{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T22:39:26Z","timestamp":1768516766448,"version":"3.49.0"},"reference-count":43,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,3,14]],"date-time":"2005-03-14T00:00:00Z","timestamp":1110758400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Br J Haematol"],"published-print":{"date-parts":[[2005,4]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p> <jats:italic>Streptococcus sanguis<\/jats:italic> is the most common oral bacterium causing infective endocarditis and its ability to adhere to platelets, leading to their activation and aggregation, is thought to be an important virulent factor. Previous work has shown that <jats:italic>S. sanguis<\/jats:italic> can bind directly to platelet glycoprotein (GP) Ib but the nature of the adhesin was unknown. Here, we have shown that a high molecular weight glycoprotein of <jats:italic>S. sanguis<\/jats:italic> mediates adhesion to glycocalacin. The bacterial glycoprotein was purified from cell extracts by chromatography on GPIb\u2010 and wheatgerm agglutinin affinity matrices and its interaction with GPIb was shown to be sialic acid\u2010dependent. We designated the glycoprotein serine\u2010rich protein A (SrpA). An insertional inactivation mutant lacking the SrpA of <jats:italic>S. sanguis<\/jats:italic> showed significantly reduced binding to glycocalacin, reduced adherence to platelets and a prolonged lag time to platelet aggregation. In addition, under flow conditions, platelets rolled and subsequently adhered on films of wild\u2010type <jats:italic>S. sanguis<\/jats:italic> cells at low shear (50\/s) but did not bind to films of the SrpA mutant. Platelets did not bind to wild\u2010type bacterial cells at high shear (1500\/s). These findings help to understand the mechanisms by which the organism might colonize platelet\u2010fibrin vegetations.<\/jats:p>","DOI":"10.1111\/j.1365-2141.2005.05421.x","type":"journal-article","created":{"date-parts":[[2005,3,21]],"date-time":"2005-03-21T14:25:52Z","timestamp":1111415152000},"page":"101-109","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":175,"title":["A serine\u2010rich glycoprotein of <i>Streptococcus sanguis<\/i> mediates adhesion to platelets via GPIb"],"prefix":"10.1111","volume":"129","author":[{"given":"Christopher","family":"Plummer","sequence":"first","affiliation":[]},{"given":"Hui","family":"Wu","sequence":"additional","affiliation":[]},{"given":"Steven W.","family":"Kerrigan","sequence":"additional","affiliation":[]},{"given":"Gerardene","family":"Meade","sequence":"additional","affiliation":[]},{"given":"Dermot","family":"Cox","sequence":"additional","affiliation":[]},{"given":"C. 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