CLONING AND EXPRESSION OF HELICOBACTER PYLORI HPAA GENE

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NAJAR PIRAYEH SH.; OTOUFI J.; HOSSEINKHANI S.; FARSHCHIAN MOEIN

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Journal: Cell Journal (Yakhteh) Year:2009 | Volume:11 | Issue:3 (43) Page(s): 273-276

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Information Journal Paper

Title

CLONING AND EXPRESSION OF HELICOBACTER PYLORI HPAA GENE

Author(s)

NAJAR PIRAYEH SH. | OTOUFI J. | HOSSEINKHANI S. | FARSHCHIAN MOEIN | Issue Writer Certificate

Keywords

HELICOBACTER PYLORIQ1

HPAAQ1

RECOMBINANT PROTEINQ1

PET28AQ1

Abstract

Objective: HELICOBACTER PYLORI is associated with chronic gastritis, peptic ulcers, gastric adenocarcinoma and gastric mucosa-associated lymphoid tissue (MALT) lymphoma. Antibiotic therapies do not protect from potential re-infection and have a risk for development of drug resistance. Therefore, prophylactic vaccine mediated protection against H. pylori is an attractive clinical interest. H. pylori adhesin A (HpaA) is a conserved surface lipoprotein and plays important roles in the pathogenesis of infection. In this study the RECOMBINANT PROTEIN (rHpaA) was over-expressed in E.coli.Materials and Methods: The HPAA gene was amplified by PCR. Prokaryote expression vector pET28a-hpaA was constructed, and used to transform E.coli BL21DE3. The expression of RECOMBINANT PROTEIN induced by IPTG was examined by SDS-PAGE. Western blot were used to determine immunoreactivity of rHpaA by a rabbit polyclonal antibodies against whole cell of H. pylori.Results: The HPAA gene nucleotide sequence in the recombinant plasmid vector of pET-28a- HPAA was consistent with that of H.pylori HPAA as published in the GenBank. SDS-PAGE demonstrated that the constructed prokaryotic expression efficiently produced rHpaA at the 1.5mmol/L of IPTG. HPAA fusion protein was able to react with the rabbit polyclonal antibody against whole cells of H. pylori.Conclusion: A prokaryotic expression system pET-28a-hpaA-BL21 with high efficiency of H. pylori HPAA gene was successfully established and the HPAA fusion protein showed satisfactory immunoreactivity. These results indicate that production of a specific RECOMBINANT PROTEIN is an alternative and potentially more expeditious strategy for development of H. pylori vaccine.

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APA: Copy

NAJAR PIRAYEH, SH., OTOUFI, J., HOSSEINKHANI, S., & FARSHCHIAN, MOEIN. (2009). CLONING AND EXPRESSION OF HELICOBACTER PYLORI HPAA GENE. CELL JOURNAL (YAKHTEH), 11(3 (43)), 273-276. SID. https://sid.ir/paper/16262/en

Vancouver: Copy

NAJAR PIRAYEH SH., OTOUFI J., HOSSEINKHANI S., FARSHCHIAN MOEIN. CLONING AND EXPRESSION OF HELICOBACTER PYLORI HPAA GENE. CELL JOURNAL (YAKHTEH)[Internet]. 2009;11(3 (43)):273-276. Available from: https://sid.ir/paper/16262/en

IEEE: Copy

SH. NAJAR PIRAYEH, J. OTOUFI, S. HOSSEINKHANI, and MOEIN FARSHCHIAN, “CLONING AND EXPRESSION OF HELICOBACTER PYLORI HPAA GENE,” CELL JOURNAL (YAKHTEH), vol. 11, no. 3 (43), pp. 273–276, 2009, [Online]. Available: https://sid.ir/paper/16262/en

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