T cell recognition of naturally presented epitopes of self-heat shock protein 70

Huib de Jong, Eva C Koffeman*, Jennifer M Meerding, Rianne C Scholman, Lotte Wieten, Wilco de Jager, Mark Klein, Henny Otten, Femke van Wijk, Ruurd van der Zee, Johannes W J Bijlsma, Femke Broere, Willem van Eden, Berent J Prakken

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review


Self-reactive T cells have shown to have a potential role as regulators of the immune system preventing or even suppressing autoimmunity. One of the most abundant proteins that can be eluted from human HLA molecules is heat shock protein 70 (HSP70). The aims of the current study are to identify HSP70 epitopes based on published HLA elution studies and to investigate whether T cells from healthy individuals may respond to such self-epitopes. A literature search and subsequent in silico binding prediction based on theoretical MHC binding motifs resulted in the identification of seven HSP70 epitopes. PBMCs of healthy controls proliferated after incubation with two of the seven peptides (H167 and H290). Furthermore H161, H290, and H443 induced CD69 expression or production of cytokines IFNγ or TNFα in healthy controls. The identification of these naturally presented epitopes and the response they elicit in the normal immune system make them potential candidates to study during inflammatory conditions as well as in autoimmune diseases.

Original languageEnglish
Pages (from-to)569-78
Number of pages10
JournalCell Stress & Chaperones
Issue number4
Publication statusPublished - Jul 2014


  • Adult
  • Amino Acid Sequence
  • Autoimmunity
  • Cell Line
  • Cell Proliferation
  • Cells, Cultured
  • Cytokines
  • Epitopes, T-Lymphocyte
  • Female
  • Genes, MHC Class II
  • HSP70 Heat-Shock Proteins
  • Humans
  • Leukocytes, Mononuclear
  • Lymphocyte Activation
  • Male
  • Molecular Sequence Data
  • Peptides
  • T-Lymphocytes
  • Young Adult


Dive into the research topics of 'T cell recognition of naturally presented epitopes of self-heat shock protein 70'. Together they form a unique fingerprint.

Cite this