A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi.
Cordes FS., Roversi P., Kraiczy P., Simon MM., Brade V., Jahraus O., Wallis R., Skerka C., Zipfel PF., Wallich R., Lea SM.
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.