Identification of E-cadherin signature motifs functioning as cleavage sites for Helicobacter pylori HtrA
Thomas P. Schmidt, Anna M. Perna, Tim Fugmann, Manja Böhm, Jan Hiss, Sarah Haller, Camilla Götz, Nicole Tegtmeyer, Benjamin Hoy, Tilman T. Rau, Dario Neri, Steffen Backert, Gisbert Schneider & Silja Wessler
Abstract:
The cell adhesion protein and tumour suppressor E-cadherin exhibits important functions in the prevention of gastric cancer. The class-I carcinogen Helicobacter pylori (H. pylori) has developed a unique strategy to interfere with E-cadherin functions. H. pylori secretes the protease high temperature requirement A (HtrA) which cleaves off the E-cadherin ectodomain on epithelial cells. This opens cell-to-cell junctions, allowing bacterial transmigration across the epithelium. Here, we investigated the molecular mechanism of the HtrA-E-cadherin interaction and identified E-cadherin cleavage sites for HtrA.
The open access article can be found  here.

Reviewed by Hans Brandstetter