biostudies-literatureWang CJLU | Program for Jilin University Science and Technology Innovative Research TeamChina Postdoctoral Science Foundation | National Postdoctoral Program for Innovative TalentsKey Projects in the National Science &amp; Technology Pillar Program in the Thirteenth Five-Year Plan PeriodNational Natural Science Foundation of ChinaChina Postdoctoral Science Foundation4252-4264https://www.ebi.ac.uk/biostudies/studies/S-EPMC7105322biostudies-literatureUnknown295(13)SAM and HD domain-containing protein 1 (SAMHD1) is a host factor that restricts reverse transcription of lentiviruses such as HIV in myeloid cells and resting T cells through its dNTP triphosphohydrolase (dNTPase) activity. Lentiviruses counteract this restriction by expressing the accessory protein Vpx or Vpr, which targets SAMHD1 for proteasomal degradation. SAMHD1 is conserved among mammals, and the feline and bovine SAMHD1 proteins (fSAM and bSAM) restrict lentiviruses by reducing cellular dNTP concentrations. However, the functional regions of fSAM and bSAM that are required for their biological functions are not well-characterized. Here, to establish alternative models to investigate SAMHD1 <i>in vivo</i>, we studied the restriction profile of fSAM and bSAM against different primate The Journal of biological chemistryThe C-terminal domain of feline and bovine SAMHD1 proteins has a crucial role in lentiviral restriction.PMC71053222018ZX10731101–002–003BX201801242018M6417862017TD-0531270807Wu JZhang KYu BWang CZhang YWang SZhang XMeng LGai YYu XSong YfalseThe C-terminal domain of feline and bovine SAMHD1 proteins has a crucial role in lentiviral restriction.SAM and HD domain-containing protein 1 (SAMHD1) is a host factor that restricts reverse transcription of lentiviruses such as HIV in myeloid cells and resting T cells through its dNTP triphosphohydrolase (dNTPase) activity. Lentiviruses counteract this restriction by expressing the accessory protein Vpx or Vpr, which targets SAMHD1 for proteasomal degradation. SAMHD1 is conserved among mammals, and the feline and bovine SAMHD1 proteins (fSAM and bSAM) restrict lentiviruses by reducing cellular dNTP concentrations. However, the functional regions of fSAM and bSAM that are required for their biological functions are not well-characterized. Here, to establish alternative models to investigate SAMHD1 <i>in vivo</i>, we studied the restriction profile of fSAM and bSAM against different primate 2020-01-01T00:00:00Z2020 Mar2026-05-02T13:44:41.363Z2022-02-09T08:12:36.854ZS-EPMC71053223207591110.1074/jbc.RA120.01276710.1074/jbc.ra120.012767