White J, Crawford F, Fremont D, Marrack P, Kappler J
Division of Basic Immunology, Howard Hughes Medical Institute, National Jewish Medical and Research Center, Denver, CO 80206, USA.
J Immunol. 1999 Mar 1;162(5):2671-6.
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 beta2-microglobulin. The MHC heavy chain and beta2-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.
产生了小鼠MHC I类分子Dd的可溶性形式，其中肽结合槽被通过共价柔性肽接头连接到相关β2-微球蛋白N端的肽均匀占据。MHC重链和β2-微球蛋白紧密结合，并且这些分子展示了一个需要肽结合槽被适当占据的抗体表位。含有来自HIV的一个特征明确的Dd结合肽的共价形式的可溶性Dd刺激了对这种组合特异的T细胞杂交瘤。此外，该分子的四价形式以明显高亲和力与这种杂交瘤特异性结合。
