Abstract
Borrelia burgdorferi, a spirochete transmitted to human hosts during feeding of infected Ixodes ticks, is the causative agent of Lyme disease. Serum-resistant B. burgdorferi strains cause a chronic, multisystemic form of the disease and bind complement factor H (FH) and FH-like protein 1 (FHL-1) on the spirochete surface. Here we report the atomic structure for the key FHL-1- and FH-binding protein BbCRASP-1 and reveal a homodimer that presents a novel target for drug design.
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Acknowledgements
Thanks to M. Walsh at BM14 and the staff of ID14-4 and ID29 at the European Synchrotron Radiation Facility for assistance with data collection and to M. Morgan for assistance with the crystallization robot in the Laboratory of Molecular Biophysics, Oxford. The authors are indebted for the financial support of the Wellcome Trust (studentship to F.S.C., no. 059380), the UK Biotechnology and Biological Sciences Research Council (43/B16601 to S.M.L.), the UK Medical Research Council and the Deutsche Forschungsgemeinschaft.
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Supplementary Table 1
Data collection, phasing and refinement statistics. (PDF 63 kb)
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Cordes, F., Roversi, P., Kraiczy, P. et al. A novel fold for the factor H–binding protein BbCRASP-1 of Borrelia burgdorferi. Nat Struct Mol Biol 12, 276–277 (2005). https://doi.org/10.1038/nsmb902
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DOI: https://doi.org/10.1038/nsmb902
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