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

Hoy B, Loewer M, Weydig C, Carra G, Tegtmeyer N, Geppert T, Schroeder P, Sewald N, Backert S, Schneider G, Wessler S (2010)


Publication Type: Journal article

Publication year: 2010

Journal

Book Volume: 11

Pages Range: 798-804

Journal Issue: 10

DOI: 10.1038/embor.2010.114

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. © 2010 European Molecular Biology Organization.

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APA:

Hoy, B., Loewer, M., Weydig, C., Carra, G., Tegtmeyer, N., Geppert, T.,... Wessler, S. (2010). Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion. EMBO Reports, 11(10), 798-804. https://doi.org/10.1038/embor.2010.114

MLA:

Hoy, Benjamin, et al. "Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion." EMBO Reports 11.10 (2010): 798-804.

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