Abstract
The T cell receptor (TCR) ζ chain was attached to the TCR α and β extracellular domains to induce efficient expression of αβ heterodimers that can recognize complexes of antigen with major histocompatibility complex (MHC) molecules. Chimeric constructs expressed in RBL-2H3 cells were efficiently transported to the cell surface uniquely as disulfide-linked heterodimers. Transfectants were activated by specific antigen-MHC complexes, which demonstrated that the expressed αβ was functional and that CD3 was not required for antigen-MHC binding. Constructs with thrombin cleavage sites were efficiently cleaved to soluble disulfide-linked heterodimers. Thus, attachment of TCR ζ domains and protease cleavage sites to TCR α and β induces expression of demonstrably functional heterodimers that can be solubilized.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 7:03 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 11, 2024, 3:07 a.m.) |
Indexed | 1 year ago (Aug. 7, 2024, 8:33 a.m.) |
Issued | 33 years, 2 months ago (May 29, 1992) |
Published | 33 years, 2 months ago (May 29, 1992) |
Published Print | 33 years, 2 months ago (May 29, 1992) |
@article{Engel_1992, title={High-Efficiency Expression and Solubilization of Functional T Cell Antigen Receptor Heterodimers}, volume={256}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1598575}, DOI={10.1126/science.1598575}, number={5061}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Engel, Isaac and Ottenhoff, Tom H. M. and Klausner, Richard D.}, year={1992}, month=may, pages={1318–1321} }