Evidence map›Paper›PMID 19929170›Full record

ReviewAIDS research and human retroviruses2009

Antiviral activity of the interferon-induced cellular protein BST-2/tetherin.

Andrey Tokarev, Mark Skasko, Kathleen Fitzpatrick, John Guatelli

Open access · greenAbstract readReview
In one paragraph

Review in AIDS research and human retroviruses, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

65 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
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  3. Review
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  14. Medical sciences (Basel, Switzerland) · 2019
    Article
  15. Article
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  19. Review
  20. Article

5 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Andrey TokarevDepartment of Medicine, University of California San Diego, California 92093-0679, USA.
Mark Skasko
Kathleen Fitzpatrick
John Guatelli
VA San Diego Healthcare System · 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
NIAID NIH HHS AI081668NIAID NIH HHS R01 AI081668NIAID NIH HHS T32AI007384PHS HHS RP41004050
6 · The paper itself

Abstract

Pathogenic microorganisms encode proteins that antagonize specific aspects of innate or adaptive immunity. Just as the study of the HIV-1 accessory protein Vif led to the identification of cellular cytidine deaminases as host defense proteins, the study of HIV-1 Vpu recently led to the discovery of the interferon-induced transmembrane protein BST-2 (CD317; tetherin) as a novel component of the innate defense against enveloped viruses. BST-2 is an unusually structured protein that restricts the release of fully formed progeny virions from infected cells, presumably by a direct retention mechanism that is independent of any viral protein target. Its spectrum of activity includes at least four virus families: retroviruses, filoviruses, arenaviruses, and herpesviruses. Viral antagonists of BST-2 include HIV-1 Vpu, HIV-2 and SIV Env, SIV Nef, the Ebola envelope glycoprotein, and the K5 protein of KSHV. The mechanisms of antagonism are diverse and currently include viral cooption of cellular endosomal trafficking and protein degradation pathways, including those mediated by ubiquitination. Orthologs of human BST-2 are present in mammals. Primate BST-2 proteins are differentially sensitive to antagonism by lentiviral Vpu and Nef proteins, suggesting that BST-2 has subjected lentiviruses to evolutionary pressure and presents barriers to cross-species transmission. BST-2 functions not only as an effector of the interferon-induced antiviral response but also as a negative feedback regulator of interferon production by plasmacytoid dendritic cells. Future work will focus on the role and regulation of BST-2 during the innate response to viral infection, on the mechanisms of restriction and of antagonism by viral gene products, and on the role of BST-2 in primate lentiviral evolution. The augmentation of BST-2 activity and the inhibition of virally encoded antagonists, in particular Vpu, represent new approaches to the prevention and treatment of HIV-1 infection.

Indexed as

HIV-1AnimalsAntigens, CDBone Marrow Stromal Antigen 2Dendritic CellsGene Expression RegulationGPI-Linked ProteinsHIV InfectionsHuman Immunodeficiency Virus ProteinsHumansInterferonsMembrane GlycoproteinsUbiquitin-Protein Ligase ComplexesViral Regulatory and Accessory ProteinsViroporin ProteinsAntigens, CDBone Marrow Stromal Antigen 2BST2 protein, humanGPI-Linked ProteinsHuman Immunodeficiency Virus ProteinsInterferonsMembrane GlycoproteinsUbiquitin-Protein Ligase ComplexesViral Regulatory and Accessory ProteinsViroporin Proteinsvpu protein, Human immunodeficiency virus 1

Identifiers

PMID19929170
PMCPMC2858902
OpenAlexW1965735010

What OpenQuestion holds

Textmetadata
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.