    • 84862871440 scopus 로고    scopus 로고
    • Dimerization of the transmembrane domain of human tetherin in membrane mimetic environments
    • Cole G., Simonetti K., Ademi I., Sharpe S. Dimerization of the transmembrane domain of human tetherin in membrane mimetic environments. Biochemistry 2012, 51:5033-5040.
    • (2012) Biochemistry , vol.51 , pp. 5033-5040
    • Cole, G.1    Simonetti, K.2    Ademi, I.3    Sharpe, S.4
  • 12
    • 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 J.L., Viswanathan K., McCarroll M.N., Gustin J.K., Fruh K., Moses A.V. Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a {beta}TrCP-dependent mechanism. Journal of Virology 2009, 83:7931-7947.
    • (2009) Journal of Virology , vol.83 , pp. 7931-7947
    • Douglas, J.L.1    Viswanathan, K.2    McCarroll, M.N.3    Gustin, J.K.4    Fruh, K.5    Moses, A.V.6
  • 13
    • 78650373530 scopus 로고    scopus 로고
    • Modulation of HIV-1-host interaction: role of the Vpu accessory protein
    • Dube M., Bego M.G., Paquay C., Cohen E.A. Modulation of HIV-1-host interaction: role of the Vpu accessory protein. Retrovirology 2010, 7:114.
    • (2010) Retrovirology , vol.7 , pp. 114
    • Dube, M.1    Bego, M.G.2    Paquay, C.3    Cohen, E.A.4
  • 15
    • 77956188831 scopus 로고    scopus 로고
    • BST-2/tetherin: a new component of the innate immune response to enveloped viruses
    • Evans D.T., Serra-Moreno R., Singh R.K., Guatelli J.C. BST-2/tetherin: a new component of the innate immune response to enveloped viruses. Trends in Microbiology 2010, 18:388-396.
    • (2010) Trends in Microbiology , vol.18 , pp. 388-396
    • Evans, D.T.1    Serra-Moreno, R.2    Singh, R.K.3    Guatelli, J.C.4
  • 16
    • 77950424913 scopus 로고    scopus 로고
    • Direct restriction of virus release and incorporation of the interferon-induced protein BST-2 into HIV-1 particles
    • Fitzpatrick K., Skasko M., Deerinck T.J., Crum J., Ellisman M.H., Guatelli J. Direct restriction of virus release and incorporation of the interferon-induced protein BST-2 into HIV-1 particles. PLoS Pathogens 2010, 6:e1000701.
    • (2010) PLoS Pathogens , vol.6
    • Fitzpatrick, K.1    Skasko, M.2    Deerinck, T.J.3    Crum, J.4    Ellisman, M.H.5    Guatelli, J.6
  • 17
    • 64249110493 scopus 로고    scopus 로고
    • The BAR domain superfamily: membrane-molding macromolecules
    • Frost A., Unger V.M., De Camilli P. The BAR domain superfamily: membrane-molding macromolecules. Cell 2009, 137:191-196.
    • (2009) Cell , vol.137 , pp. 191-196
    • Frost, A.1    Unger, V.M.2    De Camilli, P.3
  • 18
    • 84869194198 scopus 로고    scopus 로고
    • Innate Sensing of HIV-1 Assembly by Tetherin Induces NFkappaB-Dependent Proinflammatory Responses
    • Galao R.P., Le Tortorec A., Pickering S., Kueck T., Neil S.J. Innate Sensing of HIV-1 Assembly by Tetherin Induces NFkappaB-Dependent Proinflammatory Responses. Cell Host & Microbe 2012, 12:633-644.
    • (2012) Cell Host & Microbe , vol.12 , pp. 633-644
    • Galao, R.P.1    Le Tortorec, A.2    Pickering, S.3    Kueck, T.4    Neil, S.J.5
  • 19
    • 48749085127 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells: sensing nucleic acids in viral infection and autoimmune diseases
    • Gilliet M., Cao W., Liu Y.J. Plasmacytoid dendritic cells: sensing nucleic acids in viral infection and autoimmune diseases. Nature Reviews Immunology 2008, 8:594-606.
    • (2008) Nature Reviews Immunology , vol.8 , pp. 594-606
    • Gilliet, M.1    Cao, W.2    Liu, Y.J.3
  • 21
    • 0028101333 scopus 로고
    • A novel membrane antigen selectively expressed on terminally differentiated human B cells
    • Goto T., Kennel S.J., Abe M., Takishita M., Kosaka M., Solomon A., Saito S. A novel membrane antigen selectively expressed on terminally differentiated human B cells. Blood 1994, 84:1922-1930.
    • (1994) Blood , vol.84 , pp. 1922-1930
    • Goto, T.1    Kennel, S.J.2    Abe, M.3    Takishita, M.4    Kosaka, M.5    Solomon, A.6    Saito, S.7
  • 22
    • 67249100279 scopus 로고    scopus 로고
    • Mutation of a single residue renders human tetherin resistant to HIV-1 Vpu-mediated depletion
    • Gupta R.K., Hue S., Schaller T., Verschoor E., Pillay D., Towers G.J. Mutation of a single residue renders human tetherin resistant to HIV-1 Vpu-mediated depletion. PLoS Pathogens 2009, 5:e1000443.
    • (2009) PLoS Pathogens , vol.5
    • Gupta, R.K.1    Hue, S.2    Schaller, T.3    Verschoor, E.4    Pillay, D.5    Towers, G.J.6
  • 24
    • 84863116365 scopus 로고    scopus 로고
    • The tetherin/BST-2 coiled-coil ectodomain mediates plasma membrane microdomain localization and restriction of particle release
    • Hammonds J., Ding L., Chu H., Geller K., Robbins A., Wang J.J., Yi H., Spearman P. The tetherin/BST-2 coiled-coil ectodomain mediates plasma membrane microdomain localization and restriction of particle release. Journal of Virology 2012, 86:2259-2272.
    • (2012) Journal of Virology , vol.86 , pp. 2259-2272
    • Hammonds, J.1    Ding, L.2    Chu, H.3    Geller, K.4    Robbins, A.5    Wang, J.J.6    Yi, H.7    Spearman, P.8
  • 25
    • 77649251047 scopus 로고    scopus 로고
    • Immunoelectron microscopic evidence for tetherin/BST2 as the physical bridge between HIV-1 virions and the plasma membrane
    • Hammonds J., Wang J.J., Yi H., Spearman P. Immunoelectron microscopic evidence for tetherin/BST2 as the physical bridge between HIV-1 virions and the plasma membrane. PLoS Pathogens 2010, 6:e1000749.
    • (2010) PLoS Pathogens , vol.6
    • Hammonds, J.1    Wang, J.J.2    Yi, H.3    Spearman, P.4
  • 28
    • 20244374809 scopus 로고
    • Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth
    • Ishikawa J., Kaisho T., Tomizawa H., Lee B.O., Kobune Y., Inazawa J., Oritani K., Itoh M., Ochi T., Ishihara K., et al. Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth. Genomics 1995, 26:527-534.
    • (1995) Genomics , vol.26 , pp. 527-534
    • Ishikawa, J.1    Kaisho, T.2    Tomizawa, H.3    Lee, B.O.4    Kobune, Y.5    Inazawa, J.6    Oritani, K.7    Itoh, M.8    Ochi, T.9    Ishihara, K.10
  • 31
    • 84856154164 scopus 로고    scopus 로고
    • Bone marrow stromal cell antigen 2 (BST-2) restricts mouse mammary tumor virus (MMTV) replication in vivo
    • Jones P.H., Mehta H.V., Maric M., Roller R.J., Okeoma C.M. Bone marrow stromal cell antigen 2 (BST-2) restricts mouse mammary tumor virus (MMTV) replication in vivo. Retrovirology 2012, 9:10.
    • (2012) Retrovirology , vol.9 , pp. 10
    • Jones, P.H.1    Mehta, H.V.2    Maric, M.3    Roller, R.J.4    Okeoma, C.M.5
  • 34
    • 0037407691 scopus 로고    scopus 로고
    • Activation with CpG-A and CpG-B oligonucleotides reveals two distinct regulatory pathways of type I IFN synthesis in human plasmacytoid dendritic cells
    • Kerkmann M., Rothenfusser S., Hornung V., Towarowski A., Wagner M., Sarris A., Giese T., Endres S., Hartmann G. Activation with CpG-A and CpG-B oligonucleotides reveals two distinct regulatory pathways of type I IFN synthesis in human plasmacytoid dendritic cells. Journal of Immunology 2003, 170:4465-4474.
    • (2003) Journal of Immunology , vol.170 , pp. 4465-4474
    • Kerkmann, M.1    Rothenfusser, S.2    Hornung, V.3    Towarowski, A.4    Wagner, M.5    Sarris, A.6    Giese, T.7    Endres, S.8    Hartmann, G.9
  • 36
    • 84867673691 scopus 로고    scopus 로고
    • Inhibition of virus-like particle release of Sendai virus and Nipah virus, but not that of mumps virus, by tetherin/CD317/BST-2
    • Kong W.S., Irie T., Yoshida A., Kawabata R., Kadoi T., Sakaguchi T. Inhibition of virus-like particle release of Sendai virus and Nipah virus, but not that of mumps virus, by tetherin/CD317/BST-2. Hiroshima Journal of Medical Sciences 2012, 61:59-67.
    • (2012) Hiroshima Journal of Medical Sciences , vol.61 , pp. 59-67
    • Kong, W.S.1    Irie, T.2    Yoshida, A.3    Kawabata, R.4    Kadoi, T.5    Sakaguchi, T.6
  • 38
    • 64249132028 scopus 로고    scopus 로고
    • Cutting edge: TLR-dependent viral recognition along with type I IFN positive feedback signaling masks the requirement of viral replication for IFN-{alpha} production in plasmacytoid dendritic cells
    • Kumagai Y., Kumar H., Koyama S., Kawai T., Takeuchi O., Akira S. Cutting edge: TLR-dependent viral recognition along with type I IFN positive feedback signaling masks the requirement of viral replication for IFN-{alpha} production in plasmacytoid dendritic cells. Journal of Immunology 2009, 182:3960-3964.
    • (2009) Journal of Immunology , vol.182 , pp. 3960-3964
    • Kumagai, Y.1    Kumar, H.2    Koyama, S.3    Kawai, T.4    Takeuchi, O.5    Akira, S.6
  • 39
    • 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., Sugden A., Wilde A., Banting G. Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology. Traffic 2003, 4:694-709.
    • (2003) Traffic , vol.4 , pp. 694-709
    • Kupzig, S.1    Korolchuk, V.2    Rollason, R.3    Sugden, A.4    Wilde, A.5    Banting, G.6
  • 40
    • 84855333779 scopus 로고    scopus 로고
    • How SAMHD1 changes our view of viral restriction
    • Laguette N., Benkirane M. How SAMHD1 changes our view of viral restriction. Trends in Immunology 2012, 33:26-33.
    • (2012) Trends in Immunology , vol.33 , pp. 26-33
    • Laguette, N.1    Benkirane, M.2
  • 41
    • 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 S.J. Antagonism to and intracellular sequestration of human tetherin by the human immunodeficiency virus type 2 envelope glycoprotein. Journal of Virology 2009, 83:11966-11978.
    • (2009) Journal of Virology , vol.83 , pp. 11966-11978
    • Le Tortorec, A.1    Neil, S.J.2
  • 43
    • 70350278891 scopus 로고    scopus 로고
    • Simian immunodeficiency virus SIVagm from African green monkeys does not antagonize endogenous levels of African green monkey tetherin/BST-2
    • Lim E.S., Emerman M. Simian immunodeficiency virus SIVagm from African green monkeys does not antagonize endogenous levels of African green monkey tetherin/BST-2. Journal of Virology 2009, 83:11673-11681.
    • (2009) Journal of Virology , vol.83 , pp. 11673-11681
    • Lim, E.S.1    Emerman, M.2
  • 45
    • 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 L.A., Yang S.J., Hauser H., Exline C.M., Haworth K.G., Oldenburg J., Cannon P.M. Ebola virus glycoprotein counteracts BST-2/Tetherin restriction in a sequence-independent manner that does not require tetherin surface removal. Journal of Virology 2010, 84:7243-7255.
    • (2010) Journal of Virology , 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
  • 50
    • 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 J.L., Hines J., Gustin J., Moses A.V., Fruh K. Molecular mechanism of BST2/tetherin downregulation by K5/MIR2 of Kaposi's sarcoma-associated herpesvirus. Journal of Virology 2009, 83:9672-9681.
    • (2009) Journal of Virology , vol.83 , pp. 9672-9681
    • Mansouri, M.1    Viswanathan, K.2    Douglas, J.L.3    Hines, J.4    Gustin, J.5    Moses, A.V.6    Fruh, K.7
  • 55
    • 70249085585 scopus 로고    scopus 로고
    • Stromal cell contributions to the homeostasis and functionality of the immune system
    • Mueller S.N., Germain R.N. Stromal cell contributions to the homeostasis and functionality of the immune system. Nature Reviews Immunology 2009, 9:618-629.
    • (2009) Nature Reviews Immunology , vol.9 , pp. 618-629
    • Mueller, S.N.1    Germain, R.N.2
  • 57
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil S.J., Zang T., Bieniasz P.D. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 2008, 451:425-430.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.1    Zang, T.2    Bieniasz, P.D.3
  • 59
    • 77954043624 scopus 로고    scopus 로고
    • The RING-CH ligase K5 antagonizes restriction of KSHV and HIV-1 particle release by mediating ubiquitin-dependent endosomal degradation of tetherin
    • Pardieu C., Vigan R., Wilson S.J., Calvi A., Zang T., Bieniasz P., Kellam P., Towers G.J., Neil S.J. The RING-CH ligase K5 antagonizes restriction of KSHV and HIV-1 particle release by mediating ubiquitin-dependent endosomal degradation of tetherin. PLoS Pathogens 2010, 6:e1000843.
    • (2010) PLoS Pathogens , vol.6
    • Pardieu, C.1    Vigan, R.2    Wilson, S.J.3    Calvi, A.4    Zang, T.5    Bieniasz, P.6    Kellam, P.7    Towers, G.J.8    Neil, S.J.9
  • 62
    • 84861655716 scopus 로고    scopus 로고
    • Stromal cells put the brakes on T-cell responses
    • Randall T.D. Stromal cells put the brakes on T-cell responses. Immunology and Cell Biology 2012, 90:469-470.
    • (2012) Immunology and Cell Biology , vol.90 , pp. 469-470
    • Randall, T.D.1
  • 64
    • 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., Banting G. Clathrin-mediated endocytosis of a lipid-raft-associated protein is mediated through a dual tyrosine motif. Journal of Cell Science 2007, 120:3850-3858.
    • (2007) Journal of Cell Science , vol.120 , pp. 3850-3858
    • Rollason, R.1    Korolchuk, V.2    Hamilton, C.3    Schu, P.4    Banting, G.5
  • 67
    • 77951898650 scopus 로고    scopus 로고
    • Tetherin: holding on and letting go
    • Sauter D., Specht A., Kirchhoff F. Tetherin: holding on and letting go. Cell 2010, 141:392-398.
    • (2010) Cell , vol.141 , pp. 392-398
    • Sauter, D.1    Specht, A.2    Kirchhoff, F.3
  • 68
    • 77449133186 scopus 로고    scopus 로고
    • In vivo biotinylation of the vasculature in B-cell lymphoma identifies BST-2 as a target for antibody-based therapy
    • Schliemann C., Roesli C., Kamada H., Borgia B., Fugmann T., Klapper W., Neri D. In vivo biotinylation of the vasculature in B-cell lymphoma identifies BST-2 as a target for antibody-based therapy. Blood 2010, 115:736-744.
    • (2010) Blood , vol.115 , pp. 736-744
    • Schliemann, C.1    Roesli, C.2    Kamada, H.3    Borgia, B.4    Fugmann, T.5    Klapper, W.6    Neri, D.7
  • 70
    • 83655192651 scopus 로고    scopus 로고
    • Viperin: a multifunctional, interferon-inducible protein that regulates virus replication
    • Seo J.Y., Yaneva R., Cresswell P. Viperin: a multifunctional, interferon-inducible protein that regulates virus replication. Cell Host & Microbe 2011, 10:534-539.
    • (2011) Cell Host & Microbe , vol.10 , pp. 534-539
    • Seo, J.Y.1    Yaneva, R.2    Cresswell, P.3
  • 71
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy A.M., Gaddis N.C., Choi J.D., Malim M.H. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 2002, 418:646-650.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 73
    • 77957785465 scopus 로고    scopus 로고
    • Emerging role of ISG15 in antiviral immunity
    • Skaug B., Chen Z.J. Emerging role of ISG15 in antiviral immunity. Cell 2010, 143:187-190.
    • (2010) Cell , vol.143 , pp. 187-190
    • Skaug, B.1    Chen, Z.J.2
  • 74
    • 78951496038 scopus 로고    scopus 로고
    • Structural and biophysical analysis of BST-2/tetherin ectodomains reveals an evolutionary conserved design to inhibit virus release
    • Swiecki M., Scheaffer S.M., Allaire M., Fremont D.H., Colonna M., Brett T.J. Structural and biophysical analysis of BST-2/tetherin ectodomains reveals an evolutionary conserved design to inhibit virus release. Journal of Biological Chemistry 2011, 286:2987-2997.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 2987-2997
    • Swiecki, M.1    Scheaffer, S.M.2    Allaire, M.3    Fremont, D.H.4    Colonna, M.5    Brett, T.J.6
  • 75
    • 84863268937 scopus 로고    scopus 로고
    • Cutting edge: paradoxical roles of BST2/tetherin in promoting type I IFN response and viral infection
    • Swiecki M., Wang Y., Gilfillan S., Lenschow D.J., Colonna M. Cutting edge: paradoxical roles of BST2/tetherin in promoting type I IFN response and viral infection. Journal of Immunology 2012, 188:2488-2492.
    • (2012) Journal of Immunology , vol.188 , pp. 2488-2492
    • Swiecki, M.1    Wang, Y.2    Gilfillan, S.3    Lenschow, D.J.4    Colonna, M.5
  • 76
    • 84863251086 scopus 로고    scopus 로고
    • Potent in vitro and in vivo activity of an Fc-engineered humanized anti-HM1.24 antibody against multiple myeloma via augmented effector function
    • Tai Y.T., Horton H.M., Kong S.Y., Pong E., Chen H., Cemerski S., Bernett M.J., Nguyen D.H., Karki S., Chu S.Y., et al. Potent in vitro and in vivo activity of an Fc-engineered humanized anti-HM1.24 antibody against multiple myeloma via augmented effector function. Blood 2012, 119:2074-2082.
    • (2012) Blood , vol.119 , pp. 2074-2082
    • Tai, Y.T.1    Horton, H.M.2    Kong, S.Y.3    Pong, E.4    Chen, H.5    Cemerski, S.6    Bernett, M.J.7    Nguyen, D.H.8    Karki, S.9    Chu, S.Y.10
  • 78
    • 78649401965 scopus 로고    scopus 로고
    • Determinants of tetherin antagonism in the transmembrane domain of the human immunodeficiency virus type 1 Vpu protein
    • Vigan R., Neil S.J. Determinants of tetherin antagonism in the transmembrane domain of the human immunodeficiency virus type 1 Vpu protein. Journal of Virology 2010, 84:12958-12970.
    • (2010) Journal of Virology , vol.84 , pp. 12958-12970
    • Vigan, R.1    Neil, S.J.2
  • 82
    • 80054992566 scopus 로고    scopus 로고
    • Influenza virus is not restricted by tetherin whereas influenza VLP production is restricted by tetherin
    • Watanabe R., Leser G.P., Lamb R.A. Influenza virus is not restricted by tetherin whereas influenza VLP production is restricted by tetherin. Virology 2011, 417:50-56.
    • (2011) Virology , vol.417 , pp. 50-56
    • Watanabe, R.1    Leser, G.P.2    Lamb, R.A.3
  • 83
    • 78649404289 scopus 로고    scopus 로고
    • Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms
    • Weidner J.M., Jiang D., Pan X.B., Chang J., Block T.M., Guo J.T. Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms. Journal of Virology 2010, 84:12646-12657.
    • (2010) Journal of Virology , vol.84 , pp. 12646-12657
    • Weidner, J.M.1    Jiang, D.2    Pan, X.B.3    Chang, J.4    Block, T.M.5    Guo, J.T.6
  • 88
    • 78651104411 scopus 로고    scopus 로고
    • IFN-gamma-induced BST2 mediates monocyte adhesion to human endothelial cells
    • Yoo H., Park S.H., Ye S.K., Kim M. IFN-gamma-induced BST2 mediates monocyte adhesion to human endothelial cells. Cellular Immunology 2011, 267:23-29.
    • (2011) Cellular Immunology , vol.267 , pp. 23-29
    • Yoo, H.1    Park, S.H.2    Ye, S.K.3    Kim, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.