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Updated: Aug 17, 2026

Assays for Studying the Role of Vitronectin in Bacterial Adhesion and Serum Resistance
Published on: October 16, 2018
Localization of a vitronectin binding region of plasminogen activator inhibitor-1
1Department of Internal Medicine, Bowman Gray School of Medicine, Winston-Salem, NC 27157, USA.
Abstract:
The PAI-1 binding site for VN was studied using two independent methods. PAI-1 was cleaved by Staph V8 protease, producing 8 fragments, only 2 of which bound to [125I]-VN. These fragments were predicted to overlap between residues 91-130. Since PAI-2 has structural homology to PAI-1, but does not bind to vitronectin, chimeras of PAI-1 and PAI-2 were constructed. Four chimeras, containing PAI-1 residues 1-70, 1-105, 1-114, and 1-167 were constructed and expressed in vitro. PAI-1, PAI-2, and all of the chimeras retained inhibitory activity for t-PA, but only the chimera containing PAI-1 residues 1-167 formed a complex with VN. Together, these results predict that the VN binding site of PAI-1 is between residues 115-130.
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