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...
| Main Authors: | , , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2005
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| _version_ | 1826275254096363520 |
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| author | Cordes, F Roversi, P Kraiczy, P Simon, M Brade, V Jahraus, O Wallis, R Skerka, C Zipfel, P Wallich, R Lea, S |
| author_facet | Cordes, F Roversi, P Kraiczy, P Simon, M Brade, V Jahraus, O Wallis, R Skerka, C Zipfel, P Wallich, R Lea, S |
| author_sort | Cordes, F |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T22:55:54Z |
| format | Journal article |
| id | oxford-uuid:605b7dd4-3fe0-41e5-9142-4c3f3311af36 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:55:54Z |
| publishDate | 2005 |
| record_format | dspace |
| spelling | oxford-uuid:605b7dd4-3fe0-41e5-9142-4c3f3311af362022-03-26T17:53:01ZA novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:605b7dd4-3fe0-41e5-9142-4c3f3311af36EnglishSymplectic Elements at Oxford2005Cordes, FRoversi, PKraiczy, PSimon, MBrade, VJahraus, OWallis, RSkerka, CZipfel, PWallich, RLea, SBorrelia 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. |
| spellingShingle | Cordes, F Roversi, P Kraiczy, P Simon, M Brade, V Jahraus, O Wallis, R Skerka, C Zipfel, P Wallich, R Lea, S A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi. |
| title | A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi. |
| title_full | A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi. |
| title_fullStr | A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi. |
| title_full_unstemmed | A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi. |
| title_short | A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi. |
| title_sort | novel fold for the factor h binding protein bbcrasp 1 of borrelia burgdorferi |
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