ArticleScience advances2025
Restriction of HIV-1 infectivity by interferon and IFITM3 is counteracted by Nef.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Replication-competent SIVcpz CRISPR screen identifies barriers to successful cross-species transmission.Journal of virology · 2026Article
- Dual Functionality of miRNAs During HIV Infection: From Viral Genome Suppression to Immune Response Modulation.Epigenomes · 2026Review
- Molecular Regulation of HIV-1 Expression and Persistence Across Diverse Cellular Reservoirs.International journal of molecular sciences · 2026Review
- Divergent HIV-1 Restriction Phenotypes of IFITMs Expressed in Target Cells and Incorporated into Virions.Biomolecules · 2026Article
- AP2: an indispensable host factor in virus infection.Journal of virology · 2026Review
- IFITM3 at the viral fusion-pore checkpoint: membrane energetics and entry-route-dependent outcomes.Frontiers in immunology · 2026Review
- HIV-1 Nef inhibits the JAK/STAT signaling pathway by inducing proteasomal degradation of STAT1.PloS one · 2026Article
- Combined effects of restriction factors and transduction adjuvants on lentiviral vector gene transfer efficacy.Scientific reports · 2025Article
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7 authors.
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Abstract
The viral accessory protein Nef is a major determinant of HIV-1 pathogenicity in vivo. Nef is a multifunctional, immunomodulatory protein that downmodulates cell surface proteins, including CD4 and MHC class I (MHC-I), which are important for T cell-mediated immunity. In addition, Nef also regulates cell-intrinsic immunity-Nef boosts the infectivity of virions produced and released from HIV-infected cells, at least in part, by counteracting the antiviral activity of transmembrane proteins SERINC3 and SERINC5. Here, we show that Nef proteins derived from many primary isolates of HIV-1 restore infectivity in interferon-treated cells and confer resistance to the antiviral protein interferon-induced transmembrane protein 3 (IFITM3) in a SERINC3/5-independent manner. Using Nef derived from primary HIV-1 clade C infection, we found that Nef interacts with IFITM3 in membranes, reduces IFITM3 incorporation into HIV-1 virions, and restores HIV-1 fusion with target cells. Our findings reveal a previously unrecognized immunomodulatory role for Nef in the setting of the interferon-induced antiviral state during HIV-1 infection.
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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.