A Dataset of Experimental HLA-B2705 Peptide Binding Affinities

T-cell epitopes form the basis of many vaccines, diagnostics, and reagents. Current methods for the in silico identification of T-cell epitopes rely, in the main, on the accurate quantitative prediction of peptide-Major Histocompatibility Complex (pMHC) affinity using data-driven computational appro...

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Bibliographic Details
Published inDataset papers in science Vol. 2014; no. 2014; pp. 1 - 4
Main Authors Walshe, Valerie A., Hattotuwagama, Channa K., Doytchinova, Irini A., Flower, Darren R.
Format Journal Article
LanguageEnglish
Published Cairo, Egypt Hindawi Puplishing Corporation 2014
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Summary:T-cell epitopes form the basis of many vaccines, diagnostics, and reagents. Current methods for the in silico identification of T-cell epitopes rely, in the main, on the accurate quantitative prediction of peptide-Major Histocompatibility Complex (pMHC) affinity using data-driven computational approaches. Here, we describe a dataset of experimentally determined pMHC binding affinities for the problematic human class I allele HLA-B*2705. Using an in-house, FACS-based, MHC stabilization assay, we measured binding of 223 peptides. This dataset includes both nonbinding and binding peptides, with measured affinities (expressed as −log10 of the half-maximal binding level) ranging from 1.2 to 7.4. This dataset should provide a useful independent benchmark for new and existing methods for predicting peptide binding to HLA-B*2705.
ISSN:2314-8497