Recent work has also indicated that the 5C.C7 TCR has a t 1/2 for MCC/I-E k binding between those of the 2B4-MCC/I-E k and 2B4-MCC(102S)/I-E k interactions (Lyons, D.S., Teyton, L., and Davis, M.M., unpublished data). ) have shown that the 2B4 TCR αβ heterodimer binds to MCC/I-E k with a half-life (t 1/2) of 11 s and MCC(102S)/I-E k with a t 1/2 of 2 s at 25☌ ( Table 1). In contrast to immunoglobulins, the basis for TCR repertoire selection and the consequences of repertoire changes on T cell function are not well understood. Effective APC-mediated stimulation triggers context-dependent T cell developmental or effector processes. Antigen recognition is mediated by the TCR αβ heterodimer. αβ T lymphocytes, on the other hand, recognize antigenic peptides presented by major histocompatibility complex (MHC) molecules on the surface of antigen-presenting cells (APCs). Upon repeated antigenic challenge, affinity maturation improves the efficiency of this linkage by selecting for immunoglobulins of increased affinity for antigen.
Immunoglobulin molecules function by directly binding antigen, thereby linking immune effector mechanisms to specific antigens. Recall responses are often associated with a refinement of antigen-specific immunoglobulin and T cell antigen receptor (TCR) repertoires. In most cases, antigenic challenge results in the establishment of immunological memory, a state in which the immune system is poised to respond more rapidly and effectively upon recurrent antigenic exposure.
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