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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.
Type: article
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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