A Dataset of Experimental HLA-B*2705 Peptide Binding Affinities. (27th April 2014)

• Record Type: Journal Article
• Authors: Walshe, Valerie A.; Hattotuwagama, Channa K.; Doytchinova, Irini A.; Flower, Darren R.
• Other Names: Šarić T. Academic Editor.; Tung C.-W. Academic Editor.
• Is Part Of: Dataset papers in science. Volume 2014(2014)
• Publication Date: 2014-04-27
• Subjects: Science -- Periodicals; Medicine -- Periodicals; Biology -- Periodicals; Biology; Medicine; Science; Electronic journals; Electronic journals; Periodicals; 500
• DOI: 10.1155/2014/914684
• Languages: English
• ISSNs: 2314-8497

Abstract

Abstract : 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− log 10 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.