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Surface structures of bacteria contribute to the microbial pathogenic potential and are capable of causing local and generalized inflammatory reactions. Among these factors, endotoxin and peptidoglycan are of particular medical importance. Both toxic bacterial polymers are now recognized to interact with the same cellular receptor, the CD14 molecule, which is expressed on different types of immune cells, in particular, monocytes/macrophages. The interaction between these bacterial activators and CD14 leads to the production of endogenous mediators such as tumor necrosis factor alpha, interleukin 1 (IL-1), and IL-6, which are ultimately responsible for phlogistic responses. The fact that CD14 recognizes not only endotoxin and peptidoglycan but also other glycosyl-based microbial polymers suggests that this cellular surface molecule represents a lectin.

CD26 is an activation antigen which is expressed on the surface of human T-lymphocytes. It has been characterized to be the dipeptidyl peptidase IV (DPP IV). Considerable amounts of CD26 are already present on resting T-lymphocytes. The expression of CD26 is enhanced by T-cell mitogens or antigens. A correlation of CD26 expression and of enhanced enzymatic activity was observed after T-cell activation. Our data indicate that not only the immunoreactivity, but also the enzymatic activity of CD26 are detectable on the cell surface. In addition, de novo expression of CD26 was demonstrated on CD26-negative T-cells after mitogenic or antigenic stimulation. CD26 expression is initiated during the G1 phase of the cell cycle. The expression occurs nearly simultaneously with HLA-DR, but later than CD25. Similar to CD25 and HLA-DR, CD26 is not a permanent marker on the surface of T-lymphocytes, but is down-regulated after 7 days of culture. When testing the influence of interleukin 1, interleukin 2, tumour necrosis factor, and interferon-gamma on the expression of CD26, no effect was found on unstimulated or on mitogen-stimulated T-lymphocytes. The binding of two different monoclonal antibodies against CD26 (anti-DPP IV and anti-Tal) to resting and activated T-lymphocytes revealed a different pattern of immunoreactivity. Resting T-lymphocytes reacted stronger with anti-DPP IV than with anti-Tal. However, binding of the two monoclonal antibodies to T-cell blasts did not show significant differences. These data indicate that CD26 may be expressed in differently modulated configurations on the surface of T-cells, which may be associated with a distinct status of activation and/or function.

In this study we investigated the binding of three different monoclonal antibodies (MoAb), TII 19-4-7, 4EL1C7, and B1.19.2, which are clustered in CD26 to the ectoenzyme dipeptidyl peptidase IV (DPP IV) and to T lymphocytes. We found that all three MoAb bind to both unstimulated and mitogen-stimulated T lymphocytes. Further results indicated an inconsistency within the CD26-clustered MoAb: TII 19-4-7 and 4EL1C7, but not B1.19.2, recognized DPP IV on the surface o T lymphocytes and immobilized on solid-phase ELISA or Western blot. There was competition of binding to DPP IV between TII 19-4-7 and 4EL1C7. From these results we conclude that CD26 antigen is represented by the ectoenzyme DPP IV. TII 19-4-7 and 4EL1C7 recognize the same or partly identical epitopes on DPP IV, whereas B1.19.2 recognizes a different antigen. TII 19-4-7 and 4EL1C7, but not B1.19.2, should be clustered in CD26.