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Experiments with multivalent self-peptide/H-2Dᵇ tetramers revealed that the B6.2.16 TCR binds thymic self-peptide/H-2Dᵇ. Antibody blocking experiments with the clonotypic T3.70 mAb (specific for the B6.2.16 TCR α chain) showed that the antigen-binding domain of the TCR interacts with the H-2Dᵇ. The potential reactivity self-peptide/H-2Db tetramers for CD8 was not sufficient to account for the staining of B6.2.16 CD8 cells. Thus, the binding of self-peptide/H-2Dᵇ tetramers was specific for the B6.2.16 TCR. The B6.2.16 TCR bound non-agonist, self-peptide/H-2Dᵇ tetramers at different affinities, i.e. the B6.2.16 TCR binding to H-2Dᵇ tetramers was self-peptide specific. This implies that the B6.2.16 TCR either interacts to some extent with the self-peptide entrenched in the peptide binding pocket of H-2Dᵇ, or that self-peptide indirectly influences TCR binding to the α1/α2 domains of H-2Dᵇ.
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