Immunogenicity analysis of the E. coli expressed structural protein VP1 of persistent infection foot-and-mouth disease virus.

The persistent infection of FMDV in cloven hoofed animals has made the epidemic prevention and control more difficult. VP1 is the main immunogenic protein and first candidate of vaccine development for FMDV prevention. However, the mutation of VP1 in host cell with persistent infection FMDV (PI-FMDV) caused the change of its immunogenicity. Hence, it is imperative to establish the expression system for VP1 of PI-FMDV (PI-VP1) and re-evaluate its immunogenicity. In this study, the PI-VP1 with His-tag was cloned into pET-28a vector. PI-VP1 protein was expressed and purified in E. coli , and further the antiserum of immunized mice was analyzed. Results showed that purified PI-VP1 protein produced a good humoral and cellular immune response after immunizing mice. Furthermore, our study showed that the antiserum could not only neutralize PI-FMDV, but also prevent the adsorption of WT-FMDV. In summarize, our work provides valuable implications for the FMDV vaccines and therapeutics development. • CDNA of VP1 protein was obtained from the established cell model with PI-FMDV infection and inserted into the pET-28a vector. • The optimal expression conditions of VP1 protein of PI-FMDV were the E.coli cultured at 37 °C, 1 mM IPTG for 12 h. • The purified VP1 protein of PI-FMDV produced a good humoral and cellular immune response after immunizing mice. • Sera from PI-VP1-immunized mice could not only neutralize PI-FMDV, but also prevent the adsorption of WT-FMDV. [ABSTRACT FROM AUTHOR]