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https://hdl.handle.net/10316/107185
Title: | Cellular TRIM33 restrains HIV-1 infection by targeting viral integrase for proteasomal degradation | Authors: | Ali, Hashim Mano, Miguel Braga, Luca Naseem, Asma Marini, Bruna Vu, Diem My Collesi, Chiara Meroni, Germana Lusic, Marina Giacca, Mauro |
Issue Date: | 25-Feb-2019 | Publisher: | Springer Nature | Project: | Intramural Funding Programme of the ICGEB to the Molecular Medicine Laboratory in Trieste, Italy | Serial title, monograph or event: | Nature Communications | Volume: | 10 | Issue: | 1 | Abstract: | Productive HIV-1 replication requires viral integrase (IN), which catalyzes integration of the viral genome into the host cell DNA. IN, however, is short lived and is rapidly degraded by the host ubiquitin-proteasome system. To identify the cellular factors responsible for HIV-1 IN degradation, we performed a targeted RNAi screen using a library of siRNAs against all components of the ubiquitin-conjugation machinery using high-content microscopy. Here we report that the E3 RING ligase TRIM33 is a major determinant of HIV-1 IN stability. CD4-positive cells with TRIM33 knock down show increased HIV-1 replication and proviral DNA formation, while those overexpressing the factor display opposite effects. Knock down of TRIM33 reverts the phenotype of an HIV-1 molecular clone carrying substitution of IN serine 57 to alanine, a mutation known to impair viral DNA integration. Thus, TRIM33 acts as a cellular factor restricting HIV-1 infection by preventing provirus formation. | URI: | https://hdl.handle.net/10316/107185 | ISSN: | 2041-1723 | DOI: | 10.1038/s41467-019-08810-0 | Rights: | openAccess |
Appears in Collections: | I&D CNC - Artigos em Revistas Internacionais |
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Cellular-TRIM33-restrains-HIV1-infection-by-targeting-viral-integrase-for-proteasomal-degradationNature-Communications.pdf | 2.79 MB | Adobe PDF | View/Open |
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