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• W2993767766 abstract "The human immunodeficiency virus (HIV) accessory protein Nef plays a major role in establishing and maintaining infection, particularly through immune evasion. Many HIV-2-infected people experience long-term viral control and survival, resembling HIV-1 elite control. HIV-2 Nef has overlapping but also distinct functions from HIV-1 Nef. Here we report the crystal structure of HIV-2 Nef core. The di-leucine sorting motif forms a helix bound to neighboring molecules, and moreover, isothermal titration calorimetry demonstrated that the CD3 endocytosis motif can directly bind to HIV-2 Nef, ensuring AP-2-mediated endocytosis for CD3. The highly conserved C-terminal region forms a α-helix, absent from HIV-1. We further determined the structure of simian immunodeficiency virus (SIV) Nef harboring this region, demonstrating similar C-terminal α-helix, which may contribute to AP-1 binding for MHC-I downregulation. These results provide insights into the distinct pathogenesis of HIV-2 infection." @default.
• W2993767766 created "2019-12-13" @default.
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• W2993767766 date "2020-01-01" @default.
• W2993767766 modified "2023-10-13" @default.
• W2993767766 title "Structure of HIV-2 Nef Reveals Features Distinct from HIV-1 Involved in Immune Regulation" @default.
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• W2993767766 doi "https://doi.org/10.1016/j.isci.2019.100758" @default.
• W2993767766 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6956826" @default.
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