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.
|Number of pages||6|
|Journal||Journal of Immunology|
|State||Published - Mar 1 1999|