<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Bergmann T</submitter><funding>NIAID NIH HHS</funding><funding>PHS HHS</funding><pagination>675-89</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4783141</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>67(11-12)</volume><pubmed_abstract>Here we describe a detailed quantitative peptide-binding motif for the common equine leukocyte antigen (ELA) class I allele Eqca-1*00101, present in roughly 25 % of Thoroughbred horses. We determined a preliminary binding motif by sequencing endogenously bound ligands. Subsequently, a positional scanning combinatorial library (PSCL) was used to further characterize binding specificity and derive a quantitative motif involving aspartic acid in position 2 and hydrophobic residues at the C-terminus. Using this motif, we selected and tested 9- and 10-mer peptides derived from the equine herpesvirus type 1 (EHV-1) proteome for their capacity to bind Eqca-1*00101. PSCL predictions were very efficient, with an receiver operating characteristic (ROC) curve performance of 0.877, and 87 peptides der</pubmed_abstract><journal>Immunogenetics</journal><pubmed_title>The common equine class I molecule Eqca-1*00101 (ELA-A3.1) is characterized by narrow peptide binding and T cell epitope repertoires.</pubmed_title><pmcid>PMC4783141</pmcid><funding_grant_id>HHSN272200900042C</funding_grant_id><funding_grant_id>R01AI112566</funding_grant_id><funding_grant_id>AI 033993</funding_grant_id><funding_grant_id>R01 AI112566</funding_grant_id><funding_grant_id>U19 AI090023</funding_grant_id><funding_grant_id>HHSN272201400045C</funding_grant_id><funding_grant_id>R37 AI033993</funding_grant_id><funding_grant_id>R01 AI033993</funding_grant_id><funding_grant_id>U19AI090023</funding_grant_id><pubmed_authors>Osterrieder N</pubmed_authors><pubmed_authors>Bergmann T</pubmed_authors><pubmed_authors>Peters B</pubmed_authors><pubmed_authors>Sette A</pubmed_authors><pubmed_authors>Hunt DF</pubmed_authors><pubmed_authors>Wriston A</pubmed_authors><pubmed_authors>Tallmadge R</pubmed_authors><pubmed_authors>Sidney J</pubmed_authors><pubmed_authors>Oseroff C</pubmed_authors><pubmed_authors>Antczak DF</pubmed_authors><pubmed_authors>Shabanowitz J</pubmed_authors><pubmed_authors>Moore C</pubmed_authors><pubmed_authors>Miller D</pubmed_authors><pubmed_authors>Harman RM</pubmed_authors></additional><is_claimable>false</is_claimable><name>The common equine class I molecule Eqca-1*00101 (ELA-A3.1) is characterized by narrow peptide binding and T cell epitope repertoires.</name><description>Here we describe a detailed quantitative peptide-binding motif for the common equine leukocyte antigen (ELA) class I allele Eqca-1*00101, present in roughly 25 % of Thoroughbred horses. We determined a preliminary binding motif by sequencing endogenously bound ligands. Subsequently, a positional scanning combinatorial library (PSCL) was used to further characterize binding specificity and derive a quantitative motif involving aspartic acid in position 2 and hydrophobic residues at the C-terminus. Using this motif, we selected and tested 9- and 10-mer peptides derived from the equine herpesvirus type 1 (EHV-1) proteome for their capacity to bind Eqca-1*00101. PSCL predictions were very efficient, with an receiver operating characteristic (ROC) curve performance of 0.877, and 87 peptides der</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015 Nov</publication><modification>2025-04-05T11:56:43.914Z</modification><creation>2019-03-27T02:10:40Z</creation></dates><accession>S-EPMC4783141</accession><cross_references><pubmed>26399241</pubmed><doi>10.1007/s00251-015-0872-z</doi></cross_references></HashMap>