CHARACTERIZATION OF ADHERENCE PROPERTIES OF THE VWFA-DOMAIN CONTAINING PROTEINS OF THE CAUSATIVE AGENT OF LYME DISEASE

Abstract

The bacterial spirochete Borrelia burgdorferi, the causative agent of Lyme disease (LD) encodes for the von Willebrand Factor A (VWFA) domain proteins BB0172 and BB0173. VWFA domains are commonly known for adhering to extracellular matrix components (ECM), glycoproteins and metaloproteases. In silico analysis shows both of these proteins as membrane proteins. Moreover, in vitro analysis shows that both proteins have a transmembrane domain that anchors the protein to the cellular membrane with the VWFA domain available outside of the cell. The use of binding assays will help determine whether BB0172 and BB0173 play a role in the adhesion of Borrelia burgdorferi to ECM components, such as, Collagen I and IV, Laminin, plasma and cellular Fibronectin, among others, together with the use of commercially available purified integrins (αvβ3, α5β1 and α3β1).