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Prokaryotic Expression and Purification of HP1501 Recombination Protein from Helicobacter Pylori NCTC11637

Author: YangJiWen
Tutor: YangZhiBang
School: Chongqing Medical University
Course: Pathogen Biology
Keywords: Helicobacter pylori Hp1501 gene bioinformatics prokaryotic expression purification
CLC: R346
Type: Master's thesis
Year: 2011
Downloads: 27
Quote: 0
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Abstract


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.

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