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https://hdl.handle.net/10316/107185
Título: | Cellular TRIM33 restrains HIV-1 infection by targeting viral integrase for proteasomal degradation | Autor: | Ali, Hashim Mano, Miguel Braga, Luca Naseem, Asma Marini, Bruna Vu, Diem My Collesi, Chiara Meroni, Germana Lusic, Marina Giacca, Mauro |
Data: | 25-Fev-2019 | Editora: | Springer Nature | Projeto: | Intramural Funding Programme of the ICGEB to the Molecular Medicine Laboratory in Trieste, Italy | Título da revista, periódico, livro ou evento: | Nature Communications | Volume: | 10 | Número: | 1 | Resumo: | 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 | Direitos: | openAccess |
Aparece nas coleções: | I&D CNC - Artigos em Revistas Internacionais |
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Ficheiro | Descrição | Tamanho | Formato | |
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Cellular-TRIM33-restrains-HIV1-infection-by-targeting-viral-integrase-for-proteasomal-degradationNature-Communications.pdf | 2.79 MB | Adobe PDF | Ver/Abrir |
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