Resonance assignment and secondary structure of DbpA protein from the European species, Borrelia afzelii.

ABSTRACT: 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. bu

SUBMITTER: Hejduk L 

PROVIDER: S-EPMC8481140 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature