ArticleProceedings of the National Academy of Sciences of the United States of America2026
HIV-1 infection induces Vif-mediated SUMOylation of host RNA splicing factors important for proper viral RNA splicing.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Hijacking the Host: Post-Translational Modifications as Molecular Switches in HIV Persistence and Immune Evasion.Journal of medical virology · 2026Review
- HIV-1 Vif-dependent SUMOylation regulates viral RNA splicing.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
Corrections and comments
- Commented on by
Authors and funding
9 authors.
Funding
Abstract
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. Our data suggest a mechanism involving HIV-1-induced, Vif-mediated SUMOylation of host RNA splicing factors as a means to regulate HIV-1 alternative splicing.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.