ArticleJournal of immunology (Baltimore, Md. : 1950)2016
Structure of the Adenovirus Type 4 (Species E) E3-19K/HLA-A2 Complex Reveals Species-Specific Features in MHC Class I Recognition.
Article in Journal of immunology (Baltimore, Md. : 1950), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Diverse cytomegalovirus US11 antagonism and MHC-A evasion strategies reveal a tit-for-tat coevolutionary arms race in hominids.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Pediatric adenovirus pneumonia: clinical practice and current treatment.Frontiers in medicine · 2023Review
- Human adenovirus DNA polymerase is evolutionarily and functionally associated with human telomerase reverse transcriptase based onFrontiers in bioinformatics · 2023Article
- Article
- Viruses, cancer and non-self recognition.Open biology · 2021Review
- Immune evasion by adenoviruses: a window into host-virus adaptation.FEBS letters · 2019Review
- HLA-B locus products resist degradation by the human cytomegalovirus immunoevasin US11.PLoS pathogens · 2019Article
- Discovery of small molecule inhibitors of adenovirus by disrupting E3-19K/HLA-A2 interactions.Bioorganic & medicinal chemistry letters · 2018Article
- Article
- Deep analysis of Loop L1 HVRs1-4 region of the hexon gene of adenovirus field strains isolated in Poland.PloS one · 2018Article
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Authors and funding
3 authors.
Funding
Abstract
Adenoviruses (Ads) subvert MHC class I Ag presentation and impair host anti-Ad cellular activities. Specifically, the Ad-encoded E3-19K immunomodulatory protein targets MHC class I molecules for retention within the endoplasmic reticulum of infected cells. We report the x-ray crystal structure of the Ad type 4 (Ad4) E3-19K of species E bound to HLA-A2 at 2.64-Å resolution. Structural analysis shows that Ad4 E3-19K adopts a tertiary fold that is shared only with Ad2 E3-19K of species C. A comparative analysis of the Ad4 E3-19K/HLA-A2 structure with our x-ray structure of Ad2 E3-19K/HLA-A2 identifies species-specific features in HLA-A2 recognition. Our analysis also reveals common binding characteristics that explain the promiscuous, and yet high-affinity, association of E3-19K proteins with HLA-A and HLA-B molecules. We also provide structural insights into why E3-19K proteins do not associate with HLA-C molecules. Overall, our study provides new information about how E3-19K proteins selectively engage with MHC class I to abrogate Ag presentation and counteract activation of CD8(+) T cells. The significance of MHC class I Ag presentation for controlling viral infections, as well as the threats of viral infections in immunocompromised patients, underline our efforts to characterize viral immunoevasins, such as E3-19K.
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