{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9(8)"],"submitter":["Tohidpour A"],"pubmed_abstract":["Cytotoxin-associated gene product A (CagA) is a major virulence factor secreted by <i>Helicobacter pylori</i>. CagA activity in the gastric epithelium is associated with higher risk of gastric cancer development. Bacterial type IV secretion system (T4SS)-mediated translocation of CagA into the cytosol of human epithelial cells occurs via a poorly understood mechanism that requires CagA interaction with the host membrane lipid phosphatidylserine (PS) and host cell receptor integrin α₅β₁. Here we have characterized the isolated recombinant middle fragment of CagA (CagA-M) that contains the positively-charged PS-binding region (aa 613-636) and a putative β₁ integrin binding site, but lacks the EPIYA region, secretion signal peptide and the CagA multimerization motif. We show that CagA-M, when"],"journal":["Toxins"],"pagination":["E237"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5577571"],"repository":["biostudies-literature"],"pubmed_title":["The Middle Fragment of Helicobacter pylori CagA Induces Actin Rearrangement and Triggers Its Own Uptake into Gastric Epithelial Cells."],"pmcid":["PMC5577571"],"pubmed_authors":["Roujeinikova A","Kwok T","Gorrell RJ","Tohidpour A"],"additional_accession":[]},"is_claimable":false,"name":"The Middle Fragment of Helicobacter pylori CagA Induces Actin Rearrangement and Triggers Its Own Uptake into Gastric Epithelial Cells.","description":"Cytotoxin-associated gene product A (CagA) is a major virulence factor secreted by <i>Helicobacter pylori</i>. CagA activity in the gastric epithelium is associated with higher risk of gastric cancer development. Bacterial type IV secretion system (T4SS)-mediated translocation of CagA into the cytosol of human epithelial cells occurs via a poorly understood mechanism that requires CagA interaction with the host membrane lipid phosphatidylserine (PS) and host cell receptor integrin α₅β₁. Here we have characterized the isolated recombinant middle fragment of CagA (CagA-M) that contains the positively-charged PS-binding region (aa 613-636) and a putative β₁ integrin binding site, but lacks the EPIYA region, secretion signal peptide and the CagA multimerization motif. We show that CagA-M, when","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Jul","modification":"2026-05-02T05:49:15.722Z","creation":"2019-03-27T02:54:59Z"},"accession":"S-EPMC5577571","cross_references":{"pubmed":["28788072"],"doi":["10.3390/toxins9080237"]}}