| Literature DB >> 24867973 |
Andrew D Huber1, Eleftherios Michailidis2, Megan L Schultz3, Yee T Ong2, Nicolin Bloch3, Maritza N Puray-Chavez2, Maxwell D Leslie2, Juan Ji2, Anthony D Lucas2, Karen A Kirby2, Nathaniel R Landau3, Stefan G Sarafianos4.
Abstract
Sterile alpha motif- and histidine/aspartic acid domain-containing protein 1 (SAMHD1) limits HIV-1 replication by hydrolyzing deoxynucleoside triphosphates (dNTPs) necessary for reverse transcription. Nucleoside reverse transcriptase inhibitors (NRTIs) are components of anti-HIV therapies. We report here that SAMHD1 cleaves NRTI triphosphates (TPs) at significantly lower rates than dNTPs and that SAMHD1 depletion from monocytic cells affects the susceptibility of HIV-1 infections to NRTIs in complex ways that depend not only on the relative changes in dNTP and NRTI-TP concentrations but also on the NRTI activation pathways.Entities:
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Year: 2014 PMID: 24867973 PMCID: PMC4136039 DOI: 10.1128/AAC.02745-14
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191