Helicobacter pylori stimulates epithelial cell migration via CagA-mediated perturbation of host cell signaling

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• 作者：Kenji Kikuchi^a ; ^b ; Naoko Murata-Kamiya^a ; Satoshi Kondo^b ; Masanori Hatakeyama^a ; ^{mhata@m.u-tokyo.ac.jp}
• 关键词：Helicobacter pylori ; CagA ; Cell motility ; SHP2 ; PAR1/MARK
• 刊名：Microbes and Infection
• 出版年：2012
• 期刊代码：65_12864579
• 类别：imm
• 出版时间：May, 2012
• 卷：14
• 期：5
• 页码：470-476
• 文件大小：760 K

摘要

Helicobacter pylori CagA is delivered into gastric epithelial cells, where undergoes tyrosine phosphorylation at the Glu-Pro-Ile-Tyr-Ala (EPIYA) motif to interact with Src homology 2-containing protein tyrosine phosphatase-2 (SHP2) oncoprotein. CagA also binds to partitioning-defective 1 (PAR1) polarity-regulating kinase via the CagA multimerization (CM) sequence. To investigate pathophysiological role of CagA-SHP2 and/or CagA-PAR1 interaction in H. pylori infection, we generated H. pylori isogenic strains producing a phosphorylation-resistant CagA and a CagA without CM sequence. Infection studies revealed that deregulation of epithelial cell motility was more prominent in the wild-type strain than in the mutant strains. Thus, both CagA-SHP2 and CagA-PAR1 interactions are involved in the pathogenicity of cagA-positive H. pylori.