摘要
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.
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.
基金
supported by Research Grants Council of Hong Kong (HKU7042/07P,HKU7049/09P and HKU7046/12P)
