Cellular TRIM33 restrains HIV-1 infection by targeting viral integrase for proteasomal degradation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Hashim Ali, Miguel Mano, Luca Braga, Asma Naseem, Bruna Marini, Diem My Vu, Chiara Collesi, Germana Meroni, Marina Lusic, Mauro Giacca

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. More... »

PAGES

926

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41467-019-08810-0

    DOI

    http://dx.doi.org/10.1038/s41467-019-08810-0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1112366065

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/30804369


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