Evidence map›Paper›PMID 31927483›Full record

ArticleiScience2020

Structure of HIV-2 Nef Reveals Features Distinct from HIV-1 Involved in Immune Regulation.

Kengo Hirao, Sophie Andrews, Kimiko Kuroki, Hiroki Kusaka, Takashi Tadokoro, Shunsuke Kita, Toyoyuki Ose, Sarah L Rowland-Jones, Katsumi Maenaka

Open access · goldAbstract read
In one paragraph

Article in iScience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 26% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 12 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Kengo HiraoFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Sophie AndrewsNuffield Department of Medicine, University of Oxford, NDM Research Building, Oxford OX3 7FZ, UK.
Kimiko KurokiFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Hiroki KusakaFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Takashi TadokoroFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Shunsuke KitaFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Toyoyuki OseFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan; Faculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan.
Sarah L Rowland-JonesNuffield Department of Medicine, University of Oxford, NDM Research Building, Oxford OX3 7FZ, UK. Electronic address: sarah.rowland-jones@ndm.ox.ac.uk.
Katsumi MaenakaFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan. Electronic address: maenaka@pharm.hokudai.ac.jp.
Hokkaido University · JPUniversity of Oxford · GBHokkaido University of Science · JP

Funding

Medical Research Council MC_U190085854Medical Research Council MR/S020616/1
6 · The paper itself

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.

Indexed as

3D Reconstruction of ProteinBiochemistryProtein Structure AspectsStructural BiologyThree-Dimensional Reconstruction of Biomoleculair Structures

Identifiers

PMID31927483
PMCPMC6956826
OpenAlexW2993767766

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.