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

Lookup NU author(s): Pawel Stocki, Dr Nick Morris, Dr Xiao WangORCiD, Professor Anne Dickinson

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Abstract

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.


Publication metadata

Author(s): Stocki P, Morris NJ, Preisinger C, Wang XN, Kolch W, Multhoff G, Dickinson AM

Publication type: Article

Publication status: Published

Journal: Cell Stress Chaperones

Year: 2010

Volume: 15

Issue: 5

Pages: 729-741

Print publication date: 01/04/2010

ISSN (print): 1355-8145

ISSN (electronic): 1466-1268

Publisher: Springer Netherlands

URL: http://dx.doi.org/10.1007/s12192-010-0184-z

DOI: 10.1007/s12192-010-0184-z


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Funding

Funder referenceFunder name
01EZ0826German Federal Ministry of Education and Research (BMBF)
04070Leukaemia Research Fund, UK
MU1238/7-2German Research Foundation (DFG)
MRTN-CT-2004-512253European Commission

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