Soluble class I MHC with β2-microglobulin covalently linked peptides: Specific binding to a T cell hybridoma

Janice White, Frances Crawford, Daved Fremont, Philippa Marrack, John Kappler

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

Soluble forms of the mouse MHC class I molecule, D(d), were produced in which the peptide binding groove was uniformly occupied by peptides attached via a covalent flexible peptide linker to the N terminus of the associated β2-microglobulin. The MHC heavy chain and β2-microglobulin were firmly associated, and the molecules displayed an Ab epitope requiring proper occupancy of the peptide binding groove. Soluble D(d) containing a covalent version of a well-characterized D(d)-binding peptide from HIV stimulated a T cell hybridoma specific for this combination. Furthermore, a tetravalent version of this molecule bound specifically with apparent high avidity to this hybridoma.

Original languageEnglish
Pages (from-to)2671-2676
Number of pages6
JournalJournal of Immunology
Volume162
Issue number5
StatePublished - Mar 1 1999

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