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DC Field | Value | Language |
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dc.contributor.author | Banerjea, Akhil C | - |
dc.contributor.author | Ali, Amjad | - |
dc.contributor.author | Raja, Rameez | - |
dc.contributor.author | Farooqui, Sabihur Rahman | - |
dc.contributor.author | Ahmad, Shaista | - |
dc.date.accessioned | 2022-08-18T09:42:11Z | - |
dc.date.available | 2022-08-18T09:42:11Z | - |
dc.date.issued | 2017-05 | - |
dc.identifier.uri | http://hdl.handle.net/123456789/1401 | - |
dc.description.abstract | Deubiquitinases (DUBs) are key regulators of complex cellular processes. HIV-1 Tat is synthesized early after infection and is mainly responsible for enhancing viral production. Here, we report that one of the DUBs, USP7, stabilized the HIV-1 Tat protein through its deubiquitination. Treatment with either a general DUB inhibitor (PR-619) or USP7-specific inhibitor (P5091) resulted in Tat protein degradation. The USP7-specific inhibitor reduced virus production in a latently infected T-lymphocytic cell line J1.1, which produces large amounts of HIV-1 upon stimulation. A potent increase in Tat-mediated HIV-1 production was observed with USP7 in a dose-dependent manner. As expected, deletion of the USP7 gene using the CRISPR-Cas9 method reduced the Tat protein and supported less virus production. Interestingly, the levels of endogenous USP7 increased after HIV-1 infection in human T-cells (MOLT-3) and in mammalian cells transfected with HIV-1 proviral DNA. Thus, HIV-1 Tat is stabilized by the host cell deubiquitinase USP7, leading to enhanced viral production, and HIV-1 in turn up-regulates the USP7 protein level. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Portland Press Limited | en_US |
dc.subject | HIV-1; deubiquitination; protein degradation; transactivation | en_US |
dc.title | USP7 deubiquitinase controls HIV-1 production by stabilizing Tat protein | en_US |
dc.type | Article | en_US |
dc.journal | Biochem J | en_US |
dc.volumeno | 474 | en_US |
dc.issueno | 10 | en_US |
dc.pages | 1653-1668 | en_US |
Appears in Collections: | Virology- II, Publications |
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File | Description | Size | Format | |
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bcj-2016-0304.pdf | 1.17 MB | Adobe PDF | View/Open Request a copy |
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