메뉴 건너뛰기




Volumn 91, Issue 6, 2017, Pages

Efficient Vpu-mediated tetherin antagonism by an HIV-1 group O strain

Author keywords

Antagonism; HIV 1 group O; Tetherin; Vpu

Indexed keywords

ALPHA INTERFERON; CD4 ANTIGEN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON; NEF PROTEIN; TETHERIN; UNCLASSIFIED DRUG; VPU PROTEIN; BST2 PROTEIN, HUMAN; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEIN; LEUKOCYTE ANTIGEN; VIRAL PROTEIN; VPU PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 85014109948     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02177-16     Document Type: Article
Times cited : (15)

References (86)
  • 4
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5+ restricts HIV-1 infection in Old World monkeys
    • Stremlau M, Owens CM, Perron MJ. 2004. The cytoplasmic body component TRIM5+ restricts HIV-1 infection in Old World monkeys. Nature 427.
    • (2004) Nature , pp. 427
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3
  • 5
    • 14544281087 scopus 로고    scopus 로고
    • Positive selection of primate TRIM5 alpha identifies a critical species-specific retroviral restriction domain
    • Sawyer SL, Wu LI, Emerman M, Malik HS. 2005. Positive selection of primate TRIM5 alpha identifies a critical species-specific retroviral restriction domain. Proc Natl Acad Sci U S A 102:2832-2837. https://doi.org/10.1073/pnas.0409853102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2832-2837
    • Sawyer, S.L.1    Wu, L.I.2    Emerman, M.3    Malik, H.S.4
  • 6
    • 13944259674 scopus 로고    scopus 로고
    • Species-specific variation in the B30.2(SPRY) domain of TRIM5 alpha determines the potency of human immunodeficiency virus restriction
    • Stremlau M, Perron M, Welikala S, Sodroski J. 2005. Species-specific variation in the B30.2(SPRY) domain of TRIM5 alpha determines the potency of human immunodeficiency virus restriction. J Virol 79: 3139-3145. https://doi.org/10.1128/JVI.79.5.3139-3145.2005.
    • (2005) J Virol , vol.79 , pp. 3139-3145
    • Stremlau, M.1    Perron, M.2    Welikala, S.3    Sodroski, J.4
  • 8
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy AM, Gaddis NC, Choi JD, Malim MH. 2002. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418:646-650. https://doi.org/10.1038/nature00939.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 10
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat B, Turelli P, Caron G, Friedli M. 2003. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424:99-103. https://doi.org/10.1038/nature01709.
    • (2003) Nature , vol.424 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4
  • 11
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang H, Yang B, Pomerantz RJ, Zhang C, Arunachalam SC, Gao L. 2003. The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424:94-98. https://doi.org/10.1038/nature 01707.
    • (2003) Nature , vol.424 , pp. 94-98
    • Zhang, H.1    Yang, B.2    Pomerantz, R.J.3    Zhang, C.4    Arunachalam, S.C.5    Gao, L.6
  • 13
    • 84879759758 scopus 로고    scopus 로고
    • Non-M variants of human immunodeficiency virus type 1
    • Mourez T, Simon F, Plantier J-C. 2013. Non-M variants of human immunodeficiency virus type 1. Clin Microbiol Rev 26:448-461. https://doi.org/10.1128/CMR.00012-13.
    • (2013) Clin Microbiol Rev , vol.26 , pp. 448-461
    • Mourez, T.1    Simon, F.2    Plantier, J.-C.3
  • 16
    • 77951898650 scopus 로고    scopus 로고
    • Tetherin: holding on and letting go
    • Sauter D, Specht A, Kirchhoff F. 2010. Tetherin: holding on and letting go. Cell 141:392-398. https://doi.org/10.1016/j.cell.2010.04.022.
    • (2010) Cell , vol.141 , pp. 392-398
    • Sauter, D.1    Specht, A.2    Kirchhoff, F.3
  • 18
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil SJD, Zang T, Bieniasz PD. 2008. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451:425-430. https://doi.org/10.1038/nature06553.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.D.1    Zang, T.2    Bieniasz, P.D.3
  • 19
    • 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. https://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
  • 21
    • 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. 2003. Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology. Traffic 4:694-709. https://doi.org/10.1034/j.1600-0854.2003.00129.x.
    • (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
  • 22
    • 81055145390 scopus 로고    scopus 로고
    • Tetherin is a key effector of the antiretroviral activity of type I interferon in vitro and in vivo
    • Liberatore RA, Bieniasz PD. 2011. Tetherin is a key effector of the antiretroviral activity of type I interferon in vitro and in vivo. Proc Natl Acad Sci U S A 108:18097-18101. https://doi.org/10.1073/pnas.1113694108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 18097-18101
    • Liberatore, R.A.1    Bieniasz, P.D.2
  • 23
    • 84887041456 scopus 로고    scopus 로고
    • Efficient BST2 antagonism by Vpu is critical for early HIV-1 dissemination in humanized mice
    • Dave VP, Hajjar F, Dieng MM, Haddad é, Cohen éA. 2013. Efficient BST2 antagonism by Vpu is critical for early HIV-1 dissemination in humanized mice. Retrovirology 10:128. https://doi.org/10.1186/1742-4690-10-128.
    • (2013) Retrovirology , vol.10 , pp. 128
    • Dave, V.P.1    Hajjar, F.2    Dieng, M.M.3    Haddad, É.4    Cohen, É.A.5
  • 24
    • 84963548976 scopus 로고    scopus 로고
    • Quantifying the effect of Vpu on the promotion of HIV-1 replication in the humanized mouse model
    • Ikeda H, Nakaoka S, de Boer RJ, Morita S, Misawa N, Koyanagi Y. 2016. Quantifying the effect of Vpu on the promotion of HIV-1 replication in the humanized mouse model. Retrovirology 13:23. https://doi.org/10.1186/s12977-016-0252-2.
    • (2016) Retrovirology , vol.13 , pp. 23
    • Ikeda, H.1    Nakaoka, S.2    de Boer, R.J.3    Morita, S.4    Misawa, N.5    Koyanagi, Y.6
  • 25
    • 84986556429 scopus 로고    scopus 로고
    • Vpumediated counteraction of tetherin is a major determinant of HIV-1 interferon resistance
    • Kmiec D, Iyer SS, Stürzel CM, Sauter D, Hahn BH, Kirchhoff F. 2016. Vpumediated counteraction of tetherin is a major determinant of HIV-1 interferon resistance. mBio 7:e00934-16. https://doi.org/10.1128/mBio.00934-16.
    • (2016) mBio , vol.7
    • Kmiec, D.1    Iyer, S.S.2    Stürzel, C.M.3    Sauter, D.4    Hahn, B.H.5    Kirchhoff, F.6
  • 26
    • 80054698971 scopus 로고    scopus 로고
    • Ancient origin of a deletion in human BST2/tetherin that confers protection against viral zoonoses
    • Sauter D, Vogl M, Kirchhoff F. 2011. Ancient origin of a deletion in human BST2/tetherin that confers protection against viral zoonoses. Hum Mutat 32:1243-1245. https://doi.org/10.1002/humu.21571.
    • (2011) Hum Mutat , vol.32 , pp. 1243-1245
    • Sauter, D.1    Vogl, M.2    Kirchhoff, F.3
  • 33
    • 81255143057 scopus 로고    scopus 로고
    • Analysis of the human immunodeficiency virus type 1 M group Vpu domains involved in antagonizing tetherin
    • Petit SJ, Blondeau C, Towers GJ. 2011. Analysis of the human immunodeficiency virus type 1 M group Vpu domains involved in antagonizing tetherin. J Gen Virol 92:2937-2948. https://doi.org/10.1099/vir.0.035931-0.
    • (2011) J Gen Virol , vol.92 , pp. 2937-2948
    • Petit, S.J.1    Blondeau, C.2    Towers, G.J.3
  • 34
    • 80053982162 scopus 로고    scopus 로고
    • Separable determinants of subcellular localization and interaction account for the inability of group O HIV-1 Vpu to counteract tetherin
    • Vigan R, Neil SJD. 2011. Separable determinants of subcellular localization and interaction account for the inability of group O HIV-1 Vpu to counteract tetherin. J Virol 85:9737-9748. https://doi.org/10.1128/JVI.00479-11.
    • (2011) J Virol , vol.85 , pp. 9737-9748
    • Vigan, R.1    Neil, S.J.D.2
  • 38
    • 0032865615 scopus 로고    scopus 로고
    • Characterization of a highly replicative intergroup M/O human immunodeficiency virus type 1 recombinant isolated from a Cameroonian patient
    • Peeters M, Liegeois F, Torimiro N, Bourgeois A, Mpoudi E, Vergne L, Saman E, Delaporte E, Saragosti S. 1999. Characterization of a highly replicative intergroup M/O human immunodeficiency virus type 1 recombinant isolated from a Cameroonian patient. J Virol 73:7368-7375.
    • (1999) J Virol , vol.73 , pp. 7368-7375
    • Peeters, M.1    Liegeois, F.2    Torimiro, N.3    Bourgeois, A.4    Mpoudi, E.5    Vergne, L.6    Saman, E.7    Delaporte, E.8    Saragosti, S.9
  • 42
    • 84866925345 scopus 로고    scopus 로고
    • Identification of alternatively translated tetherin isoforms with differing antiviral and signaling activities
    • Cocka LJ, Bates P. 2012. Identification of alternatively translated tetherin isoforms with differing antiviral and signaling activities. PLoS Pathog 8:e1002931. https://doi.org/10.1371/journal.ppat.1002931.
    • (2012) PLoS Pathog , vol.8
    • Cocka, L.J.1    Bates, P.2
  • 43
    • 84869194198 scopus 로고    scopus 로고
    • Innate sensing of HIV-1 assembly by tetherin induces N-kB-dependent proinflammatory responses
    • Galão RP, Le Tortorec A, Pickering S, Kueck T, Neil SJD. 2012. Innate sensing of HIV-1 assembly by tetherin induces N-kB-dependent proinflammatory responses. Cell Host Microbe 12:633-644. https://doi.org/10.1016/j.chom.2012.10.007.
    • (2012) Cell Host Microbe , vol.12 , pp. 633-644
    • Galão, R.P.1    Le Tortorec, A.2    Pickering, S.3    Kueck, T.4    Neil, S.J.D.5
  • 44
    • 84873864091 scopus 로고    scopus 로고
    • Stimulation of NF-κB activity by the HIV restriction factor BST2
    • Tokarev A, Suarez M, Kwan W, Fitzpatrick K, Singh R, Guatelli J. 2013. Stimulation of NF-κB activity by the HIV restriction factor BST2. J Virol 87:2046-2057. https://doi.org/10.1128/JVI.02272-12.
    • (2013) J Virol , vol.87 , pp. 2046-2057
    • Tokarev, A.1    Suarez, M.2    Kwan, W.3    Fitzpatrick, K.4    Singh, R.5    Guatelli, J.6
  • 45
    • 0035163739 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor κB-dependent expression of antiapoptotic factors
    • Akari H, Bour S, Kao S, Adachi A, Strebel K. 2001. The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor κB-dependent expression of antiapoptotic factors. J Exp Med 194:12991312.
    • (2001) J Exp Med , vol.194
    • Akari, H.1    Bour, S.2    Kao, S.3    Adachi, A.4    Strebel, K.5
  • 46
    • 0035844173 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein inhibits NF-κB activation by interfering with βTrCP-mediated degradation of IκB
    • Bour S, Perrin C, Akari H, Strebel K. 2001. The human immunodeficiency virus type 1 Vpu protein inhibits NF-κB activation by interfering with βTrCP-mediated degradation of IκB. J Biol Chem 276:15920-15928. https://doi.org/10.1074/jbc.M010533200.
    • (2001) J Biol Chem , vol.276 , pp. 15920-15928
    • Bour, S.1    Perrin, C.2    Akari, H.3    Strebel, K.4
  • 47
    • 36549052593 scopus 로고    scopus 로고
    • Clathrinmediated endocytosis of a lipid-raft-associated protein is mediated through a dual tyrosine motif
    • Rollason R, Korolchuk V, Hamilton C, Schu P, Banting G. 2007. Clathrinmediated endocytosis of a lipid-raft-associated protein is mediated through a dual tyrosine motif. J Cell Sci 120:3850-3858. https://doi.org/10.1242/jcs.003343.
    • (2007) J Cell Sci , vol.120 , pp. 3850-3858
    • Rollason, R.1    Korolchuk, V.2    Hamilton, C.3    Schu, P.4    Banting, G.5
  • 48
    • 67650120099 scopus 로고    scopus 로고
    • HM1.24 is internalized from lipid rafts by clathrin-mediated endocytosis through interaction with α-adaptin
    • Masuyama N, Kuronita T, Tanaka R, Muto T, Hirota Y, Takigawa A, Fujita H, Aso Y, Amano J, Tanaka Y. 2009. HM1.24 is internalized from lipid rafts by clathrin-mediated endocytosis through interaction with α-adaptin. J Biol Chem 284:15927-15941. https://doi.org/10.1074/jbc.M109.005124.
    • (2009) J Biol Chem , vol.284 , pp. 15927-15941
    • Masuyama, N.1    Kuronita, T.2    Tanaka, R.3    Muto, T.4    Hirota, Y.5    Takigawa, A.6    Fujita, H.7    Aso, Y.8    Amano, J.9    Tanaka, Y.10
  • 49
    • 84899090611 scopus 로고    scopus 로고
    • Differential sensitivities of tetherin isoforms to counteraction by primate lentiviruses
    • Weinelt J, Neil SJD. 2014. Differential sensitivities of tetherin isoforms to counteraction by primate lentiviruses. J Virol 88:5845-5858. https://doi.org/10.1128/JVI.03818-13.
    • (2014) J Virol , vol.88 , pp. 5845-5858
    • Weinelt, J.1    Neil, S.J.D.2
  • 51
    • 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. https://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
  • 52
    • 84876864784 scopus 로고    scopus 로고
    • Vpu Binds Directly to Tetherin and Displaces It from Nascent Virions
    • McNatt MW, Zang T, Bieniasz PD. 2013. Vpu Binds Directly to Tetherin and Displaces It from Nascent Virions. PLoS Pathog 9:e1003299.
    • (2013) PLoS Pathog , vol.9
    • McNatt, M.W.1    Zang, T.2    Bieniasz, P.D.3
  • 53
    • 84875057927 scopus 로고    scopus 로고
    • The transmembrane domain of HIV-1 Vpu is sufficient to confer anti-tetherin activity to SIVcpz and SIVgor Vpu proteins: cytoplasmic determinants of Vpu function
    • Kluge SF, Sauter D, Vogl M, Peeters M, Li Y, Bibollet-Ruche F, Hahn BH, Kirchhoff F. 2013. The transmembrane domain of HIV-1 Vpu is sufficient to confer anti-tetherin activity to SIVcpz and SIVgor Vpu proteins: cytoplasmic determinants of Vpu function. Retrovirology 10:32. https://doi.org/10.1186/1742-4690-10-32.
    • (2013) Retrovirology , vol.10 , pp. 32
    • Kluge, S.F.1    Sauter, D.2    Vogl, M.3    Peeters, M.4    Li, Y.5    Bibollet-Ruche, F.6    Hahn, B.H.7    Kirchhoff, F.8
  • 54
    • 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. https://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
  • 55
    • 78650373530 scopus 로고    scopus 로고
    • Modulation of HIV-1-host interaction: role of the Vpu accessory protein
    • Dubé M, Bego MG, Paquay C, Cohen éA. 2010. Modulation of HIV-1-host interaction: role of the Vpu accessory protein. Retrovirology 7:114. https://doi.org/10.1186/1742-4690-7-114.
    • (2010) Retrovirology , vol.7 , pp. 114
    • Dubé, M.1    Bego, M.G.2    Paquay, C.3    Cohen, É.A.4
  • 56
    • 77950495072 scopus 로고    scopus 로고
    • Antagonism of CD317 restriction of human immunodeficiency virus type 1 (HIV-1) particle release and depletion of CD317 are separable activities of HIV-1 Vpu
    • Goffinet C, Homann S, Ambiel I, Tibroni N, Rupp D, Keppler OT, Fackler OT. 2010. Antagonism of CD317 restriction of human immunodeficiency virus type 1 (HIV-1) particle release and depletion of CD317 are separable activities of HIV-1 Vpu. J Virol 84:4089-4094. https://doi.org/10.1128/JVI.01549-09.
    • (2010) J Virol , vol.84 , pp. 4089-4094
    • Goffinet, C.1    Homann, S.2    Ambiel, I.3    Tibroni, N.4    Rupp, D.5    Keppler, O.T.6    Fackler, O.T.7
  • 57
    • 79751526122 scopus 로고    scopus 로고
    • β-TrCP is dispensable for Vpu's ability to overcome the CD317/tetherinimposed restriction to HIV-1 release
    • Tervo H-M, Homann S, Ambiel I, Fritz JV, Fackler OT, Keppler OT. 2011. β-TrCP is dispensable for Vpu's ability to overcome the CD317/tetherinimposed restriction to HIV-1 release. Retrovirology 8:9. https://doi.org/10.1186/1742-4690-8-9.
    • (2011) Retrovirology , vol.8 , pp. 9
    • Tervo, H.-M.1    Homann, S.2    Ambiel, I.3    Fritz, J.V.4    Fackler, O.T.5    Keppler, O.T.6
  • 58
    • 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, Selig L, Benichou S, Richard V, Thomas D, Strebel K, Benarous R. 1998. 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 1:565-574. https://doi.org/10.1016/S1097-2765(00)80056-8.
    • (1998) Mol Cell , vol.1 , pp. 565-574
    • Margottin, F.1    Bour, S.P.2    Durand, H.3    Selig, L.4    Benichou, S.5    Richard, V.6    Thomas, D.7    Strebel, K.8    Benarous, R.9
  • 59
    • 67449119401 scopus 로고    scopus 로고
    • Targeting NEDD8-activated cullin-RING ligases for the treatment of cancer
    • Soucy TA, Smith PG, Rolfe M. 2009. Targeting NEDD8-activated cullin-RING ligases for the treatment of cancer. Clin Cancer Res 15:3912-3916. https://doi.org/10.1158/1078-0432.CCR-09-0343.
    • (2009) Clin Cancer Res , vol.15 , pp. 3912-3916
    • Soucy, T.A.1    Smith, P.G.2    Rolfe, M.3
  • 60
    • 84937903128 scopus 로고    scopus 로고
    • HIV-1 Vpu utilizes both cullin-RING ligase (CRL) dependent and independent mechanisms to downmodulate host proteins
    • Ramirez PW, Beatriz A, Silva D, Szaniawski M, Barker E, Bosque A. 2015. HIV-1 Vpu utilizes both cullin-RING ligase (CRL) dependent and independent mechanisms to downmodulate host proteins. Retrovirology 12:65. https://doi.org/10.1186/s12977-015-0192-2.
    • (2015) Retrovirology , vol.12 , pp. 65
    • Ramirez, P.W.1    Beatriz, A.2    Silva, D.3    Szaniawski, M.4    Barker, E.5    Bosque, A.6
  • 62
    • 0141521574 scopus 로고    scopus 로고
    • Down-modulation of mature major histocompatibility complex class II and up-regulation of invariant chain cell surface expression are well-conserved functions of human and simian immunodeficiency virus nef alleles
    • Schindler M, Würfl S, Benaroch P, Greenough TC, Daniels R, Easterbrook P, Brenner M, Münch J, Kirchhoff F. 2003. Down-modulation of mature major histocompatibility complex class II and up-regulation of invariant chain cell surface expression are well-conserved functions of human and simian immunodeficiency virus nef alleles. J Virol 77:10548-10556. https://doi.org/10.1128/JVI.77.19.10548-10556.2003.
    • (2003) J Virol , vol.77 , pp. 10548-10556
    • Schindler, M.1    Würfl, S.2    Benaroch, P.3    Greenough, T.C.4    Daniels, R.5    Easterbrook, P.6    Brenner, M.7    Münch, J.8    Kirchhoff, F.9
  • 63
    • 37849053288 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein interacts with CD74 and modulates major histocompatibility complex class II presentation
    • Hussain A, Wesley C, Khalid M, Chaudhry A, Jameel S. 2008. Human immunodeficiency virus type 1 Vpu protein interacts with CD74 and modulates major histocompatibility complex class II presentation. J Virol 82:893-902. https://doi.org/10.1128/JVI.01373-07.
    • (2008) J Virol , vol.82 , pp. 893-902
    • Hussain, A.1    Wesley, C.2    Khalid, M.3    Chaudhry, A.4    Jameel, S.5
  • 66
    • 84938776229 scopus 로고    scopus 로고
    • Vpu exploits the cross-talk between BST2 and the ILT7 receptor to suppress anti-HIV-1 responses by plasmacytoid dendritic cells
    • Bego MG, Côté é, Aschman N, Mercier J, Weissenhorn W, Cohen éA. 2015. Vpu exploits the cross-talk between BST2 and the ILT7 receptor to suppress anti-HIV-1 responses by plasmacytoid dendritic cells. PLoS Pathog 11:e1005024. https://doi.org/10.1371/journal.ppat.1005024.
    • (2015) PLoS Pathog , vol.11
    • Bego, M.G.1    Côté, É.2    Aschman, N.3    Mercier, J.4    Weissenhorn, W.5    Cohen, É.A.6
  • 67
    • 84995495192 scopus 로고    scopus 로고
    • Differential control of BST2 restriction and plasmacytoid dendritic cell antiviral response by antagonists encoded by HIV-1 group M and O strains
    • 31 August
    • Bego MG, Cong L, Mack K, Kirchhoff F. 31 August 2016. Differential control of BST2 restriction and plasmacytoid dendritic cell antiviral response by antagonists encoded by HIV-1 group M and O strains. J Virol https://doi.org/10.1128/JVI.01131-16.
    • (2016) J Virol
    • Bego, M.G.1    Cong, L.2    Mack, K.3    Kirchhoff, F.4
  • 69
    • 0028180868 scopus 로고
    • Nef induces CD4 endocytosis: requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain
    • Aiken C, Konner J, Landau NR, Lenburg ME, Trono D. 1994. Nef induces CD4 endocytosis: requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain. Cell 76:853-864. https://doi.org/10.1016/0092-8674(94)90360-3.
    • (1994) Cell , vol.76 , pp. 853-864
    • Aiken, C.1    Konner, J.2    Landau, N.R.3    Lenburg, M.E.4    Trono, D.5
  • 70
    • 0028200761 scopus 로고
    • Human immunodeficiency virus type 1 Nefinduced down-modulation of CD4 is due to rapid internalization and degradation of surface CD4
    • Rhee SS, Marsh JW. 1994. Human immunodeficiency virus type 1 Nefinduced down-modulation of CD4 is due to rapid internalization and degradation of surface CD4. J Virol 68:5156-5163.
    • (1994) J Virol , vol.68 , pp. 5156-5163
    • Rhee, S.S.1    Marsh, J.W.2
  • 71
    • 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
  • 72
    • 0037370728 scopus 로고    scopus 로고
    • Nef-mediated disruption of HLA-A2 transport to the cell surface in T cells
    • Kasper MR, Collins KL. 2003. Nef-mediated disruption of HLA-A2 transport to the cell surface in T cells. J Virol 77:3041-3049. https://doi.org/10.1128/JVI.77.5.3041-3049.2003.
    • (2003) J Virol , vol.77 , pp. 3041-3049
    • Kasper, M.R.1    Collins, K.L.2
  • 73
    • 16844383765 scopus 로고    scopus 로고
    • HIV-1 Nef disrupts antigen presentation early in the secretory pathway
    • Kasper MR, Roeth JF, Williams M, Filzen TM, Fleis RI, Collins KL. 2005. HIV-1 Nef disrupts antigen presentation early in the secretory pathway. J Biol Chem 280:12840-12848. https://doi.org/10.1074/jbc.M413538200.
    • (2005) J Biol Chem , vol.280 , pp. 12840-12848
    • Kasper, M.R.1    Roeth, J.F.2    Williams, M.3    Filzen, T.M.4    Fleis, R.I.5    Collins, K.L.6
  • 76
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0
    • Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, Gascuel O. 2010. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst Biol 59: 307-321. https://doi.org/10.1093/sysbio/syq010.
    • (2010) Syst Biol , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 77
    • 84864453108 scopus 로고    scopus 로고
    • jModelTest 2: more models, new heuristics and parallel computing
    • Darriba D, Taboada GL, Doallo R, Posada D. 2012. jModelTest 2: more models, new heuristics and parallel computing. Nat Methods 9:772. https://doi.org/10.1038/nmeth.2109.
    • (2012) Nat Methods , vol.9 , pp. 772
    • Darriba, D.1    Taboada, G.L.2    Doallo, R.3    Posada, D.4
  • 78
    • 0032889281 scopus 로고    scopus 로고
    • Full-length human immunodeficiency virus type 1 genomes from subtype C-infected seroconverters in India, with evidence of intersubtype recombination
    • Lole KS, Bollinger RC, Paranjape RS, Gadkari D, Kulkarni SS, Novak NG, Ingersoll R, Sheppard HW, Ray SC. 1999. Full-length human immunodeficiency virus type 1 genomes from subtype C-infected seroconverters in India, with evidence of intersubtype recombination. J Virol 73:152-160.
    • (1999) J Virol , vol.73 , pp. 152-160
    • Lole, K.S.1    Bollinger, R.C.2    Paranjape, R.S.3    Gadkari, D.4    Kulkarni, S.S.5    Novak, N.G.6    Ingersoll, R.7    Sheppard, H.W.8    Ray, S.C.9
  • 79
    • 0030747461 scopus 로고    scopus 로고
    • HIV-1 infection of non-dividing cells: evidence that the amino-terminal basic region of the viral matrix protein is important for Gag processing but not for post-entry nuclear import
    • Fouchier RAM, Meyer BE, Simon JHM, Fischer U, Malim MH. 1997. HIV-1 infection of non-dividing cells: evidence that the amino-terminal basic region of the viral matrix protein is important for Gag processing but not for post-entry nuclear import. EMBO J 16:4531-4539. https://doi.org/10.1093/emboj/16.15.4531.
    • (1997) EMBO J , vol.16 , pp. 4531-4539
    • Fouchier, R.A.M.1    Meyer, B.E.2    Simon, J.H.M.3    Fischer, U.4    Malim, M.H.5
  • 80
    • 37049029214 scopus 로고    scopus 로고
    • Nef-mediated enhancement of virion infectivity and stimulation of viral replication are fundamental properties of primate lentiviruses
    • Münch J, Rajan D, Schindler M, Specht A, Ru E, Novembre FJ, Nerrienet E, Mu MC, Peeters M, Hahn BH, Kirchhoff F. 2007. Nef-mediated enhancement of virion infectivity and stimulation of viral replication are fundamental properties of primate lentiviruses. J Virol 81:13852-13864. https://doi.org/10.1128/JVI.00904-07.
    • (2007) J Virol , vol.81 , pp. 13852-13864
    • Münch, J.1    Rajan, D.2    Schindler, M.3    Specht, A.4    Ru, E.5    Novembre, F.J.6    Nerrienet, E.7    Mu, M.C.8    Peeters, M.9    Hahn, B.H.10    Kirchhoff, F.11
  • 81
    • 0031954686 scopus 로고    scopus 로고
    • Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1
    • Platt EJ, Wehrly K, Kuhmann SE, Chesebro B, Kabat D. 1998. Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1. J Virol 72: 2855-2864.
    • (1998) J Virol , vol.72 , pp. 2855-2864
    • Platt, E.J.1    Wehrly, K.2    Kuhmann, S.E.3    Chesebro, B.4    Kabat, D.5
  • 85
    • 84942815345 scopus 로고    scopus 로고
    • Structural determination of virus protein U from HIV-1 by NMR in membrane environments
    • Zhang H, Lin EC, Das BB, Tian Y, Opella SJ. 2015. Structural determination of virus protein U from HIV-1 by NMR in membrane environments. BiochimBiophysActa1848:3007-3018.https://doi.org/10.1016/j.bbamem.2015.09.008.
    • (2015) BiochimBiophys Acta , vol.1848 , pp. 3007-3018
    • Zhang, H.1    Lin, E.C.2    Das, B.B.3    Tian, Y.4    Opella, S.J.5
  • 86
    • 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. https://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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.