Evidence map›Paper›PMID 21237475›Full record

ArticleVirology2011

BST-2 is rapidly down-regulated from the cell surface by the HIV-1 protein Vpu: evidence for a post-ER mechanism of Vpu-action.

Mark Skasko, Andrey Tokarev, Cheng-Chang Chen, Wolfgang B Fischer, Satish K Pillai, John Guatelli

Open access · greenAbstract read
In one paragraph

Article in Virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

42 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  5. Review
  6. Medical sciences (Basel, Switzerland) · 2019
    Article
  7. Article
  8. Review
  9. Article
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  13. Article
  14. Tetherin antagonism by Vpu protects HIV-infected cells from antibody-dependent cell-mediated cytotoxicity.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. HIV-1 Vpu - an ion channel in search of a job.Biochimica et biophysica acta · 2014
    Review
  16. Review
  17. Article
  18. Article
  19. Article
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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

6 authors at 3 institutions in 2 countries.

Mark SkaskoDepartment of Pathology, University of California-San Diego, La Jolla, CA 92093-0679, USA. mskasko@ucsd.edu
Andrey Tokarev
Cheng-Chang Chen
Wolfgang B Fischer
Satish K Pillai
John Guatelli
University of California San Diego · USNational Yang Ming Chiao Tung University · TWUniversity of California, San Francisco · US

Funding

HOPE Training GrantT32AI007384 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Sara Gianella Weibel, Scott L Letendre · 1990 to 2026
$9.7M
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
Antiviral Role of APOBEC3 in HIV/HCV Coinfected PatientsK01DA024654 · NIDA · VITALANT · PI PILLAI, SATISH KUMAR · 2008 to 2012
$902k
NIAID NIH HHS AI081668NIAID NIH HHS R01 AI081668NIAID NIH HHS R37 AI081668NIAID NIH HHS T32 AI007384NIAID NIH HHS T32AI007384NIDA NIH HHS K01 DA024654
6 · The paper itself

Abstract

Recent evidence suggests that transmembrane domain (TMD) interactions are essential for HIV-1 Vpu-mediated antagonism of the restriction factor BST-2/tetherin. We made Vpu TMD mutants to study the mechanism of BST-2 antagonism. Vpu-I17A, -A18F, -W22L, and -S23L co-localized with BST-2 within endosomal membranes while effectively enhancing virion release and down-regulating surface BST-2. However, Vpu-A18H was confined to an endoplasmic reticulum (ER)-like distribution, resulting in impaired down-regulation of BST-2 and reduced virion release. Brefeldin A confined wild type Vpu to the ER, resulting in a similarly impaired phenotype, as did the addition of a C-terminal ER-retention signal to Vpu. We determined the half-life of cell-surface BST-2 to be ~8 hours, whereas Vpu mediated an ~80% reduction of surface BST-2 within 6 hours, suggesting that TMD interactions between Vpu and BST-2 occur within post-ER membranes to directly and rapidly remove BST-2 from the cell surface and relieve restricted virion release.

Indexed as

Host-Pathogen InteractionsAmino Acid SubstitutionAntigens, CDBone Marrow Stromal Antigen 2Down-RegulationEndoplasmic ReticulumEndosomesGPI-Linked ProteinsHeLa CellsHIV-1Human Immunodeficiency Virus ProteinsHumansIntracellular MembranesMutagenesis, Site-DirectedMutant ProteinsViral Regulatory and Accessory ProteinsAntigens, CDBone Marrow Stromal Antigen 2BST2 protein, humanGPI-Linked ProteinsHuman Immunodeficiency Virus ProteinsMutant ProteinsViral Regulatory and Accessory ProteinsViroporin Proteinsvpu protein, Human immunodeficiency virus 1

Identifiers

PMID21237475
PMCPMC3086044
OpenAlexW2141030267

What OpenQuestion holds

Textmetadata
LicenceTDM
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.