{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Valkenburg SA"],"funding":["NIAID NIH HHS"],"pagination":["5570-5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3619348"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["110(14)"],"pubmed_abstract":["A reverse-genetics approach has been used to probe the mechanism underlying immune escape for influenza A virus-specific CD8(+) T cells responding to the immunodominant D(b)NP366 epitope. Engineered viruses with a substitution at a critical residue (position 6, P6M) all evaded recognition by WT D(b)NP366-specific CD8(+) T cells, but only the NPM6I and NPM6T mutants altered the topography of a key residue (His155) in the MHC class I binding site. Following infection with the engineered NPM6I and NPM6T influenza viruses, both mutations were associated with a substantial \"hole\" in the naïve T-cell receptor repertoire, characterized by very limited T-cell receptor diversity and minimal primary responses to the NPM6I and NPM6T epitopes. Surprisingly, following respiratory challenge with a serol"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Preemptive priming readily overcomes structure-based mechanisms of virus escape."],"pmcid":["PMC3619348"],"funding_grant_id":["AI170251"],"pubmed_authors":["Purcell AW","Doherty PC","Bird NA","Rossjohn J","Gras S","Jackson DC","Turner SJ","Valkenburg SA","Twist KA","Halim H","Guillonneau C","Hatton LA","Kedzierska K"],"additional_accession":[]},"is_claimable":false,"name":"Preemptive priming readily overcomes structure-based mechanisms of virus escape.","description":"A reverse-genetics approach has been used to probe the mechanism underlying immune escape for influenza A virus-specific CD8(+) T cells responding to the immunodominant D(b)NP366 epitope. Engineered viruses with a substitution at a critical residue (position 6, P6M) all evaded recognition by WT D(b)NP366-specific CD8(+) T cells, but only the NPM6I and NPM6T mutants altered the topography of a key residue (His155) in the MHC class I binding site. Following infection with the engineered NPM6I and NPM6T influenza viruses, both mutations were associated with a substantial \"hole\" in the naïve T-cell receptor repertoire, characterized by very limited T-cell receptor diversity and minimal primary responses to the NPM6I and NPM6T epitopes. Surprisingly, following respiratory challenge with a serol","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Apr","modification":"2026-05-01T20:55:37.208Z","creation":"2026-04-07T17:14:57.248Z"},"accession":"S-EPMC3619348","cross_references":{"pubmed":["23493558"],"doi":["10.1073/pnas.1302935110"]}}