Lyme disease, caused by spirochetes in the Borrelia burgdorferi sensu lato complex, is the most prevalent vector-borne disease in the United States and Europe. Surface-exposed bacterial proteins called adhesins promote interaction of the bacteria with a host cell or the extracellular matrix (ECM) and are key mediators of bacterial colonization. Specifically, B. burgdorferi adhesins bind, among others, the host cell-associated integrin decorin, a small proteoglycan which is an essential component of connective tissues. The lp54 linear plasmid of B. burgdorferi sensu stricto carries a two-gene operon that encodes two surface lipoproteins, decorin-binding proteins A and B (DbpA and DbpB), responsible for decorin binding. Structural domains comprising this superfamily share the structure of this proteins. Decorin-binding protein A (DbpA) of Borrelia burgdorferi mediates bacterial adhesion to heparin and dermatan sulfate associated with decorin PMID:24842928,PMID:25695518.