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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism
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Bacterial Proteins / physiology
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Blood Proteins / metabolism
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Complement C3b Inactivator Proteins
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Complement Factor H / metabolism
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Dimerization
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Lyme Disease / metabolism
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Membrane Proteins / chemistry*
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Membrane Proteins / metabolism
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Membrane Proteins / physiology
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Protein Folding
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Protein Structure, Secondary
Substances
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Bacterial Proteins
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Blood Proteins
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CFH protein, human
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CFHR1 protein, human
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Complement C3b Inactivator Proteins
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Membrane Proteins
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complement regulator-acquiring surface proteins, Borrelia burgdorferi
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Complement Factor H