{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T11:36:52Z","timestamp":1790854612918,"version":"4.1.0"},"reference-count":81,"publisher":"Microbiology Society","issue":"3","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2009,3,1]]},"abstract":"<jats:p>The Lyme disease spirochaete,<jats:italic>Borrelia burgdorferi<\/jats:italic>, can invade and persistently infect its hosts' connective tissues. We now demonstrate that<jats:italic>B. burgdorferi<\/jats:italic>adheres to the extracellular matrix component laminin. The surface-exposed outer-membrane protein ErpX was identified as having affinity for laminin, and is the first laminin-binding protein to be identified in a Lyme disease spirochaete. The adhesive domain of ErpX was shown to be contained within a small, unstructured hydrophilic segment at the protein's centre. The sequence of that domain is distinct from any previously identified bacterial laminin adhesin, suggesting a unique mode of laminin binding.<\/jats:p>","DOI":"10.1099\/mic.0.024604-0","type":"journal-article","created":{"date-parts":[[2009,2,26]],"date-time":"2009-02-26T22:56:47Z","timestamp":1235689007000},"page":"863-872","source":"Crossref","is-referenced-by-count":62,"title":["The Borrelia burgdorferi outer-surface protein ErpX binds mammalian laminin"],"prefix":"10.1099","volume":"155","author":[{"given":"Catherine A.","family":"Brissette","sequence":"first","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky College of Medicine, Lexington, KY 40536-0298, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ashutosh","family":"Verma","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky College of Medicine, Lexington, KY 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