{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["12(6)"],"submitter":["Choi S"],"pubmed_abstract":["Enterohemorrhagic <i>Escherichia coli</i> (EHEC) causes thrombotic microangiopathy, yet the red blood cell (RBC)-centered mechanism has remained unclear. We identify the RTX-family hemolysin EhxA as the driver of RBC-mediated thrombogenesis. Deletion of <i>ehxA</i> abolishes Ca<sup>2+</sup> influx, phosphatidylserine (PS) exposure, progression from discocyte to echinocyte to spherocyte, thrombin generation, RBC-endothelium adhesion, and RBC aggregation. Genetic complementation restores these readouts to wild type, and purified EhxA in bacteria-free assays recapitulates them while localizing to intact RBC membranes. By contrast, Δ<i>stx2</i> mutants do not elicit these RBC phenotypes, distinguishing this pathway from Shiga toxin-dependent effects. Multiple regression quantifies the link bet"],"journal":["Science advances"],"pagination":["eady8284"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12880542"],"repository":["biostudies-literature"],"pubmed_title":["RTX-family toxin EhxA drives morphological remodeling and thrombogenesis in RBCs during enterohemorrhagic &lt;i&gt;Escherichia coli&lt;/i&gt; infection."],"pmcid":["PMC12880542"],"pubmed_authors":["Choi S","Park H","Chung HY","Bian Y","Bae ON","Im H"],"additional_accession":[]},"is_claimable":false,"name":"RTX-family toxin EhxA drives morphological remodeling and thrombogenesis in RBCs during enterohemorrhagic &lt;i&gt;Escherichia coli&lt;/i&gt; infection.","description":"Enterohemorrhagic <i>Escherichia coli</i> (EHEC) causes thrombotic microangiopathy, yet the red blood cell (RBC)-centered mechanism has remained unclear. We identify the RTX-family hemolysin EhxA as the driver of RBC-mediated thrombogenesis. Deletion of <i>ehxA</i> abolishes Ca<sup>2+</sup> influx, phosphatidylserine (PS) exposure, progression from discocyte to echinocyte to spherocyte, thrombin generation, RBC-endothelium adhesion, and RBC aggregation. Genetic complementation restores these readouts to wild type, and purified EhxA in bacteria-free assays recapitulates them while localizing to intact RBC membranes. By contrast, Δ<i>stx2</i> mutants do not elicit these RBC phenotypes, distinguishing this pathway from Shiga toxin-dependent effects. Multiple regression quantifies the link bet","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-15T07:39:53.514Z","creation":"2026-07-01T03:07:47.54Z"},"accession":"S-EPMC12880542","cross_references":{"pubmed":["41650273"],"doi":["10.1126/sciadv.ady8284"]}}