Decorin binding proteins (Dbps) mediate attachment of spirochetes in host organisms during the early stages of Lyme disease infection. Previously, different binding mechanisms of Dbps to glycosaminoglycans have been elucidated for the pathogenic species Borrelia burgdorferi sensu stricto and B. afzelii. We are investigating various European Borrelia spirochetes and their interactions at the atomic level using NMR. We report preparative scale recombinant expression of uniformly stable isotope enriched B. afzelii DbpA in Escherichia coli, its chromatographic purification, and solution NMR assignments of its backbone and sidechain 1H, 13C, and 15N atoms. This data was used to predict secondary structure propensity, which we compared to the North American B. burgdorferi sensu stricto and European B. garinii DbpA for which solution NMR structures had been determined previously. Backbone dynamics of DbpA from B. afzelii were elucidated from spin relaxation and heteronuclear NOE experiments. NMR-based secondary structure analysis together with the backbone dynamics characterization provided a first look into structural differences of B. afzelii DbpA compared to the North American species and will serve as the basis for further investigation of how these changes affect interactions with host components.

Faculty of Science University of South Bohemia Branišovská 1760 37005 České Budějovice Czech Republic

Institute of Analytical Chemistry University of Vienna Währingerstraße 38 1090 Vienna Austria

Institute of Inorganic Chemistry Johannes Kepler University Altenbergerstraße 69 4040 Linz Austria

Institute of Organic Chemistry Johannes Kepler University Altenbergerstraße 69 4040 Linz Austria

Institute of Parasitology Biology Centre Czech Academy of Sciences Branišovská 31 37005 České Budějovice Czech Republic

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