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• W2138162801 abstract "ABSTRACT The concept of an infectious agent playing a role in cardiovascular disease is slowly gaining attention. Among several pathogens identified, the oral bacterium Streptococcus gordonii has been implicated as a plausible agent. Platelet adhesion and subsequent aggregation are critical events in the pathogenesis and dissemination of the infective process. Here we describe the identification and characterization of a novel cell wall-anchored surface protein, PadA (397 kDa), of S. gordonii DL1 that binds to the platelet fibrinogen receptor GPIIbIIIa. Wild-type S. gordonii cells induced platelet aggregation and supported platelet adhesion in a GPIIbIIIa-dependent manner. Deletion of the padA gene had no effect on platelet aggregation by S. gordonii but significantly reduced (>75%) platelet adhesion to S. gordonii . Purified N-terminal PadA recombinant polypeptide adhered to platelets. The padA mutant was unaffected in production of other platelet-interactive surface proteins (Hsa, SspA, and SspB), and levels of adherence of the mutant to fetuin or platelet receptor GPIb were unaffected. Wild-type S. gordonii , but not the padA mutant, bound to Chinese hamster ovary cells stably transfected with GPIIbIIIa, and this interaction was ablated by addition of GPIIbIIIa inhibitor Abciximab. These results highlight the growing complexity of interactions between S. gordonii and platelets and demonstrate a new mechanism by which the bacterium could contribute to unwanted thrombosis." @default.
• W2138162801 created "2016-06-24" @default.
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• W2138162801 date "2010-01-01" @default.
• W2138162801 modified "2023-10-16" @default.
• W2138162801 title "Human Platelets Recognize a Novel Surface Protein, PadA, on <i>Streptococcus gordonii</i> through a Unique Interaction Involving Fibrinogen Receptor GPIIbIIIa" @default.
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• W2138162801 doi "https://doi.org/10.1128/iai.00664-09" @default.
• W2138162801 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2798181" @default.
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