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A murine monoclonal IgG1 antibody, marked as MAb26, specific for tetanus toxoid has been immunochemically characterized. By performing en- zyme-linked immunosorbent assays (ELISAs) and western blot analyses, it was demonstrated that MAb26 reacted with tetanus toxoid, tetanus toxin and β2-gly- coprotein I (β2GPI). According to the results, MAb26 recognized the sequential epitope on the tetanus heavy chain. The affinity constant, calculated from Scat- chard plots of MAb26 binding to tetanus toxoid, was 1.145×10 8 M -1 and the measurement of the relative affinity of MAb26 by ELISA using thiocyanate elution showed a significantly higher affinity of MAb26 to the toxoid (p = = 0.0012) in comparison to the toxin. Additionally, the reactivity of MAb26 toward the toxoid forms increased when the tetanus toxin was detoxified using 8 mM and higher formaldehyde concentrations. The similarity of the tetanus toxoid to several sera proteins, either at the level of its conformation (IL-1α) or at the level of peptide sequences (β2GPI, laminin) favors its role in auto- immunity by the mechanism of molecular mimicry. As the induction of an au- toimmune disease is dependent on the breakdown of tolerance, which could be the result of an overt hyperstimulation, the control of the presence and concen- tration of self-reactive epitopes in vaccine preparations is a prerequisite. In this study, it was shown that MAb26 can: 1) discriminate between the tetanus toxin and different toxoid forms, which makes it a good candidate for antibody con- trol during vaccine preparation; 2) due to its cross-reactivity with β2GPI, it could provide information on the presence of a potentially dangerous sequential epi- tope expressed at the protein surface.

journal of the serbian chemical society

The monoclonal antibody 26 raised against tetanus toxoid also recognizes tetanus toxin and β2-glycoprotein I - its binding properties in vitro and potential applications