{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T05:25:40Z","timestamp":1789709140919,"version":"4.0.1"},"reference-count":35,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2015,6,15]],"date-time":"2015-06-15T00:00:00Z","timestamp":1434326400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2015,6,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>Replication of the integrated HIV-1 genome is tightly regulated by a series of cellular factors. In previous work we showed that transactivation of the HIV-1 promoter is regulated by the cellular splicing factor SRSF1. Here we report that SRSF1 can downregulate the replication of B, C, and D subtype viruses by &gt;200-fold in a cell culture system. We show that viral transcription and splicing are inhibited by SRSF1 expression. Furthermore, SRSF1 deletion mutants containing the protein RNA-binding domains but not the arginine serine-rich activator domain can downregulate viral replication by &gt;2,000-fold with minimal impact on cell viability and apoptosis. These data suggest a therapeutic potential for SRSF1 and its RNA-binding domains.<\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            Most drugs utilized to treat the HIV-1 infection are based on compounds that directly target proteins encoded by the virus. However, given the high viral mutation rate, the appearance of novel drug-resistant viral strains is common. Thus, there is a need for novel therapeutics with diverse mechanisms of action. In this study, we show that the cellular protein SRSF1 is a strong inhibitor of viral replication. Furthermore, expression of the SRSF1 RNA-binding domains alone can inhibit viral replication by &gt;2,000-fold in multiple viral strains without impacting cell viability. Given the strong antiviral properties of this protein, the RNA-binding domains, and the minimal effects observed on cell metabolism, further studies are warranted to assess the therapeutic potential of peptides derived from these sequences.\n          <\/jats:p>","DOI":"10.1128\/jvi.00693-15","type":"journal-article","created":{"date-parts":[[2015,4,9]],"date-time":"2015-04-09T02:32:09Z","timestamp":1428546729000},"page":"6275-6286","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":21,"title":["SRSF1 RNA Recognition Motifs Are Strong Inhibitors of HIV-1 Replication"],"prefix":"10.1128","volume":"89","author":[{"given":"Sean","family":"Paz","sequence":"first","affiliation":[{"name":"Charles E. Schmidt College of Medicine, Florida Atlantic University, Boca Raton, Florida, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael L.","family":"Lu","sequence":"additional","affiliation":[{"name":"Charles E. Schmidt College of Medicine, Florida Atlantic University, Boca Raton, Florida, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroshi","family":"Takata","sequence":"additional","affiliation":[{"name":"Vaccine Gene Therapy Institute Florida, Port Saint Lucie, Florida, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lydie","family":"Trautmann","sequence":"additional","affiliation":[{"name":"Vaccine Gene Therapy Institute Florida, Port Saint Lucie, Florida, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Massimo","family":"Caputi","sequence":"additional","affiliation":[{"name":"Charles E. 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