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Yersinia pestis , the causative agent of plague, evades host immune responses and rapidly causes disease. TheY. pestis adhesin Ail mediates host cell binding and is critical for Yop delivery. To identify the Ail receptor(s), Ail was purified following overexpression inEscherichia coli . Ail bound specifically to fibronectin, an extracellular matrix protein with the potential to act as a bridge between Ail and host cells. Ail expressed byE. coli also mediated binding to purified fibronectin, and Ail-mediatedE. coli adhesion to host cells was dependent on fibronectin. Ail expressed byY. pestis bound purified fibronectin, as did theY. pestis adhesin plasminogen activator (Pla). However, a KIM5 Δail mutant had decreased binding to host cells, while a KIM5 Δpla mutant had no significant defect in adhesion. Furthermore, treatment with antifibronectin antibodies decreased Ail-mediated adhesion by KIM5 and the KIM5 Δpla mutant, indicating that the Ail-fibronectin interaction was important for cell binding. Finally, antifibronectin antibodies inhibited the KIM5-mediated cytotoxicity of host cells in an Ail-dependent fashion. These data indicate that Ail is a key adhesin that mediates binding to host cells through interaction with fibronectin on the surface of host cells, and this interaction is important for Yop delivery byY. pestis .

Ail Binding to Fibronectin Facilitates Yersinia pestis Binding to Host Cells and Yop Delivery