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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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Main Authors: Cordes, Frank (Author) , Roversi, Pietro (Author) , Kraiczy, Peter (Author) , Simon, Markus M. (Author) , Brade, Volker (Author) , Jahraus, Oliver (Author) , Wallis, Russell (Author) , Skerka, Christine (Author) , Zipfel, Peter F. (Author) , Wallich, Reinhard (Author) , Lea, Susan M. (Author)
Format: Article (Journal)
Language:English
Published: 13 February 2005
In: Nature structural & molecular biology
Year: 2005, Volume: 12, Issue: 3, Pages: 276-277
ISSN:1545-9985
DOI:10.1038/nsmb902
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Author Notes:Frank S. Cordes, Pietro Roversi, Peter Kraiczy, Markus M. Simon, Volker Brade, Oliver Jahraus, Russell Wallis, Christine Skerka, Peter F. Zipfel, Reinhard Wallich & Susan M. Lea
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Summary: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.
Item Description:Gesehen am 07.06.2021
Physical Description:Online Resource
ISSN:1545-9985
DOI:10.1038/nsmb902

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