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

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

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...

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Detaylı Bibliyografya
Asıl Yazarlar: Cordes, F, Roversi, P, Kraiczy, P, Simon, M, Brade, V, Jahraus, O, Wallis, R, Skerka, C, Zipfel, P, Wallich, R, Lea, S
Materyal Türü: Journal article
Dil:English
Baskı/Yayın Bilgisi: 2005
Diğer Bilgiler
Özet: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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