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Structure of HIV-2 Nef Reveals Features Distinct from HIV-1 Involved in Immune Regulation
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Title: | Structure of HIV-2 Nef Reveals Features Distinct from HIV-1 Involved in Immune Regulation |
Authors: | Hirao, Kengo Browse this author | Andrews, Sophie Browse this author | Kuroki, Kimiko Browse this author →KAKEN DB | Kusaka, Hiroki Browse this author | Tadokoro, Takashi Browse this author →KAKEN DB | Kita, Shunsuke Browse this author | Ose, Toyoyuki Browse this author | Rowland-Jones, Sarah L. Browse this author | Maenaka, Katsumi Browse this author →KAKEN DB |
Issue Date: | 24-Jan-2020 |
Publisher: | Cell Press |
Journal Title: | iScience |
Volume: | 23 |
Issue: | 1 |
Start Page: | 100758 |
Publisher DOI: | 10.1016/j.isci.2019.100758 |
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 alpha-helix, absent from HIV-1. We further determined the structure of simian immunodeficiency virus (SIV) Nef harboring this region, demonstrating similar C-terminal a-helix, which may contribute to AP-1 binding for MHC-I downregulation. These results provide insights into the distinct pathogenesis of HIV-2 infection. |
Rights: | https://creativecommons.org/licenses/by-nc-nd/4.0/ |
Type: | article |
URI: | http://hdl.handle.net/2115/76924 |
Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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