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GOLDSTONE, David C; ENNIS-ADENIRAN, Valerie; DE CARVALHO, Luiz Pedro S; STOYE, Jonathan P; CROW, Yanick J; TAYLOR, Ian A; WEBB, Michelle; HEDDEN, Joseph J; GROOM, Harriet C. T; RICE, Gillian I; CHRISTODOULOU, Evangelos; WALKER, Philip A; KELLY, Geoff; HAIRE, LesleyF; YAP, Melvyn W
Nature (London), 12/2011, Letnik: 480, Številka: 7377Journal Article
SAMHD1, an analogue of the murine interferon (IFN)-γ-induced gene Mg11 (ref. 1), has recently been identified as a human immunodeficiency virus-1 (HIV-1) restriction factor that blocks early-stage virus replication in dendritic and other myeloid cells and is the target of the lentiviral protein Vpx, which can relieve HIV-1 restriction. SAMHD1 is also associated with Aicardi-Goutières syndrome (AGS), an inflammatory encephalopathy characterized by chronic cerebrospinal fluid lymphocytosis and elevated levels of the antiviral cytokine IFN-α. The pathology associated with AGS resembles congenital viral infection, such as transplacentally acquired HIV. Here we show that human SAMHD1 is a potent dGTP-stimulated triphosphohydrolase that converts deoxynucleoside triphosphates to the constituent deoxynucleoside and inorganic triphosphate. The crystal structure of the catalytic core of SAMHD1 reveals that the protein is dimeric and indicates a molecular basis for dGTP stimulation of catalytic activity against dNTPs. We propose that SAMHD1, which is highly expressed in dendritic cells, restricts HIV-1 replication by hydrolysing the majority of cellular dNTPs, thus inhibiting reverse transcription and viral complementary DNA (cDNA) synthesis.
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