Prokaryotic Expression And Purification Of HP1501 Recombination Protein From Helicobacter Pylori NCTC11637

Objective To research the function of Hp1501 gene from Helicobacter pylori(Hp) NCTC11637 and to search the protective antigens which can be used in a vaccine to prevent Hp infection.Methods Polymerase chain reaction(PCR) was used to amplify the Hp1501 gene from Hp chromosomal DNA.DNA sequence was determined and analyzed after T-A clone. The recombinant plasmid pQE30-Hp1501a was transformed into E. coli XL1-blue and was induced for prokaryotic expression with IPTG. The recombinant fusion protein was analyzed by SDS-PAGE and Western blot,and was purified by affinity chromatograph.Results Hp1501 gene from Hp NCTC11637 was 1164bp in length, 96%～97% identites in DNA sequence and 97%～98% identites in amino acid sequence compared with standard strain 26695 and J99. SDS-PAGE and Western blot showed the recombinant fusion protein was about 37kDa in size. The purity of target protein was 93%.Conclusion The recombinant fusion protein of Hp1501a gene from Hp NCTC11637 has been obtained and purified successfully, providing a good foundation for the studies such as exploring the biological function of outer membrane protein and bolting a novel vaccine candidate of Hp.