Expression and purification of streptococcus pneumoniae virulence factor PspA / 重庆医科大学学报

ABSTRACT

Objective:To obtain purified PspA produced by prokaryotic expression system.Methods:Template DNA was isolated from cultured Streptococcus pneumonia TIGR4.By gene recombination technology in vitro,sequence encoding PspA antigen epitope was cloned into PET-32(a) expression vector.After being confirmed by sequencing,expressed antigen protein was identified by SDS-PAGE and Western blot.Results:The DNA sequence analysis confirmed that the cloned PspA gene was according to GenBank data.The PspA fusion protein was proved by Western blot.Conclusion:A highly expressed recombinant PspA protein was successfully obtained.