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A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi

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Simon,  Markus M.
Metchnikoff Laboratory, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Citation

Cordes, F. S., Roversi, P., Kraiczy, P., Simon, M. M., Brade, V., Jahraus, O., et al. (2005). A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi. Nature Structural & Molecular Biology, 12, 276-277.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-9333-8
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.