A peptide from heat shock protein 60 is the dominant peptide bound to Qa-1 in the absence of the MHC class Ia leader sequence peptide Qdm

Adrian Davies, Suzanne Kalb, Bitao Liang, Carla J. Aldrich, François A. Lemonnier, Hong Jiang, Robert Cotter, Mark J. Soloski

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Abstract

The MHC class Ib molecule Qa-1 binds specifically and predominantly to a single 9-aa peptide (AMAPRTLLL) derived from the leader sequence of many MHC class Ia proteins. This peptide is referred to as Qdm. In this study, we report the isolation and sequencing of a heat shock protein 60-derived peptide (GMKFDRGYI) from Qa-1. This peptide is the dominant peptide bound to Qa-1 in the absence of Qdm. A Qa-1-restricted CTL clone recognizes this heat shock protein 60 peptide, further verifying that it binds to Qa-1 and a peptide from the homologous Salmonella typhimurium protein GroEL (GMQFDRGYL). These observations have implications for how Qa-1 can influence NK cell and T cell effector function via the TCR and CD94/NKG2 family members, and how this effect can change under conditions that cause the peptides bound to Qa-1 to change.

Original languageEnglish (US)
Pages (from-to)5027-5033
Number of pages7
JournalJournal of Immunology
Volume170
Issue number10
DOIs
StatePublished - May 15 2003

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ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Cite this

Davies, A., Kalb, S., Liang, B., Aldrich, C. J., Lemonnier, F. A., Jiang, H., Cotter, R., & Soloski, M. J. (2003). A peptide from heat shock protein 60 is the dominant peptide bound to Qa-1 in the absence of the MHC class Ia leader sequence peptide Qdm. Journal of Immunology, 170(10), 5027-5033. https://doi.org/10.4049/jimmunol.170.10.5027