Journal
MICROBIOLOGY AND IMMUNOLOGY
Volume 49, Issue 8, Pages 795-800Publisher
WILEY
DOI: 10.1111/j.1348-0421.2005.tb03659.x
Keywords
Streptococcus gordonii; adhesin; sialic acid; platelet glycoproteins
Categories
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available