Adhesion of spirochetes from Borrelia burgdorferi sensu lato complex is the crucial step in early phase of Lyme disease infection. Decorin binding proteins (Dbp) are glycosaminoglycan (GAG) binding adhesins exposed on the surface of borrelia spirochetes. Dbps are expressed in two homologous forms A and B, both of them were characterized as main factors of borrelia virulence(1). Based on the previous described differences in binding mechanisms of Dbp-GAG interaction (2), we focused on the relations between structural differences and GAG binding. We aim to describe the structural differences in detail among Dbps from european Borelia species and their particular interactions with different GAGs using solution nuclear magnetic resonance (NMR) spectroscopy at atomic resolution. Almost complete backbone and sidechain assignments of DbpA from B. Afzelii and B. Bavariensis have been achieved. Predictions of secondary structure propensity for both variants, calculated from assigned chemical shifts, were compared with available NMR structures of North American borrelia species. Backbone dynamics was described by T1 and T2 spin relaxations and 1H 15N heteronuclear NOE (Nuclear Overhauser effect) experiments. We performed initial protein-GAG interaction studies of both variants of DbpA with different GAGs by NMR titrations including protein dynamics measurement by heteronuclear NOE experiments, hydrogen-deuterium exchange mass spectrometry (HDX-MS) and surface plasmon resonance (SPR) trial measurement. NMR-based prediction of secondary structure propensity and protein backbone dynamics combined with initial protein-ligand interaction experiments, which indicates interspecific differences in GAG binding, provided insight into structural characteristics of DbpA and will set the starting point for future extensive research of specific differences in structure and dynamics of Dbps and how it influence the interaction mechanism with GAG ligands.