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Although accumulating evidence indicates the importance of deubiquitination enzymes (DUBs) in innate immunity, it is unknown if they participate in A3G stability. Here, we found that USP49 directly interacts with A3G and efficiently removes ubiquitin, consequently increasing A3G protein expression and significantly enhancing its anti-HIV-1 activity. Unexpectedly, A3G degradation was also mediated by a Vif- and cullin-ring-independent pathway, which was effectively counteracted by USP49. Furthermore, clinical data suggested that USP49 is correlated with A3G protein expression and hypermutations in Vif-positive proviruses, and inversely with the intact provirus ratio in the HIV-1 latent reservoir. Our studies demonstrated a mechanism to effectively stabilize A3G expression, which could comprise a target to control HIV-1 infection and eradicate the latent reservoir.<\/jats:p>","DOI":"10.7554\/elife.48318","type":"journal-article","created":{"date-parts":[[2019,8,9]],"date-time":"2019-08-09T08:00:18Z","timestamp":1565337618000},"source":"Crossref","is-referenced-by-count":32,"title":["USP49 potently stabilizes APOBEC3G protein by removing ubiquitin and inhibits HIV-1 replication"],"prefix":"10.7554","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7106-7312","authenticated-orcid":true,"given":"Ting","family":"Pan","sequence":"first","affiliation":[{"name":"Institute of Human Virology, Key Laboratory of Tropical Disease Control of Ministry of Education, Guangdong Engineering Research Center for Antimicrobial Agent and Immunotechnology, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, 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