3D modeling of BmpA, BmpB, BmpC and BmpD from Borrelia burgdorfer | 44450
Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

+44 1223 790975

3D modeling of BmpA, BmpB, BmpC and BmpD from Borrelia burgdorferi

14th International Conference on Structural Biology

September 24-26, 2018 | Berlin, Germany

Mia Astrand, Julia Cuellar, Jukka Hytonen and Tiina A Salminen

Abo Akademi University, Finland
University of Turku, Finland

Posters & Accepted Abstracts: J Proteomics Bioinform

Abstract :

B. burgdorferi is one of the main Borrelia species causing Lyme disease in humans. The pathogens are transmitted by the Ixodes ticks and there are 60,000-200,000 Lyme disease infections in Europe annually. The BmpA, BmpB, BmpC and BmpD proteins are expressed by B. burgdorferi in infected patients, but the exact role of the proteins is still unknown. The Bmp proteins are reported to be homologous to T. pallidum PnrA (Purine nucleoside receptor A), which has been characterized as a substrate binding lipoprotein of the ATP binding cassette (ABC) transporter family, preferentially binding purine nucleosides. Based on our 3D homology models, the Bmp proteins share the typical fold of the substrate-binding protein family. Moreover, the residues involved in binding the ribose moiety of the nucleoside are highly conserved in the Bmp models, whereas the residues in the purine binding site are less conserved. In particular, the BmpC model has differences in the residues binding the base moiety of the nucleoside. In conclusion, the revealed differences indicate that the Bmp proteins could prefer different nucleosides and thus, might have distinct biological functions. Recent Publications: 1. Sykes R A (2014) An estimate of Lyme borreliosis incidence in Western Europe. Journal of Public Health DOI: 10.1093/ pubmed/fdw017. 2. Bryksin A V, Godfrey H P, Carbonaro C A, Wormser G P, Aguero-Rosenfeld M E and Cabello F C (2005) Borrelia burgdorferi BmpA, BmpB, and BmpD proteins are expressed in human infection and contribute to P39 immunoblot reactivity in patients with Lyme disease. Clinical and Diagnostic Laboratory Immunology 12:935�??40. 3. Ramamoorthy R, Povinelli L and Philipp M T (1996) Molecular characterization, genomic arrangement, and expression of bmpD, a new member of the bmp class of genes encoding membrane proteins of Borrelia burgdorferi. Infection and Immunity 64:1259�??1264. 4. Deka R K, Brautigam C A, Yang X F, Blevins J S, Machius M, Tomchick D R and Norgard M V (2006) The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucleoside receptor encoded within an ATPbinding cassette (ABC)-like operon in Treponema pallidum. Journal of Biological Chemistry 281(12):8072-81. 5. Deka R K, Brautigam C A, Biddy B A, Liu W Z and Norgard M V (2013) Evidence for an ABC-type riboflavin transporter system in pathogenic spirochetes. MBio DOI: 10.1128/mBio.00615-12.

Biography :