Unknown

Dataset Information

0

Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion.


ABSTRACT: Mammalian and prokaryotic high-temperature requirement A (HtrA) proteins are chaperones and serine proteases with important roles in protein quality control. Here, we describe an entirely new function of HtrA and identify it as a new secreted virulence factor from Helicobacter pylori, which cleaves the ectodomain of the cell-adhesion protein E-cadherin. E-cadherin shedding disrupts epithelial barrier functions allowing H. pylori designed to access the intercellular space. We then designed a small-molecule inhibitor that efficiently blocks HtrA activity, E-cadherin cleavage and intercellular entry of H. pylori.

SUBMITTER: Hoy B 

PROVIDER: S-EPMC2948180 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion.

Hoy Benjamin B   Löwer Martin M   Weydig Christiane C   Carra Gert G   Tegtmeyer Nicole N   Geppert Tim T   Schröder Peter P   Sewald Norbert N   Backert Steffen S   Schneider Gisbert G   Wessler Silja S  

EMBO reports 20100903 10


Mammalian and prokaryotic high-temperature requirement A (HtrA) proteins are chaperones and serine proteases with important roles in protein quality control. Here, we describe an entirely new function of HtrA and identify it as a new secreted virulence factor from Helicobacter pylori, which cleaves the ectodomain of the cell-adhesion protein E-cadherin. E-cadherin shedding disrupts epithelial barrier functions allowing H. pylori designed to access the intercellular space. We then designed a smal  ...[more]

Similar Datasets

| S-EPMC4895972 | biostudies-literature
| S-EPMC4794652 | biostudies-literature
2022-02-17 | PXD025360 | Pride
| S-EPMC4773856 | biostudies-literature
| S-EPMC3137895 | biostudies-literature
| S-EPMC6311382 | biostudies-literature