Front cover: High‐sensitivity HLA class I peptidome analysis enables a precise definition of peptide motifs and the identification of peptides from cell lines and patients' sera. Issue 10 (11th May 2016)

• Record Type: Journal Article
• Authors: Ritz, Danilo; Gloger, Andreas; Weide, Benjamin; Garbe, Claus; Neri, Dario; Fugmann, Tim
• Is Part Of: Proteomics. Volume 16:Issue 10(2016)
• Page Start: NA
• Page End: NA
• Publication Date: 2016-05-11
• Subjects: Proteins -- Separation -- Periodicals; Bioinformatics -- Periodicals; Proteomics -- Periodicals; Genomes -- Periodicals; Molecular genetics -- Periodicals; 572.605
• DOI: 10.1002/pmic.201670100
• Languages: English
• ISSNs: 1615-9853

Abstract

Abstract : DOI:10.1002/pmic.201500445 The characterization of peptides bound to human leukocyte antigen (HLA) class I is of fundamental importance for understanding CD8+ T cell‐driven immunological processes and for the development of immunomodulatory therapeutic strategies. Capitalizing on the recent developments in mass spectrometry and bioinformatics, a methodology for the efficient recovery of acid‐eluted HLA peptides after purification with the pan‐reactive antibody W6/32 is implemented and a total of 27 862 unique peptides from five human cancer cell lines is identified. Knowledge of the HLA class I peptidome should facilitate multiplex tetramer technology‐based characterization of T cells, and allow the development of patient selection, stratification and immunomodulatory therapeutic strategies. Considering the observed depth of our peptidome analysis, a combination with high throughput sequencing data of individual patients could enable the identification of mutated peptides from patient serum in the future, thus generating patient‐ and tumor‐specific HLA peptidomes. For details, see research article by D. Ritz et al., pages 1570–1580.