<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>9(8)</volume><submitter>Tohidpour A</submitter><pubmed_abstract>Cytotoxin-associated gene product A (CagA) is a major virulence factor secreted by &lt;i>Helicobacter pylori&lt;/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</pubmed_abstract><journal>Toxins</journal><pagination>E237</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5577571</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>The Middle Fragment of Helicobacter pylori CagA Induces Actin Rearrangement and Triggers Its Own Uptake into Gastric Epithelial Cells.</pubmed_title><pmcid>PMC5577571</pmcid><pubmed_authors>Roujeinikova A</pubmed_authors><pubmed_authors>Kwok T</pubmed_authors><pubmed_authors>Gorrell RJ</pubmed_authors><pubmed_authors>Tohidpour A</pubmed_authors></additional><is_claimable>false</is_claimable><name>The Middle Fragment of Helicobacter pylori CagA Induces Actin Rearrangement and Triggers Its Own Uptake into Gastric Epithelial Cells.</name><description>Cytotoxin-associated gene product A (CagA) is a major virulence factor secreted by &lt;i>Helicobacter pylori&lt;/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</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Jul</publication><modification>2026-05-02T05:49:15.722Z</modification><creation>2019-03-27T02:54:59Z</creation></dates><accession>S-EPMC5577571</accession><cross_references><pubmed>28788072</pubmed><doi>10.3390/toxins9080237</doi></cross_references></HashMap>