期刊
MICROBIOLOGY AND IMMUNOLOGY
卷 49, 期 8, 页码 795-800出版社
WILEY
DOI: 10.1111/j.1348-0421.2005.tb03659.x
关键词
Streptococcus gordonii; adhesin; sialic acid; platelet glycoproteins
Aggregation of human platelets by Streptococcus gordonii DL1, an interaction implicated in the pathogenesis of infective endocarditis, requires the expression of hsa, the gene encoding the sialic acid-binding adhesin (Hsa) of this organism. To identify the sialoglycoproteins on the platelet surface as the receptors for Hsa, intrinsic membrane proteins were assessed by bacterial overlay assay. S. gordonii DL1 adhered to 130-140-kDa proteins, a reaction that was abolished by neuraminidase treatment of immobilized platelet surface proteins. These sialoglycoproteins were identified as platelet glycoprotein Ib alpha (GPIb alpha) and glycoprotein IIb (GPIIb) by immunoprecipitation with specific monoclonal antibody against each glycoprotein.
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