Evidence map›Paper›PMID 21084286›Full record

ArticleThe Journal of biological chemistry2011

Structural and biophysical analysis of BST-2/tetherin ectodomains reveals an evolutionary conserved design to inhibit virus release.

Melissa Swiecki, Suzanne M Scheaffer, Marc Allaire, Daved H Fremont, Marco Colonna, Tom J Brett

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.5field-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

51 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Review
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  6. Article
  7. A CRISPR-Cas Cure for HIV/AIDS.International journal of molecular sciences · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Multi-functional BST2/tetherin against HIV-1, other viruses and LINE-1.Frontiers in cellular and infection microbiology · 2022
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Limiting Respiratory Viral Infection by Targeting Antiviral and Immunological Functions of BST-2/Tetherin: Knowledge and Gaps.BioEssays : news and reviews in molecular, cellular and developmental biology · 2018
    Review
  18. Article
  19. Review
  20. 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

6 authors at 3 institutions in 2 countries.

Melissa SwieckiDepartment of Pathology and Immunology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Suzanne M Scheaffer
Marc Allaire
Daved H Fremont
Marco Colonna
Tom J Brett
Washington University in St. Louis · USBrookhaven National Laboratory · USInstitute of Molecular Biology and Biophysics · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

BST-2/tetherin is a host antiviral molecule that functions to potently inhibit the release of enveloped viruses from infected cells. In return, viruses have evolved antagonists to this activity. BST-2 traps budding virions by using two separate membrane-anchoring regions that simultaneously incorporate into the host and viral membranes. Here, we detailed the structural and biophysical properties of the full-length BST-2 ectodomain, which spans the two membrane anchors. The 1.6-Å crystal structure of the complete mouse BST-2 ectodomain reveals an ∼145-Å parallel dimer in an extended α-helix conformation that predominantly forms a coiled coil bridged by three intermolecular disulfides that are required for stability. Sequence analysis in the context of the structure revealed an evolutionarily conserved design that destabilizes the coiled coil, resulting in a labile superstructure, as evidenced by solution x-ray scattering displaying bent conformations spanning 150 and 180 Å for the mouse and human BST-2 ectodomains, respectively. Additionally, crystal packing analysis revealed possible curvature-sensing tetrameric structures that may aid in proper placement of BST-2 during the genesis of viral progeny. Overall, this extended coiled-coil structure with inherent plasticity is undoubtedly necessary to accommodate the dynamics of viral budding while ensuring separation of the anchors.

Indexed as

Evolution, MolecularAnimalsAntigens, CDBone Marrow Stromal Antigen 2Crystallography, X-RayGPI-Linked ProteinsHEK293 CellsHumansMembrane GlycoproteinsMiceProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryVirusesVirus ReleaseAntigens, CDBone Marrow Stromal Antigen 2BST2 protein, humanBST2 protein, mouseGPI-Linked ProteinsMembrane Glycoproteins

Identifiers

PMID21084286
PMCPMC3024793
OpenAlexW2065865744

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.