HIV-1 Vpu protein forms stable oligomers in aqueous solution via its transmembrane domain self-association. | HIV-1 Vpu protein forms stable oligomers in aqueous solution via its transmembrane domain self-association. Majeed S, Dang L, Islam MM, Ishola O, Borbat PP, Ludtke SJ, Georgieva ER., Free PMC Article | 09/8/2023 |
A Novel Vpu Adaptive Mutation of HIV-1 Degrades Tetherin in Northern Pig-Tailed Macaques (Macaca leonina) Mainly via the Ubiquitin-Proteasome Pathway and Increases Viral Release. | A Novel Vpu Adaptive Mutation of HIV-1 Degrades Tetherin in Northern Pig-Tailed Macaques (Macaca leonina) Mainly via the Ubiquitin-Proteasome Pathway and Increases Viral Release. Lu Y, Pang W, Zhang MD, Song JH, Shen F, He WQ, Zheng YT., Free PMC Article | 05/26/2023 |
Insights into the oligomeric structure of the HIV-1 Vpu protein. | Insights into the oligomeric structure of the HIV-1 Vpu protein. Majeed S, Adetuyi O, Borbat PP, Majharul Islam M, Ishola O, Zhao B, Georgieva ER., Free PMC Article | 03/14/2023 |
Host KIR/HLA-C Genotypes Determine HIV-Mediated Changes of the NK Cell Repertoire and Are Associated With Vpu Sequence Variations Impacting Downmodulation of HLA-C. | Host KIR/HLA-C Genotypes Determine HIV-Mediated Changes of the NK Cell Repertoire and Are Associated With Vpu Sequence Variations Impacting Downmodulation of HLA-C. Vollmers S, Lobermeyer A, Niehrs A, Fittje P, Indenbirken D, Nakel J, Virdi S, Brias S, Trenkner T, Sauer G, Peine S, Behrens GMN, Lehmann C, Meurer A, Pauli R, Postel N, Roider J, Scholten S, Spinner CD, Stephan C, Wolf E, Wyen C, Richert L, Norman PJ, Sauter J, Schmidt AH, Hoelzemer A, Altfeld M, Körner C., Free PMC Article | 10/22/2022 |
Conditional activation of an HIV-1 protease attenuated mutant by a leucine zipper dimerization motif. | Conditional activation of an HIV-1 protease attenuated mutant by a leucine zipper dimerization motif. Yu FH, Huang KJ, Wang CT. | 04/23/2022 |
Role of Viral Protein U (Vpu) in HIV-1 Infection and Pathogenesis. | Role of Viral Protein U (Vpu) in HIV-1 Infection and Pathogenesis. Khan N, Geiger JD., Free PMC Article | 02/5/2022 |
HIV-1 Vpu Promotes Phagocytosis of Infected CD4(+) T Cells by Macrophages through Downregulation of CD47. | HIV-1 Vpu Promotes Phagocytosis of Infected CD4(+) T Cells by Macrophages through Downregulation of CD47. Cong L, Sugden SM, Leclair P, Lim CJ, Pham TNQ, Cohen ÉA., Free PMC Article | 12/25/2021 |
The viral protein U (Vpu)-interacting host protein ATP6V0C down-regulates cell-surface expression of tetherin and thereby contributes to HIV-1 release. | The viral protein U (Vpu)-interacting host protein ATP6V0C down-regulates cell-surface expression of tetherin and thereby contributes to HIV-1 release. Waheed AA, Swiderski M, Khan A, Gitzen A, Majadly A, Freed EO., Free PMC Article | 12/26/2020 |
Differential Vpu-Mediated CD4 and Tetherin Downregulation Functions among Major HIV-1 Group M Subtypes. | Differential Vpu-Mediated CD4 and Tetherin Downregulation Functions among Major HIV-1 Group M Subtypes. Umviligihozo G, Cobarrubias KD, Chandrarathna S, Jin SW, Reddy N, Byakwaga H, Muzoora C, Bwana MB, Lee GQ, Hunt PW, Martin JN, Brumme CJ, Bangsberg DR, Karita E, Allen S, Hunter E, Ndung'u T, Brumme ZL, Brockman MA., Free PMC Article | 11/21/2020 |
HIV-1 Vpu Downregulates Tim-3 from the Surface of Infected CD4(+) T Cells. | HIV-1 Vpu Downregulates Tim-3 from the Surface of Infected CD4(+) T Cells. Prévost J, Edgar CR, Richard J, Trothen SM, Jacob RA, Mumby MJ, Pickering S, Dubé M, Kaufmann DE, Kirchhoff F, Neil SJD, Finzi A, Dikeakos JD., Free PMC Article | 09/19/2020 |
In summary, these findings demonstrate that HIV-1 Vpu potently suppresses NF-kappaB-elicited antiviral immune responses at the transcriptional level. | HIV-1 Vpu is a potent transcriptional suppressor of NF-κB-elicited antiviral immune responses. Langer S, Hammer C, Hopfensperger K, Klein L, Hotter D, De Jesus PD, Herbert KM, Pache L, Smith N, van der Merwe JA, Chanda SK, Fellay J, Kirchhoff F, Sauter D., Free PMC Article | 03/28/2020 |
this study shows that the activation of the JAK/STAT pathway by IFN-alpha stimulation is disrupted by HIV proteins Vpu and Nef, which both reduce IFN-alpha induction of STAT1 phosphorylation | HIV blocks Type I IFN signaling through disruption of STAT1 phosphorylation. Nguyen NV, Tran JT, Sanchez DJ., Free PMC Article | 07/6/2019 |
cellular targets of the HIV-1 accessory protein Vpu were identified. | Large-Scale Arrayed Analysis of Protein Degradation Reveals Cellular Targets for HIV-1 Vpu. Jain P, Boso G, Langer S, Soonthornvacharin S, De Jesus PD, Nguyen Q, Olivieri KC, Portillo AJ, Yoh SM, Pache L, Chanda SK., Free PMC Article | 06/22/2019 |
The primary role of the S(52,56) residues of Vpu in antagonism of CD4, GaLV Env, and BST-2/tetherin is to recruit the SCF/betaTrCP ubiquitin ligase. | βTrCP is Required for HIV-1 Vpu Modulation of CD4, GaLV Env, and BST-2/Tetherin. Song YE, Cyburt D, Lucas TM, Gregory DA, Lyddon TD, Johnson MC., Free PMC Article | 12/22/2018 |
Dual regulation of CD62L by HIV-1 via enhanced expression by Vpr in contrast with cell-surface down-modulation by Nef and Vpu has been reported. | Dual regulation of L-selectin (CD62L) by HIV-1: Enhanced expression by Vpr in contrast with cell-surface down-modulation by Nef and Vpu. Giuliani E, Vassena L, Galardi S, Michienzi A, Desimio MG, Doria M. | 09/22/2018 |
RNA sequencing and functional analyses found that subtype A Vpu alleles displayed similar levels of CD4 and SNAT1 downregulation than NL4.3. The ability of both subtype for downregulation of CD4 was comparable but subtype A displayed a greater SNAT1 downregulation activity. The Vpu alleles differentially induced downregulation of HLA-C but the downregulation of tetherin and enhancement of virus release was similar. | Functional conservation and coherence of HIV-1 subtype A Vpu alleles. Romani B, Kavyanifard A, Allahbakhshi E., Free PMC Article | 09/8/2018 |
The results establish tetherin as a key effector of the intrinsic immune defense against HIV-1, and they demonstrate that Vpu-mediated tetherin antagonism is critical for efficient viral spread during the initial phase of HIV-1 replication. | Human-Specific Adaptations in Vpu Conferring Anti-tetherin Activity Are Critical for Efficient Early HIV-1 Replication In Vivo. Yamada E, Nakaoka S, Klein L, Reith E, Langer S, Hopfensperger K, Iwami S, Schreiber G, Kirchhoff F, Koyanagi Y, Sauter D, Sato K. | 08/18/2018 |
Vpu oligomerizaion is driven by the assembly of the transmembrane domain, independent of negative charges due to phosphorylation of the two serines 52 and 56. | Membrane protein assembly: two cytoplasmic phosphorylated serine sites of Vpu from HIV-1 affect oligomerization. Chen CP, Lin MH, Chan YT, Chen LC, Ma C, Fischer WB., Free PMC Article | 06/2/2018 |
Coimmunoprecipitation studies indicated that non-glycosylated tetherin is stabilized through the formation of a ternary SGTA/Vpu/tetherin complex. Although the results do not provide support for a physiological function of SGTA in HIV-1 replication, they demonstrate that SGTA overexpression regulates tetherin expression and stability, thus providing insights into the function of SGTA in endoplasmic reticulum translocation | The Vpu-interacting Protein SGTA Regulates Expression of a Non-glycosylated Tetherin Species. Waheed AA, MacDonald S, Khan M, Mounts M, Swiderski M, Xu Y, Ye Y, Freed EO., Free PMC Article | 01/20/2018 |
Promiscuous yet Specific Interactions of the HIV-1 Vpu Transmembrane Domain | FRET Analysis of the Promiscuous yet Specific Interactions of the HIV-1 Vpu Transmembrane Domain. Cole GB, Reichheld SE, Sharpe S., Free PMC Article | 12/2/2017 |
Our results identify cGAS as mediator of an IFN-I response to HIV-1 infection in CD4(+) T cells and demonstrate that this response is modulated by the viral accessory proteins Vpr and Vpu. Thus, viral innate immune evasion is incomplete in the main target cells of HIV-1 | HIV Triggers a cGAS-Dependent, Vpu- and Vpr-Regulated Type I Interferon Response in CD4(+) T Cells. Vermeire J, Roesch F, Sauter D, Rua R, Hotter D, Van Nuffel A, Vanderstraeten H, Naessens E, Iannucci V, Landi A, Witkowski W, Baeyens A, Kirchhoff F, Verhasselt B. | 12/2/2017 |
a non-canonical autophagy pathway reminiscent of LC3-associated phagocytosis contributes to Vpu counteraction of BST2 restriction. | LC3C Contributes to Vpu-Mediated Antagonism of BST2/Tetherin Restriction on HIV-1 Release through a Non-canonical Autophagy Pathway. Madjo U, Leymarie O, Frémont S, Kuster A, Nehlich M, Gallois-Montbrun S, Janvier K, Berlioz-Torrent C. | 11/25/2017 |
HLA-C reduction is mediated by viral Vpu and reduces the ability of HLA-C restricted CTLs to suppress viral replication in CD4+ cells in vitro. | HIV-1 Vpu Mediates HLA-C Downregulation. Apps R, Del Prete GQ, Chatterjee P, Lara A, Brumme ZL, Brockman MA, Neil S, Pickering S, Schneider DK, Piechocka-Trocha A, Walker BD, Thomas R, Shaw GM, Hahn BH, Keele BF, Lifson JD, Carrington M., Free PMC Article | 09/23/2017 |
Data suggest that, for HIV-1 protease, substrates interact with protease through multiple main chain hydrogen bonding and nonpolar interactions, while inhibitors interact majorly with side chains of protease active site residues. | How Mutations Can Resist Drug Binding yet Keep HIV-1 Protease Functional. Appadurai R, Senapati S. | 07/8/2017 |
Thus, efficient human immunodeficiency virus type 1 release from infected cells seems to play an important role in the spread of the virus in the human population and requires a fully functional Vpu protein that counteracts human tetherin. | Vpu-Mediated Counteraction of Tetherin Is a Major Determinant of HIV-1 Interferon Resistance. Kmiec D, Iyer SS, Stürzel CM, Sauter D, Hahn BH, Kirchhoff F., Free PMC Article | 06/24/2017 |