Cloning, expression and purification of MPT53 of mycobacterial tuberculosis

Objective To construct a expression vector of MPT53 of mycobacterium tuberculosis and identify and purify the protein in the E. coli. Methods The gene encoding protein MPT53 was amplified from mycobacterium tuberculosis H37RV chromosomal DNA by using PCR, then cloned into pMD-T vector after identifying, then cloned pET32a expressing vector, transformed into E. coli BL21. Bcaterial lyastes prepared from IPTG induced cultures were loading SDS-PAGE. Results Recombinant plasmid PET32a-MPT53 was constructed, and 36 ku MPT53 protein was expressed, which consistent with the theoretical value. Conclusion MPT53 protein expressed successfully and lays the foundation for its application.