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Urease inactivation by an unusual GroES chaperonin
Authors:ShuJian Cun  HongZhe Sun
Institution:1. Department of Chemistry, The University of Hong Kong, Hong Kong, China
2. Department of Chemistry, The Scripps Research Institute, La Jolla, CA, 92037, USA
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.
Keywords:GroES chaperonin  Helicobacter pylori  metal binding  microbial pathogenesis  nickel  urease inactivation
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