{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,18]],"date-time":"2025-10-18T10:42:26Z","timestamp":1760784146883,"version":"3.38.0"},"reference-count":53,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2016,8,1]],"date-time":"2016-08-01T00:00:00Z","timestamp":1470009600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2016,8,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>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-\u00c5 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.<\/jats:p>","DOI":"10.4049\/jimmunol.1600541","type":"journal-article","created":{"date-parts":[[2016,7,7]],"date-time":"2016-07-07T01:31:02Z","timestamp":1467855062000},"page":"1399-1407","source":"Crossref","is-referenced-by-count":13,"title":["Structure of the Adenovirus Type 4 (Species E) E3-19K\/HLA-A2 Complex Reveals Species-Specific Features in MHC Class I Recognition"],"prefix":"10.1093","volume":"197","author":[{"given":"Lenong","family":"Li","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, College of Medicine, University of Illinois , Chicago, IL 60612"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9032-9699","authenticated-orcid":false,"given":"Bernard D","family":"Santarsiero","sequence":"additional","affiliation":[{"name":"Department of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, University of Illinois , Chicago, IL 60612"},{"name":"Center for Biomolecular Sciences, College of Pharmacy, University of Illinois , Chicago, IL 60607"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marlene","family":"Bouvier","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, College of Medicine, University of Illinois , Chicago, IL 60612"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2016,8,15]]},"reference":[{"key":"2025030617473307700_r1","first-page":"191","article-title":"Molecular epidemiology of human adenoviruses","volume":"110","author":"Wadell","year":"1984","journal-title":"Curr. 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