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

J White, F Crawford, D Fremont, P Marrack… - The Journal of …, 1999 - journals.aai.org
J White, F Crawford, D Fremont, P Marrack, J Kappler
The Journal of Immunology, 1999journals.aai.org
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 β 2-microglobulin. The MHC heavy chain and β 2-
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 …
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 β 2-microglobulin. The MHC heavy chain and β 2-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.
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