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Cellular TRIM33 restrains HIV-1 infection by targeting viral integrase for proteasomal degradation
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Cellular TRIM33 restrains HIV-1 infection by targeting viral integrase for proteasomal degradation
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Journal Article
Cellular TRIM33 restrains HIV-1 infection by targeting viral integrase for proteasomal degradation
2019
Overview
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.
HIV-1 integration into host DNA is mediated by the viral integrase (IN). Here, using siRNA screen and high-content microscopy, the authors identify the host E3 RING ligase TRIM33 to affect IN stability and show that TRIM33 prevents viral integration by triggering IN proteasome-mediated degradation.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/1
/ 13/109
/ 13/44
/ 13/89
/ 38/22
/ 38/35
/ 38/47
/ 38/89
/ 38/90
/ 631/337
/ Alanine
/ DNA
/ Genomes
/ HIV
/ Human immunodeficiency virus
/ Humanities and Social Sciences
/ Humans
/ Mutation
/ Proteasome Endopeptidase Complex - genetics
/ Proteasome Endopeptidase Complex - metabolism
/ Science
/ Serine
/ siRNA
/ Transcription Factors - genetics
