Non-neutralizing monoclonal antibody, in complex with its epitope on the Foot-and-Mouth disease virus enhances binding of three neutralizing monoclonal antibodies
2011
Valcic, M., Faculty of Veterinary Medicine, Belgrade (Serbia) | Radojicic, S., Faculty of Veterinary Medicine, Belgrade (Serbia) | Bacic, D., Faculty of Veterinary Medicine, Belgrade (Serbia) | Obrenovic, S., Faculty of Veterinary Medicine, Belgrade (Serbia)
Competitive radio immuno test (CRIA) is a frequently used method in order to detect and investigate epitopes in the structure of complex antigens. While mapping epitopes in the structure of the Foot-and-Mouth disease virus, it was found that there is one monoclonal antibody (Mab), among many others that has no neutralizing effect on the virus. Usually, such hybridoma cell clones are discarded as useless since they have no biological and/or physiological effect on the virus as far as infectology and infectious disease are concerned. However, results of binding of one Mat that was specific for sequentional epitope on the FMDV structure, which was not neutralizing, show that such an immune complex enhanced the binding of other three Mabs. These three Mabs were neutralizing and specific for three different epitopes in the virus immunodominant protein 1 (VP1). Out of these three epitopes, one was sequentional and other two were conformational. The same phenomenon has been registered for other three viruses: Sindbis, hepatitis a and influenza virus. It has been proposed three essentially different mechanisms which may result in synergistic binding of Mabs: stabilization of antigen-antibody complex, enhancement of avidity and /or increased affinity. This phenomenon showsthat non-neutralizing antibodies, despite being useless as far as protection from disease is concerned, still have some biological and/or physiological roles in the virus life. At the same time, this phenomenon can explain why there has to be several thousands more in quantity mass of epitope in subunit vaccine in order to achieve neutralization in comparison to the same epitope incorporated in the structure of the particular virus.
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