Abstract
The paper reports the purification and its optimization of recombinant proteins p10, p32, p54, p54ΔTM, DNA ligase and DNA ligaseΔDBD of African swine fever virus. The corresponding coding sequences were subcloned into pASG-IBA105 and pASG-IBA103 vectors, multiplied and used for transformation of competent E. coli expression strain. Expressed proteins were purified using Strep-Tactin XT purification system under native and denaturing conditions, as well as using detergents according to the optimized protocol for recombinant proteins solubilization from inclusion bodies. Among all expressed and purified proteins p32 and p54 were found to be immunoreactive and specific. Although p54 was unstable during long-term storage, after further storage condition optimization, the protein can be used for indirect ASF ELISA development. Recombinant p32 was shown to be an effective antigen for ASF ELISA providing detection of antibodies against ASFV with low background signal
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