Evidence map›Paper›PMID 26423533›Full record

ArticleScientific reports2015

Inhibition of HIV-1 assembly by coiled-coil domain containing protein 8 in human cells.

Min Wei, Xia Zhao, Mi Liu, Zhi Huang, Yong Xiao, Meijuan Niu, Yiming Shao, Lawrence Kleiman

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed, 1 pooled it
0.5field-weighted citation impact, top 34% 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, 1 synthesis or guideline pooled it, 10 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Cullin-RING E3 Ubiquitin Ligase 7 in Growth Control and Cancer.Advances in experimental medicine and biology · 2020
    Review
  6. Article
  7. Article
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

8 authors at 5 institutions in 2 countries.

Min WeiSchool of Medicine, Nankai University, Tianjin, China, 300071.
Xia ZhaoLady Davis Institute, Jewish General Hospital, McGill University, Canada, H3T 1E2.
Mi LiuState Key Laboratory for Infectious Disease Prevention and Control, National Center for AIDS/STD Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing, China.
Zhi HuangLady Davis Institute, Jewish General Hospital, McGill University, Canada, H3T 1E2.
Yong XiaoLady Davis Institute, Jewish General Hospital, McGill University, Canada, H3T 1E2.
Meijuan NiuLady Davis Institute, Jewish General Hospital, McGill University, Canada, H3T 1E2.
Yiming ShaoSchool of Medicine, Nankai University, Tianjin, China, 300071.
Lawrence KleimanLady Davis Institute, Jewish General Hospital, McGill University, Canada, H3T 1E2.
McGill University · CAJewish General Hospital · CAChinese Center For Disease Control and Prevention · CNNankai University · CNPeking University · CN

Funding

Canadian Institutes of Health Research HOP 81389
6 · The paper itself

Abstract

Human Immunodeficiency Virus type 1 (HIV-1) major structure protein Gag is synthesized in the cytoplasm, assembles on the plasma membrane, subsequently buds and releases. HIV-1 viral particles incorporate a number of host proteins to facilitate or inhibit HIV-1 replication. Here we identify a new host protein, coiled-coil domain containing protein 8 (CCDC8), in HIV-1 particles. Incorporation of CCDC8 into virions is dependent on the interaction between CCDC8 and Gag matrix region. Exogenous overexpression of CCDC8 can strongly inhibit HIV-1 production, up to ~30 fold. CCDC8 is a membrane-associated protein. The interaction between exogenously expressed CCDC8 and Gag on the plasma membrane changes the assembly of Gag, and redirects it into intracellular sites, or causes Gag endocytosis. CCDC8, along with cytoskeleton protein obscuring-like1 (Obsl1) and E3 ligase Cul7, induces Gag polyubiquitination and degradation. Thus we identify a new host protein and a new pathway for HIV-1 Gag polyubiquitination and degradation. This pathway presents potential therapeutic strategies against HIV infection.

Indexed as

Virus AssemblyCarrier ProteinsCell LineCell MembraneCytoplasmEndocytosisgag Gene Products, Human Immunodeficiency VirusGene ExpressionHIV-1HIV InfectionsHumansProtein BindingProtein Processing, Post-TranslationalProtein TransportProteolysisUbiquitinationCarrier ProteinsCCDC8 protein, humangag Gene Products, Human Immunodeficiency Virus

Identifiers

PMID26423533
PMCPMC4589731
OpenAlexW2416944827

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.