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

被引：57

作者：

Cordes, FS

Roversi, P

Kraiczy, P

Simon, MM

Brade, V

Jahraus, O

Wallis, R

Skerka, C

Zipfel, PF

Wallich, R

Lea, SM

机构：

[1] Univ Oxford, Lab Mol Biophys, Oxford OX1 3QU, England

[2] Univ Oxford, Glycobiol Inst, Oxford OX1 3QU, England

[3] Univ Hosp Frankfurt, Inst Med Microbiol, D-60596 Frankfurt, Germany

[4] Max Planck Inst Microbiol, D-79108 Freiburg, Germany

[5] Univ Heidelberg, Inst Immunol, Infect Immunol Grp, D-69120 Heidelberg, Germany

[6] Leibniz Inst Nat Prod Res & Infect Biol, D-07745 Jena, Germany

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2005年 / 12卷 / 03期

基金：

英国医学研究理事会; 英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

D O I：

10.1038/nsmb902

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：276 / 277

页数：2

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