Evidence map›Paper›PMID 23115291›Full record

ArticleJournal of virology2013

Crystal structure of the cowpox virus-encoded NKG2D ligand OMCP.

Eric Lazear, Lance W Peterson, Chris A Nelson, Daved H Fremont

Abstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Review
  2. Review
  3. A comprehensive review of monkeypox virus and mpox characteristics.Frontiers in cellular and infection microbiology · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Cowpox virus encodes a protein that binds B7.1 and B7.2 and subverts T cell costimulation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. 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

4 authors.

Eric LazearDepartment of Pathology and Immunology, Washington University in St. Louis, St. Louis, MO, USA.
Lance W Peterson
Chris A Nelson
Daved H Fremont

Funding

Virology and Smallpox VaccinationsU54AI057160 · NIAID · WASHINGTON UNIVERSITY · PI RAY, RANJIT · 2003 to 2013
$80.9M
MHC-I regulation by herpes virusR01AI019687 · NIAID · WASHINGTON UNIVERSITY · PI FREMONT, DAVED H. · 1985 to 2016
$5.2M
INNATE IMMUNE RECEPTOR ANTAGONISM BY ORTHOPOXVIRUS PROTEINSR01AI073552 · NIAID · WASHINGTON UNIVERSITY · PI FRENCH, ANTHONY R · 2008 to 2011
$1.5M
NIAID NIH HHS HHSN272200700058CNIAID NIH HHS HHSN272201200026CNIAID NIH HHS R01 AI019687NIAID NIH HHS R01 AI073552NIAID NIH HHS U54 AI057160
6 · The paper itself

Abstract

The NKG2D receptor is expressed on the surface of NK, T, and macrophage lineage cells and plays an important role in antiviral and antitumor immunity. To evade NKG2D recognition, herpesviruses block the expression of NKG2D ligands on the surface of infected cells using a diverse repertoire of sabotage methods. Cowpox and monkeypox viruses have taken an alternate approach by encoding a soluble NKG2D ligand, the orthopoxvirus major histocompatibility complex (MHC) class I-like protein (OMCP), which can block NKG2D-mediated cytotoxicity. This approach has the advantage of targeting a single conserved receptor instead of numerous host ligands that exhibit significant sequence diversity. Here, we show that OMCP binds the NKG2D homodimer as a monomer and competitively blocks host ligand engagement. We have also determined the 2.25-Å-resolution crystal structure of OMCP from the cowpox virus Brighton Red strain, revealing a truncated MHC class I-like platform domain consisting of a beta sheet flanked with two antiparallel alpha helices. OMCP is generally similar in structure to known host NKG2D ligands but has notable variations in regions typically used to engage NKG2D. Additionally, the determinants responsible for the 14-fold-higher affinity of OMCP for human than for murine NKG2D were mapped to a single loop in the NKG2D ligand-binding pocket.

Indexed as

Amino Acid SequenceAnimalsCowpox virusCrystallography, X-RayHumansMiceModels, MolecularMolecular Sequence DataNK Cell Lectin-Like Receptor Subfamily KProtein BindingProtein Structure, QuaternarySequence Homology, Amino AcidViral ProteinsNK Cell Lectin-Like Receptor Subfamily KViral Proteins

Identifiers

PMID23115291
PMCPMC3554055

What OpenQuestion holds

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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.