Identification of potential HLA class I and class II epitope precursors associated with heat shock protein 70 (HSPA)

  1. Lookup NU author(s)
  2. Pawel Stocki
  3. Dr Nick Morris
  4. Dr Xiao Wang
  5. Professor Anne Dickinson
Author(s)Stocki P, Morris NJ, Preisinger C, Wang XN, Kolch W, Multhoff G, Dickinson AM
Publication type Article
JournalCell Stress Chaperones
Year2010
Volume15
Issue5
Pages729-741
ISSN (print)1355-8145
ISSN (electronic)1466-1268
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Heat shock protein 70 (HSPA) is a molecular chaperone which has been suggested to shuttle human leukocyte antigen (HLA) epitope precursors from the proteasome to the transporter associated with antigen processing. Despite the reported observations that peptides chaperoned by HSPA are an effective source of antigens for cross-priming, little is known about the peptides involved in the process. In this study, we investigated the possible involvement of HSPA in HLA class I or class II antigen presentation and analysed the antigenic potential of the associated peptides. HSPA was purified from CCRF-CEM and K562 cell lines, and using mass spectrometry techniques, we identified 44 different peptides which were co-purified with HSPA. The affinity of the identified peptides to two HSPA isoforms, HSPA1A and HSPA8, was confirmed using a peptide array. Four of the HSPA-associated peptides were matched with 13 previously reported HLA epitopes. Of these 13 peptides, nine were HLA class I and four were HLA class II epitopes. These results demonstrate the association of HSPA with HLA class I and class II epitopes, therefore providing further evidence for the involvement of HSPA in the antigen presentation process.
PublisherSpringer Netherlands
URLhttp://dx.doi.org/10.1007/s12192-010-0184-z
DOI10.1007/s12192-010-0184-z
Actions    Link to this publication