Structure-function relationships among highly diverse T cells that recognize a determinant from influenza virus hemagglutinin.

Abstract
We have analyzed the structural and genetic basis for T cell recognition of the complex formed between antigen and class II products of the major histocompatibility complex by performing sequence analysis of T cell receptors (TCRs) induced in response to the helper T cell site 1 of the influenza virus hemagglutinin. The results demonstrate, first, that structurally highly diverse TCRs can be utilized in recognition of the same antigen/I-Ed complex: 12 of 13 TCRs utilize unique V.alpha./V.beta. gene segment combinations, suggesting that .apprx. 70 different V.alpha./V.beta. combinations are available to BALB/c mice in response to this determinant. Second, comparison of these sequences with the ability of each hybridoma to recognize a panel of peptide analogues suggests that .alpha. and .beta. chains of these TCRs frequently determine specificity for the NH2-terminal and the COOH terminal portions, respectively, of the site 1 determinant.