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 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.
Cordes
Frank S
FS
Laboratory of Molecular Biophysics, Department of Biochemistry, South Parks Road, Oxford, UK.
Roversi
Pietro
P
Kraiczy
Peter
P
Simon
Markus M
MM
Brade
Volker
V
Jahraus
Oliver
O
Wallis
Russell
R
Skerka
Christine
C
Zipfel
Peter F
PF
Wallich
Reinhard
R
Lea
Susan M
SM
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D001798:Blood Proteins / Q000378:metabolism; D003180:Complement C3b Inactivator Proteins; D017242:Complement Factor H / Q000378:metabolism; D019281:Dimerization; D008193:Lyme Disease / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D017510:Protein Folding; D017433:Protein Structure, Secondary
D001426:Bacterial Proteins; D001798:Blood Proteins; C493495:CFH protein, human; C517621:CFHR1 protein, human; D003180:Complement C3b Inactivator Proteins; D008565:Membrane Proteins; C440651:complement regulator-acquiring surface proteins, Borrelia burgdorferi; D017242:Complement Factor H