Abstract
It remains uncovered yet how the common gastric pathogen, Helicobacter pylori, survives through the acidic barrier and the immune response simultaneously in the stomach. Herein we report a unique GroES chaperonin that effectively inactivates Helicobacter pylori urease in Escherichia coli model. Such a function depends on the quaternary structure as well as the metal binding at the C terminus. Surprisingly, the C-terminal metal capacity seems not closely relevant to the apparent urease inactivation. Our findings have possibly revealed a survival strategy of Helicobacter pylori after its gastric localization.
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Cun, S., Sun, H. Urease inactivation by an unusual GroES chaperonin. Sci. China Chem. 57, 842–848 (2014). https://doi.org/10.1007/s11426-014-5088-9
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DOI: https://doi.org/10.1007/s11426-014-5088-9