H. Seimiya et al., T-CELL RECEPTOR-EXTRACELLULAR CONSTANT REGIONS AS HETERO-CROSS-LINKERS FOR IMMUNOGLOBULIN VARIABLE REGIONS, Journal of Biochemistry, 113(6), 1993, pp. 687-691
The T cell receptor alpha and beta chains are covalently linked via a
disulfide bond in their extracellular constant regions. To use these d
omains as specific hetero-cross-linkers of two different polypeptides,
we created genetic constructs encoding a chimeric antibody Fab fragme
nt in which mouse immunoglobulin constant regions from a phosphorylcho
line-specific antibody were substituted for human alphabeta-T cell rec
eptor (TCR) extracellular constant regions (for solubilization, the tr
ansmembrane- and cytoplasmic-regions of the receptor were deleted). Th
ese constructs, i.e., chimeric heavy (V(H)C(beta)C(kappa)) and light (
V(L)C(alpha)) chains, were cotransfected into murine SP2/0 myeloma cel
ls for expression. Cells transfected with the genes expressed mRNAs fo
r chimeric heavy and light chains. Without CD3 molecules, the two chim
eric chains specifically associated via a disulfide bond to form a chi
meric Fab fragment in the cells. These data indicate that the TCR C(al
pha)- and C(beta)-regions might be used as potent specific hetero-cros
s-linkers for protein engineering.