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OMVs activated complement more potently than parental bacteria or\u00a0homologous\u00a0LPS, independently of chemotype. A high molecular weight polysaccharide fraction, distinct from LPS, was recognized by serum mannose\u2010binding lectin (MBL).\n                    <jats:italic>In vivo<\/jats:italic>\n                    experiments demonstrated that complement depletion weakened the hallmarks of OMVs\u2010induced SIRS in mice. LPS chemotype affected the biodistribution of OMVs and long O\u2010specific polysaccharide protected them from clearance. Chemotype influenced OMVs secretion with their highest release by bacteria with LPS reduced to the inner core and lipid A (Rd1). The shift from environmental to host's temperature stimulated secretion of smaller OMVs, with less\u2010toxic, tetra\u2010acyl lipid A. Our data are consistent with a contribution of OMVs to\u00a0\n                    <jats:italic>Yersinia<\/jats:italic>\n                    pathogenicity through complement activation. Their potency as complex virulence factor is influenced by size, length of oligo\u2010\/polysaccharide chain, and lipid A form. This study comprehensively characterizes OMV\u2010complement interactions in YeO3, extending the knowledge of mechanisms previously established for other Gram\u2010negative bacteria.\n                  <\/jats:p>","DOI":"10.1002\/jev2.70270","type":"journal-article","created":{"date-parts":[[2026,4,17]],"date-time":"2026-04-17T13:02:48Z","timestamp":1776430968000},"source":"Crossref","is-referenced-by-count":1,"title":["<i>Yersinia enterocolitica<\/i>\n                    O:3 Outer Membrane Vesicles as a Platform for Complement Activation"],"prefix":"10.1002","volume":"15","author":[{"given":"C\u00e9dric","family":"Battaglino","sequence":"first","affiliation":[{"name":"Institute of Medical Biology Polish Academy of Sciences  Lodz Poland"},{"name":"BioMedChem Doctoral School of University of Lodz and Lodz Institutes of the Polish Academy of Sciences Lodz 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