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The Journal of Immunology, 1999, 162: 2671-2676.
Copyright © 1999 by The American Association of Immunologists

Soluble Class I MHC with ß2-Microglobulin Covalently Linked Peptides: Specific Binding to a T Cell Hybridoma1

Janice White*, Frances Crawford*, Daved Fremont{dagger}, Philippa Marrack*,{ddagger} and John Kappler2,*,§

* Division of Basic Immunology, Howard Hughes Medical Institute, National Jewish Medical and Research Center, Denver, CO 80206; {dagger} Department of Pathology, Center for Immunology, Washington University School of Medicine, St Louis, MO 63110; and {ddagger} Departments of Immunology and of Biochemistry, Biophysics and Genetics, and § Departments of Immunology, Pharmacology and Medicine, University of Colorado Health Science Center, Denver, CO 80262

Soluble forms of the mouse MHC class I molecule, Dd, 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 ß2-microglobulin. The MHC heavy chain and ß2-microglobulin were firmly associated, and the molecules displayed an Ab epitope requiring proper occupancy of the peptide binding groove. Soluble Dd containing a covalent version of a well-characterized Dd-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.




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