期刊
MICROBES AND INFECTION
卷 14, 期 5, 页码 470-476出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.micinf.2011.12.003
关键词
Helicobacter pylori; CagA; Cell motility; SHP2; PAR1/MARK
资金
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan
- Grants-in-Aid for Scientific Research [22114002, 22240085] Funding Source: KAKEN
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. (c) 2011 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.
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