Abstract
An inhibitor of the adhesion of human platelets to collagen was identified in soluble extracts of the soft tick Ornithodoros Moubata and purified by four chromatographic steps. The isolated inhibitor, TAI (Tick Adhesion Inhibitor), is a ∼15-kDa protein that completely blocks the adhesion of platelets to collagen-coated microtiter plates with an IC50 of 8 nM. In the same concentration range it does not inhibit collagen-induced platelet aggregation or platelet adhesion to fibrinogen and has a partial inhibitory effect on platelet adhesion to fibronectin. TAI also blocks the adhesion of human endothelial cells to collagen, thus its inhibitory effect is not limited to platelets. TAI competes for the binding to platelets of a radiolabeled monoclonal antibody against the platelet glycoprotein Ia-IIa integrin complex. Based on its selective activity and small size, TAI is a promising new molecule for exploring cell-collagen interactions.
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