A novel single chain I-Ab molecule can stimulate and stain antigen-specific T cells

Wesley P. Thayer, Chinh T. Dao, Leszek Ignatowicz, Peter E. Jensen

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Multimers of soluble major histocompatibility complex class I and II molecules have proven to be useful reagents in quantifying and following specific T cell populations. This study describes the design, generation, and characterization of a novel, single chain I-Ab molecule which utilizes a unique linker derived from the murine invariant chain. A fragment of the invariant chain, residues 58-85, binds to a region proximal to the class II peptide binding groove and stabilizes occupancy of the class II invariant chain-associated peptide. We have utilized this fragment, replacing CLIP with the Eα peptide sequence, to lock the attached peptide into the class II binding groove. The single chain I-Ab molecule was recognized by a panel of conformation-sensitive, I-Ab-specific, monoclonal antibodies. Membrane-bound and soluble forms of the single chain I-Ab stimulated an antigen-specific T cell hybridoma, and tetramers made from soluble monomers stained these cells. The unique features of this molecule may be useful in the design of recombinant T cell receptor ligands containing peptides with low affinity for MHC.

Original languageEnglish (US)
Pages (from-to)861-870
Number of pages10
JournalMolecular Immunology
Volume39
Issue number14
DOIs
StatePublished - May 2003

Keywords

  • Antigen presentation
  • Class II major histocompatibility molecules
  • Invariant chain
  • Peptides
  • T cells
  • Tetramers

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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