Evidence map›Paper›PMID 26068188›Full record

ArticleThe Journal of general virology2015

VP22 core domain from Herpes simplex virus 1 reveals a surprising structural conservation in both the Alpha- and Gammaherpesvirinae subfamilies.

Kelly Hew, Sue-Li Dahlroth, Lucy Xin Pan, Tobias Cornvik, Pär Nordlund

Open access · hybridAbstract read
In one paragraph

Article in The Journal of general virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Structural basis of higher order oligomerization of KSHV inhibitor of cGAS.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  8. Article
  9. Evasion of Intracellular DNA Sensing by Human Herpesviruses.Frontiers in cellular and infection microbiology · 2021
    Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Viral evasion of DNA-stimulated innate immune responses.Cellular & molecular immunology · 2017
    Review
  18. Article
  19. Article
  20. Review
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

5 authors at 1 institution in 2 countries.

Kelly HewDivision of Structural Biology and Biochemistry, School of Biological Sciences, Nanyang Technological University, 138673, Singapore.
Sue-Li DahlrothDivision of Structural Biology and Biochemistry, School of Biological Sciences, Nanyang Technological University, 138673, Singapore.
Lucy Xin PanDivision of Structural Biology and Biochemistry, School of Biological Sciences, Nanyang Technological University, 138673, Singapore.
Tobias CornvikDivision of Structural Biology and Biochemistry, School of Biological Sciences, Nanyang Technological University, 138673, Singapore.
Pär NordlundDivision of Biophysics, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm 171 11, Sweden.
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The viral tegument is a layer of proteins between the herpesvirus capsid and its outer envelope. According to phylogenetic studies, only a third of these proteins are conserved amongst the three subfamilies (Alpha-, Beta- and Gammaherpesvirinae) of the family Herpesviridae. Although some of these tegument proteins have been studied in more detail, the structure and function of the majority of them are still poorly characterized. VP22 from Herpes simplex virus 1 (subfamily Alphaherpesvirinae) is a highly interacting tegument protein that has been associated with tegument assembly. We have determined the crystal structure of the conserved core domain of VP22, which reveals an elongated dimer with several potential protein-protein interaction regions and a peptide-binding site. The structure provides us with the structural basics to understand the numerous functional mutagenesis studies of VP22 found in the literature. It also establishes an unexpected structural homology to the tegument protein ORF52 from Murid herpesvirus 68 (subfamily Gammaherpesvirinae). Homologues for both VP22 and ORF52 have been identified in their respective subfamilies. Although there is no obvious sequence overlap in the two subfamilies, this structural conservation provides compelling structural evidence for shared ancestry and functional conservation.

Indexed as

Conserved SequenceCrystallography, X-RayHerpesvirus 1, HumanModels, MolecularProtein ConformationRhadinovirusViral Structural Proteinsherpes simplex virus type 1 protein VP22Viral Structural Proteins

Identifiers

PMID26068188
PMCPMC4635490
OpenAlexW1872428189

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.