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

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By Cordes FS, Roversi P, Kraiczy P, Simon MM, Brade V, Jahraus O, Wallis R, Skerka C, Zipfel PF, Wallich R, Lea SM • www.ProHealth.com • March 1, 2005


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.

Nat Struct Mol Biol. 2005 Mar;12(3):276-7. Epub 2005 Feb 13. Research Support, Non-U.S. Gov't





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