Structural characterization of Borrelia Burgdorferi protein BBA05 Laura Drunka 1 and Kalvis Brangulis 2 1 Latvian Institute of Organic Synthesis, Latvia 2 Latvian Biomedical Research and Study Centre, Latvia Borrelia Burgdorferi is Lyme disease-causing agent in humans that is transferred to the host with the help of Ixodes ticks. About 10 % of its 1.5 mbp genome encodes lipoprotein genes, many of which are important either for survival of B. Burgdorferi or its ability to infect the host. Therefore lipoproteins such as BBA05 are important objectives in Lyme disease research. Previous research suggest that BBA05 might not be essential for survival of B. Burgdorferi but it is unclear if there are other proteins that are compensating the loss of BBA05 or its role in the life cycle is non-essential. This protein can not be found throughout full life cycle of B. Burgdorferi but is expressed when nymphs are fed with blood, suggesting that expression might be induced either by temperature or components of the blood. In our study, we produced recombinant BBA05 and solved the crystal structure to answer some questions about its function. BBA05 is made from two domains (amino acids 140-276 and 277-417) consisting of seven and eight α-spirals, respectively. Despite the relatively low sequence similarity, solved structure appears to be similar to some of other proteins encoded in lp54 plasmid (BBA64 for example), although it is not mentioned in the literature as a member of PFam54 paralogous gene family. This work was supported by the Latvian Council of Science projects VPP-EM-BIOMEDICĪNA-2022/1-0001 and lzp-2021/1-0068. References
1. Casjens, S.et. al. Molecular Microbiology, 2002, 35 (3) , 490-516 2. Xu, H.et. al. Infection and Immunity, 2010, 78 (1) , 100-107 3. Brangulis, K.et. al. Acta Crystallographica Section D, 2013, 69 (6) , 1099-1107
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