中国生物工程杂志

To express and purify recombinant mature adhesive protein （rCPM36）of avian Pasteurella multocida type strain P1059 and detect its antigenicity. Methods: The cpm36 gene, encoding a mature adhesive protein without signal peptide was amplified by PCR from genomic DNA of avian Pasteurella multocida strain P1059, PCR product was cloned into the expression vector pQE30 to constructed recombinant plasmid pQE30-cpm36 and then transformed into E. coli M15, inducing it with 0.2mmol/L IPTG for 4 hours. The expression and solubility of recombinant protein was detected by DSD-PAGE. The interest protein was purified by Ni-NTA affinity chromatography and its antigenicity was detected Western blot analysis. Results: SDS-PAGE showed the 37kDa recombinant protein was successfully expressed in E.coli after IPTG inducing. In Western blot analysis，rabbit antiserum against rCPM36 reacted with rCPM36, it demonstrated that the recombinant protein is an antigenic protein. Conclusion: rCPM36 is successfully expressed in E. coli. The interest protein is successfully purified by Ni-NTA affinity chromatography and is detected its antigenicity. The rCPM36 protein might be a useful vaccine candidate antigen for avian Pasteurella multocida.