Evidence map›Paper›PMID 20019814›Full record

ArticlePLoS pathogens2009

BCA2/Rabring7 promotes tetherin-dependent HIV-1 restriction.

Kei Miyakawa, Akihide Ryo, Tsutomu Murakami, Kenji Ohba, Shoji Yamaoka, Mitsunori Fukuda, John Guatelli, Naoki Yamamoto

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed, 1 pooled it
3.3field-weighted citation impact, top 7% 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

60 citing papers in PubMed, 1 synthesis or guideline pooled it, 91 citations in OpenAlex.

  1. Pooled it
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  5. Article
  6. Article
  7. The RING finger protein family in health and disease.Signal transduction and targeted therapy · 2022
    Review
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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

8 authors at 4 institutions in 2 countries.

Kei MiyakawaAIDS Research Center, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo, Japan.
Akihide Ryo
Tsutomu Murakami
Kenji Ohba
Shoji Yamaoka
Mitsunori Fukuda
John Guatelli
Naoki Yamamoto
National Institute of Infectious Diseases · JPTohoku University · JPTokyo Medical and Dental University · JPUniversity of California, San Diego · US

Funding

HIV-1 Vpu and BST-2/CD317R37AI081668 · NIAID · VETERANS MEDICAL RESEARCH FDN/SAN DIEGO · PI GUATELLI, JOHN C. · 2014 to 2023
$4.8M
HIV-1 Vpu and BST-2/CD317R01AI081668 · NIAID · VETERANS MEDICAL RESEARCH FDN/SAN DIEGO · PI GUATELLI, JOHN C. · 2009 to 2013
$2.1M
NIAID NIH HHS AI081668NIAID NIH HHS R01 AI081668NIAID NIH HHS R37 AI081668
6 · The paper itself

Abstract

Host cell factors can either positively or negatively regulate the assembly and egress of HIV-1 particles from infected cells. Recent reports have identified a previously uncharacterized transmembrane protein, tetherin/CD317/BST-2, as a crucial host restriction factor that acts during a late budding step in HIV-1 replication by inhibiting viral particle release. Although tetherin has been shown to promote the retention of nascent viral particles on the host cell surface, the precise molecular mechanisms that occur during and after these tethering events remain largely unknown. We here report that a RING-type E3 ubiquitin ligase, BCA2 (Breast cancer-associated gene 2; also called Rabring7, ZNF364 or RNF115), is a novel tetherin-interacting host protein that facilitates the restriction of HIV-1 particle production in tetherin-positive cells. The expression of human BCA2 in "tetherin-positive" HeLa, but not in "tetherin-negative" HOS cells, resulted in a strong restriction of HIV-1 particle production. Upon the expression of tetherin in HOS cells, BCA2 was capable of inhibiting viral particle production as in HeLa cells. The targeted depletion of endogenous BCA2 by RNA interference (RNAi) in HeLa cells reduced the intracellular accumulation of viral particles, which were nevertheless retained on the plasma membrane. BCA2 was also found to facilitate the internalization of HIV-1 virions into CD63(+) intracellular vesicles leading to their lysosomal degradation. These results indicate that BCA2 accelerates the internalization and degradation of viral particles following their tethering to the cell surface and is a co-factor or enhancer for the tetherin-dependent restriction of HIV-1 release from infected cells.

Indexed as

Antigens, CDBone Marrow Stromal Antigen 2Cell LineEndocytosisGPI-Linked ProteinsHIV-1HumansImmunity, InnateLysosomesMembrane GlycoproteinsUbiquitin-Protein LigasesVirionVirus ReplicationAntigens, CDBone Marrow Stromal Antigen 2BST2 protein, humanGPI-Linked ProteinsMembrane GlycoproteinsRNF115 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID20019814
PMCPMC2788703
OpenAlexW2091495168

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.