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...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Conference item |
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2006
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| _version_ | 1826305294327611392 |
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| author | Cordes, F Kraiczy, P Roversi, P Simon, M Brade, V Jahraus, O Wallis, R Goodstadt, L Ponting, C Skerka, C Zipfel, P Wallich, R Lea, S |
| author_facet | Cordes, F Kraiczy, P Roversi, P Simon, M Brade, V Jahraus, O Wallis, R Goodstadt, L Ponting, C Skerka, C Zipfel, P Wallich, R Lea, S |
| author_sort | Cordes, F |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T06:30:44Z |
| format | Conference item |
| id | oxford-uuid:f5e73abb-cfb0-44fc-9729-a096b68faa63 |
| institution | University of Oxford |
| last_indexed | 2024-03-07T06:30:44Z |
| publishDate | 2006 |
| record_format | dspace |
| spelling | oxford-uuid:f5e73abb-cfb0-44fc-9729-a096b68faa632022-03-27T12:30:52ZStructure-function mapping of BbCRASP-1, the key complement factor H and FHL-1 binding protein of Borrelia burgdorferi.Conference itemhttp://purl.org/coar/resource_type/c_5794uuid:f5e73abb-cfb0-44fc-9729-a096b68faa63Symplectic Elements at Oxford2006Cordes, FKraiczy, PRoversi, PSimon, MBrade, VJahraus, OWallis, RGoodstadt, LPonting, CSkerka, CZipfel, PWallich, RLea, SBorrelia 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. |
| spellingShingle | Cordes, F Kraiczy, P Roversi, P Simon, M Brade, V Jahraus, O Wallis, R Goodstadt, L Ponting, C Skerka, C Zipfel, P Wallich, R Lea, S Structure-function mapping of BbCRASP-1, the key complement factor H and FHL-1 binding protein of Borrelia burgdorferi. |
| title | Structure-function mapping of BbCRASP-1, the key complement factor H and FHL-1 binding protein of Borrelia burgdorferi. |
| title_full | Structure-function mapping of BbCRASP-1, the key complement factor H and FHL-1 binding protein of Borrelia burgdorferi. |
| title_fullStr | Structure-function mapping of BbCRASP-1, the key complement factor H and FHL-1 binding protein of Borrelia burgdorferi. |
| title_full_unstemmed | Structure-function mapping of BbCRASP-1, the key complement factor H and FHL-1 binding protein of Borrelia burgdorferi. |
| title_short | Structure-function mapping of BbCRASP-1, the key complement factor H and FHL-1 binding protein of Borrelia burgdorferi. |
| title_sort | structure function mapping of bbcrasp 1 the key complement factor h and fhl 1 binding protein of borrelia burgdorferi |
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