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Structure-function mapping of BbCRASP-1, the key complement factor H and FHL-1 binding protein of Borrelia burgdorferi

Borrelia burgdorferi, a spirochaete transmitted to human hosts during feeding of infected Ixodes ticks, is the causative agent of Lyme disease, the most frequent vector-borne disease in Eurasia and North America. Sporadically Lyme disease develops into a chronic, multisystemic disorder. Serum-resist...

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Main Authors: Cordes, Frank (Author) , Kraiczy, Peter (Author) , Roversi, Pietro (Author) , Simon, Markus M. (Author) , Brade, Volker (Author) , Jahraus, Oliver (Author) , Wallis, Russell (Author) , Goodstadt, Leo (Author) , Ponting, Chris P. (Author) , Skerka, Christine (Author) , Zipfel, Peter F. (Author) , Wallich, Reinhard (Author) , Lea, Susan M. (Author)
Format: Article (Journal)
Language:English
Published: 10 March 2006
In: International journal of medical microbiology
Year: 2006, Volume: 296, Pages: 177-184
ISSN:1618-0607
DOI:10.1016/j.ijmm.2006.01.011
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.ijmm.2006.01.011
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/abs/pii/S1438422106000129
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Author Notes:Frank S. Cordes, Peter Kraiczy, Pietro Roversi, Markus M. Simon, Volker Brade, Oliver Jahraus, Russell Wallis, Leo Goodstadt, Chris P. Ponting, Christine Skerka, Peter F. Zipfel, Reinhard Wallich, Susan M. Lea

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520 |a Borrelia burgdorferi, a spirochaete transmitted to human hosts during feeding of infected Ixodes ticks, is the causative agent of Lyme disease, the most frequent vector-borne disease in Eurasia and North America. Sporadically Lyme disease develops into a chronic, multisystemic disorder. Serum-resistant B. burgdorferi strains bind complement factor H (FH) and FH-like protein 1 (FHL-1) on the spirochaete surface. This binding is dependent on the expression of proteins termed complement-regulator acquiring surface proteins (CRASPs). The atomic structure of BbCRASP-1, the key FHL-1/FH-binding protein of B. burgdorferi, has recently been determined. Our analysis indicates that its protein topology apparently evolved to provide a high affinity interaction site for FH/FHL-1 and leads to an atomic-level hypothesis for the functioning of BbCRASP-1. This work demonstrates that pathogens interact with complement regulators in ways that are distinct from the mechanisms used by the host and are thus obvious targets for drug design. 
650 4 |a Amino Acid Sequence 
650 4 |a Bacterial Proteins 
650 4 |a Binding Sites 
650 4 |a Borrelia burgdorferi 
650 4 |a Complement C3b Inactivator Proteins 
650 4 |a Complement Factor H 
650 4 |a Humans 
650 4 |a Membrane Proteins 
650 4 |a Models, Molecular 
650 4 |a Molecular Sequence Data 
650 4 |a Protein Structure, Secondary 
650 4 |a Protein Structure, Tertiary 
650 4 |a Sequence Alignment 
650 4 |a Structure-Activity Relationship 
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