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Science 10 August 1990:
Vol. 249. no. 4969, pp. 677 - 679
DOI: 10.1126/science.1696397
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Articles

Science, Vol 249, Issue 4969, 677-679
Copyright © 1990 by American Association for the Advancement of Science

articles

Expression of T cell antigen receptor heterodimers in a lipid-linked form

AY Lin, B Devaux, A Green, C Sagerstrom, JF Elliott, and MM Davis

Howard Hughes Medical Institute, Stanford University School of Medicine, CA 94305-5402.

The interaction of the T cell receptor for antigen (TCR) with its antigen-major histocompatibility complex ligand is difficult to study because both are cell surface multimers. The TCR consists of two chains (alpha and beta) that are complexed to the five or more nonpolymorphic CD3 polypeptides. A soluble form of the TCR was engineered by replacing the carboxyl termini of alpha and beta with signal sequences from lipid-linked proteins, making them susceptible to enzymatic cleavage. In this manner, TCR heterodimers can be expressed independently of the CD3 polypeptides and in significant quantities (0.5 milligram per week). This technique seems generalizable to biochemical and structural studies of many other cell surface molecules as well.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)