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Comparative studies on immunoreactivity of truncated recombinant proteins of foot and mouth disease virus (FMDV) produced in E.coli and insect cells.

For effective FMD control programme, India needs large quantities of cheaper diagnostics in addition to vaccine. Diagnostic reagents produced through conventional methods may not be able to meet such requirements. Alternatively, rDNA technology using suitable heterologous systems that permit production of recombinant antigens to the most native form may be exploited. Studies conducted in our laboratory have led us to select carboxy terminal part of VP1 for expression and evaluation. The protein, which was purified from E.coli under denaturing conditions, was renatured and its reactivity was compared with the protein expressed in insect cells through recombinant baculovirus. The expressed protein in the insect cell whole lysate reacted more efficiently with antibodies raised against whole virus than the purified and renatured protein produced in E.coli. But for its lower reactivity, protein produced from E.coli was found to be suitable in type detection. In addition, the size of the protein is small (16 kD) and production and purification of it from E.coli may be cost effective. Hence, it may be exploited for FMDV typing.