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 language | English |
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Pages (from-to) | 2671-2676 |
Number of pages | 6 |
Journal | Journal of Immunology |
Volume | 162 |
Issue number | 5 |
State | Published - Mar 1 1999 |