Urease inactivation by an unusual GroES chaperonin  

作　　者：CUN ShuJian SUN HongZhe 

机构地区：[1]Department of Chemistry,The University of Hong Kong [2]Department of Chemistry,The Scripps Research Institute

出　　处：《Science China Chemistry》2014年第6期842-848,共7页中国科学（化学英文版）

基　　金：supported by Research Grants Council of Hong Kong (HKU7042/07P,HKU7049/09P and HKU7046/12P)

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.

关 键 词：GroES chaperonin Helicobacter pylori metal binding microbial pathogenesis nickel urease inactivation 

分 类 号：TQ460.1[化学工程—制药化工]