Kwok T, Zabler D, Urman S, Rohde M, Hartig R, Wessler S, Misselwitz R, Berger J, Sewald N, König W, Backert S (2007)
Publication Type: Journal article
Publication year: 2007
Book Volume: 449
Pages Range: 862-866
Journal Issue: 7164
DOI: 10.1038/nature06187
Integrins are important mammalian receptors involved in normal cellular functions as well as pathogenesis of chronic inflammation and cancer. We propose that integrins are exploited by the gastric pathogen and type-1 carcinogen Helicobacter pylori for injection of the bacterial oncoprotein cytotoxin-associated gene A (CagA) into gastric epithelial cells. Virulent H. pylori express a type-IV secretion pilus that injects CagA into the host cell; CagA then becomes tyrosine-phosphorylated by Src family kinases. However, the identity of the host cell receptor involved in this process has remained unknown. Here we show that the H. pylori CagL protein is a specialized adhesin that is targeted to the pilus surface, where it binds to and activates integrin α5β1 receptor on gastric epithelial cells through an arginine-glycine-aspartate motif. This interaction triggers CagA delivery into target cells as well as activation of focal adhesion kinase and Src. Our findings provide insights into the role of integrins in H.-pylori-induced pathogenesis. CagL may be exploited as a new molecular tool for our further understanding of integrin signalling. ©2007 Nature Publishing Group.
APA:
Kwok, T., Zabler, D., Urman, S., Rohde, M., Hartig, R., Wessler, S.,... Backert, S. (2007). Helicobacter exploits integrin for type IV secretion and kinase activation. Nature, 449(7164), 862-866. https://doi.org/10.1038/nature06187
MLA:
Kwok, Terry, et al. "Helicobacter exploits integrin for type IV secretion and kinase activation." Nature 449.7164 (2007): 862-866.
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