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

0555372 - BC 2022 RIV DE eng J - Journal Article
Hejduk, Libor - Rathner, P. - Strnad, Martin - Grubhoffer, Libor - Štěrba, J. - Rego, Ryan O. M. - Müller, N. - Rathner, A.
Resonance assignment and secondary structure of DbpA protein from the European species, Borrelia afzelii.
Biomolecular NMR Assignments. Roč. 15, č. 2 (2021), s. 415-420. ISSN 1874-2718. E-ISSN 1874-270X
R&D Projects: GA MŠMT(CZ) LTARF18021; GA ČR(CZ) GA18-27204S; GA MŠMT(CZ) 8J20AT024
Institutional support: RVO:60077344
Keywords : decorin-binding-protein * burgdorferi * backbone * NMR resonance assignment * Decorin-binding proteins * Borrelia afzelii
OECD category: Biochemistry and molecular biology
Impact factor: 0.731, year: 2021
Method of publishing: Open access
https://link.springer.com/article/10.1007/s12104-021-10039-2

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 H-1, C-13, and N-15 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.
Permanent Link: http://hdl.handle.net/11104/0329889