{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,29]],"date-time":"2026-03-29T01:14:38Z","timestamp":1774746878171,"version":"3.50.1"},"reference-count":48,"publisher":"Oxford University Press (OUP)","issue":"9","license":[{"start":{"date-parts":[[2008,5,1]],"date-time":"2008-05-01T00:00:00Z","timestamp":1209600000000},"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":[[2008,5,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Immunohistochemical detection of increased levels of protein-associated nitrotyrosine has become widely used as a surrogate marker of in situ inflammation. However, the potential consequences of protein-associated nitrotyrosine formation in terms of cellular immune recognition has received surprisingly little attention. Using a well-defined I-EK-restricted epitope of pigeon cytochrome c, we previously demonstrated that conversion of a single tyrosine residue to nitrotyrosine can have a profound effect on recognition by CD4 T cells. In this study, we used the MHC class I-restricted epitope of lymphocytic choriomeningitis virus glycoprotein (gp33) to demonstrate that conversion of tyrosine to nitrotyrosine can also profoundly affect recognition of MHC class I-restricted epitopes. Conversion of the Y4 residue of the gp33 epitope to nitrotyrosine completely abrogated recognition by gp33-specific T cells from P14 TCR-transgenic mice. In contrast, CD8+ T cells specific for \u201cnitrated gp33\u201d (NY-gp33) can be readily elicited in C57BL\/6 mice after immunization with NY-gp33 peptide. Interestingly, T-T hybridomas specific for NY-gp33 peptide were found to fall into two distinct subsets, being specific for NY-gp33 presented in the context of either H-2Db or H-2Kb. This latter result is surprising in light of previous structural studies showing that Y4 comprises a critical TCR-contact residue when presented by H-2Db but that the same residue points downward into the peptide-binding groove of the MHC when presented by H-2Kb. Together, these results indicate that nitrotyrosine formation can impact T cell recognition both directly, through alteration of TCR-contact residues, or indirectly, through alterations in MHC-contact positions.<\/jats:p>","DOI":"10.4049\/jimmunol.180.9.5956","type":"journal-article","created":{"date-parts":[[2014,4,23]],"date-time":"2014-04-23T19:58:20Z","timestamp":1398283100000},"page":"5956-5962","source":"Crossref","is-referenced-by-count":49,"title":["Conversion of Tyrosine to the Inflammation-Associated Analog 3\u2032-Nitrotyrosine at Either TCR- or MHC-Contact Positions Can Profoundly Affect Recognition of the MHC Class I-Restricted Epitope of Lymphocytic Choriomeningitis Virus Glycoprotein 33 by CD8 T Cells"],"prefix":"10.1093","volume":"180","author":[{"given":"Lani L","family":"Hardy","sequence":"first","affiliation":[{"name":"Trev and Joyce Deeley Research Centre, British Columbia Cancer Agency , Victoria, British Columbia ,","place":["Canada"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Darin A","family":"Wick","sequence":"additional","affiliation":[{"name":"Trev and Joyce Deeley Research Centre, British Columbia Cancer Agency , Victoria, British Columbia ,","place":["Canada"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John R","family":"Webb","sequence":"additional","affiliation":[{"name":"Trev and Joyce Deeley Research Centre, British Columbia Cancer Agency , Victoria, British Columbia ,","place":["Canada"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2008,5,1]]},"reference":[{"key":"2026012809271047000_R1","first-page":"315","volume-title":"Physiol. 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