{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T23:57:13Z","timestamp":1790985433549,"version":"4.1.0"},"reference-count":48,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2011,1,10]],"date-time":"2011-01-10T00:00:00Z","timestamp":1294617600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2011,2]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p> <jats:italic>Leptospira<\/jats:italic> immunoglobulin\u2010like (Lig) proteins including LigA and LigB are adhesins that bind to fibronectin, collagen, laminin and elastin. In addition, Lig proteins are fibrinogen (Fg)\u2010binding proteins, although the physiological role of the Lig\u2013Fg interaction is unclear. In this study, a previously identified Fg\u2010binding region, LigBCen2 (amino acids 1014\u20131165 of LigB), has been further localized to LigBCen2R, which consists of the partial 11th and entire 12th Ig\u2010like domain (amino acids 1014\u20131119). LigBCen2R was found to bind to the C\u2010terminal \u03b1C domain of Fg (Fg\u03b1CC; amino acids 392\u2013644 in Fg \u03b1 chain; isothermal titration calorimetry, <jats:italic>K<jats:sub>D<\/jats:sub><\/jats:italic>\u2003=\u20030.375\u2003\u00b5M; fluorescence spectrometry, <jats:italic>K<jats:sub>D<\/jats:sub><\/jats:italic>\u2003=\u20030.364\u2003\u00b5M). The quenching and blue shift observed for the maximum wavelength intensities of the tryptophan fluorescence spectra for Fg\u03b1CCY570W upon LigBCen2RW1073C binding suggested an RGD motif close to the sole tryptophan on Fg\u03b1CCY570W was buried in LigBCen2R upon saturation with Fg\u03b1CC. A conformational change in LigBCen2R when bound to the Fg\u03b1CC RGD motif blocked further binding to integrin \u03b1<jats:sub>IIb<\/jats:sub>\u03b23 on platelets, thus preventing their aggregation. LigBCen2R binding to Fg\u03b1CC reduced clot formation but did not affect plasminogen and tissue\u2010type plasminogen activator interactions with Fg\u03b1CC. This study is the first to report that a spirochaetal protein binds to the C\u2010terminal \u03b1C domain of Fg, which regulates thrombosis and fibrinolysis, and may help explain the pulmonary haemorrhage and thrombocytopenia seen in clinical cases of leptospirosis.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2010.07510.x","type":"journal-article","created":{"date-parts":[[2010,12,14]],"date-time":"2010-12-14T12:04:49Z","timestamp":1292328289000},"page":"1063-1076","source":"Crossref","is-referenced-by-count":45,"title":["<i>Leptospira<\/i> immunoglobulin\u2010like protein B (LigB) binding to the C\u2010terminal fibrinogen \u03b1C domain inhibits fibrin clot formation, platelet adhesion and aggregation"],"prefix":"10.1111","volume":"79","author":[{"given":"Yi\u2010Pin","family":"Lin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sean 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