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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2026,5,5]]},"abstract":"<jats:p>SUMOylation is a dynamically regulated post-translational modification involving covalent attachment of small ubiquitin-like modifiers (SUMOs) to lysine residues of target proteins. SUMOylation modulates multiple fundamental host cellular pathways, including pathways hijacked by HIV-1 to enable replication, but has not been explored by large-scale proteomics in the context of HIV-1 infection. Here, we performed a proteome-wide, mass spectrometry-based screen to identify proteins that are SUMOylated in response to HIV-1 infection. We show that infection with HIV-1 leads to the widespread increased SUMOylation of the heterogeneous nuclear ribonucleoprotein (HNRNP) A\/B family. This phenotype was driven by expression of HIV-1 Viral Infectivity Factor (Vif), suggesting an unexplored function for this protein. Depletion of HNRNP A\/B proteins led to altered splicing of HIV-1 viral RNAs and dramatically reduced HIV-1 infectivity. 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