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Stoichiometry of the murine T cell receptor

Laboratory of Mammalian Genes and Development, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892

CORRESPONDENCE Sandra M. Hayes: hayessa{at}upstate.edu

The T cell receptor for antigen (TCR) complex is organized into two functional domains: the antigen-binding clonotypic heterodimer and the signal-transducing invariant CD3 and TCR chains. In most vertebrates, there are two different clonotypic heterodimers (TCRß and TCR) that define the ß and T cell lineages, respectively. ß- and TCRs also differ in their invariant chain subunit composition, in that ßTCRs contain CD3 and CD3 dimers, whereas TCRs contain only CD3 dimers. This difference in subunit composition of the ß- and TCRs raises the question of whether the stoichiometries of these receptor complexes are different. As the stoichiometry of the murine TCR has not been previously investigated, we used two quantitative immunofluorescent approaches to determine the valency of TCR heterodimers and CD3 dimers in surface murine TCR complexes. Our results support a model of murine TCR stoichiometry in which there are two CD3 dimers for every TCR heterodimer.

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