{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T14:41:36Z","timestamp":1791297696258,"version":"4.1.0"},"reference-count":61,"publisher":"The Company of Biologists","issue":"9-10","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2010,9,1]]},"abstract":"<jats:title>SUMMARY<\/jats:title>\n               <jats:p>Helicobacter pylori, a common pathogen that causes chronic gastritis and cancer, has evolved to establish persistent infections in the human stomach. Epidemiological evidence suggests that H. pylori with both highly active vacuolating cytotoxin A (VacA) and cytotoxin-associated gene A (CagA), the major virulence factors, has an advantage in adapting to the host environment. However, the mechanistic relationship between VacA and CagA remains obscure. Here, we report that CagA interferes with eukaryotic endocytosis, as revealed by genome-wide screening in yeast. Moreover, CagA suppresses pinocytic endocytosis and the cytotoxicity of VacA in gastric epithelial cells without affecting clathrin-dependent endocytosis. Our data suggest that H. pylori secretes VacA to attack distant host cells while injecting CagA into the gastric epithelial cells to which the bacteria are directly attached, thereby protecting these attached host cells from the cytotoxicity of VacA and creating a local ecological niche. This mechanism might allow H. pylori to balance damage to one population of host cells with the preservation of another, allowing for persistent infection.<\/jats:p>","DOI":"10.1242\/dmm.004879","type":"journal-article","created":{"date-parts":[[2010,8,4]],"date-time":"2010-08-04T02:26:49Z","timestamp":1280888809000},"page":"605-617","source":"Crossref","is-referenced-by-count":33,"title":["<i>Helicobacter pylori<\/i> CagA inhibits endocytosis of cytotoxin VacA in host cells"],"prefix":"10.1242","volume":"3","author":[{"given":"Junko K.","family":"Akada","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Functional Proteomics, Yamaguchi University Graduate School of Medicine, Ube, Yamaguchi 755-8505, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroki","family":"Aoki","sequence":"additional","affiliation":[{"name":"Department of Molecular Cardiovascular Biology, Yamaguchi University School of Medicine, Ube, Yamaguchi 755-8505, 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