A comprehensive analysis of constitutive naturally processed and presented HLA‐C*04:01 (Cw4) – specific peptides. Issue 3 (7th January 2014)

• Record Type: Journal Article
• Authors: Schittenhelm, R. B.; Dudek, N. L.; Croft, N. P.; Ramarathinam, S. H.; Purcell, A. W.
• Is Part Of: Tissue antigens. Volume 83:Issue 3(2014)
• Page Start: 174
• Page End: 179
• Publication Date: 2014-01-07
• Subjects: Antigens -- Periodicals; Immunological tolerance -- Periodicals; Immunogenetics -- Periodicals; 571.9645
• DOI: 10.1111/tan.12282
• Languages: English
• ISSNs: 0001-2815

Abstract

<abstract abstract-type="main" id="tan12282-abs-0001"> <title>Abstract</title> <p id="tan12282-para-0001">The human B lymphoblastoid cell line C1R is widely regarded as human leukocyte antigen‐A (HLA‐A)/HLA‐B negative and is therefore frequently exploited as a recipient cell line to study HLA class I functions. However, the normal levels of <italic>HLA‐C*04:01</italic> often hamper the investigation of introduced HLA class I allomorphs, which is particularly evident in sensitive applications such as mass spectrometry. Here we describe the comprehensive analysis of endogenous <italic>HLA‐C*04:01</italic> ligands expressed on the surface of C1R cells to (i) define a large sequence dataset of <italic>HLA‐C*04:01</italic> ligands, to (ii) refine the <italic>HLA‐C*04:01</italic> peptide‐binding motif and (iii) to provide a resource that allows discrimination between peptides bound to introduced HLA class I subtypes and to the endogenous <italic>HLA‐C*04:01</italic> molecules.</p> </abstract>