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. 1991 Sep 15;88(18):8077-81.
doi: 10.1073/pnas.88.18.8077.

Engineered secreted T-cell receptor alpha beta heterodimers

C Grégoire  1 , N Rebaï, F Schweisguth, A Necker, G Mazza, N Auphan, A Millward, A M Schmitt-Verhulst, B Malissen
Affiliations

Engineered secreted T-cell receptor alpha beta heterodimers

C Grégoire et al. Proc Natl Acad Sci U S A. .

Abstract

We have produced a soluble form of a mouse alpha beta T-cell antigen receptor (TCR) by shuffling its variable (V) and constant (C) domains to the C region of an immunoglobulin kappa light chain. These chimeric molecules composed of V alpha C alpha C kappa and V beta C beta C kappa chains were efficiently secreted (up to 1 micrograms/ml) by transfected myeloma cells as noncovalent heterodimers of about 95-kDa molecular mass. In the absence of direct binding measurement, we have refined the epitopic analysis of the soluble V alpha C alpha C kappa-V beta C beta C kappa dimers and shown that they react with an anti-clonotypic antibody and two antibodies directed to the C domain of the TCR alpha and beta chains. Conversely, we have raised three distinct monoclonal antibodies against the soluble TCR heterodimers and shown that they recognize surface-expressed TCRs. Two of these antibodies were found to react specifically with the products of the V alpha 2 (V delta 8) and V beta 2 gene segments, respectively. When considered together, these data suggest that these soluble TCR molecules are folded in a conformation indistinguishable from that which they assume at the cell surface.

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