Intact long-type DupA protein in Helicobacter pylori is an ATPase involved in multifunctional biological activities

Microbial Pathogenesis
Ming-yi WangShihe Shao

Abstract

The function of intact long-type DupA protein in Helicobacter pylori was analyzed using immunoblotting and molecular biology techniques in the study. After cloning, expression and purification, ATPase activity of DupA protein was detected. Antibody was produced for localization and interaction proteins analysis. The dupA-deleted mutant was generated for adhesion and CagA protein translocation assay, susceptibility to different pH, IL-8 secretion assay, cytotoxicity to MKN-45 cells and proteins-involved apoptosis analysis. DupA protein exhibited an ATPase activity (129.5±17.8 U/mgprot) and located in bacterial membrane, while it did not involve the adhesion and CagA protein delivery of H. pylori. DupA protein involved the urease secretion as the interaction proteins. The wild type strain had a stronger growth in low pH than the dupA-deleted mutant (p < 0.001). IL-8 productions from GES-1 cells infected with the wild type strain were significantly higher than from those with the mutant (p < 0.001). The amounts of vital MKN-45 cells were decreased and the numbers of apoptotic cells were increased with the wild type strain, compared to those with the mutant after 12 h (p < 0.05). The increase of cleaved Caspase-3 and Bax was signif...Continue Reading

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Citations

Sep 9, 2015·Future Microbiology·Ming-Yi WangXiao-Zhong Gao
Jun 22, 2018·Future Microbiology·Xiao-Yan YuanMing-Yi Wang
Jun 13, 2019·Journal of Cellular Physiology·Masoud KeikhaMohsen Karbalaei
Dec 29, 2016·World Journal of Gastroenterology : WJG·Amin Talebi Bezmin Abadi, Guillermo Perez-Perez
Sep 15, 2020·World Journal of Gastroenterology : WJG·Jawed AlamAsish K Mukhopadhyay

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