| Online-Ressource |
Verfasst von: | Cordes, Frank [VerfasserIn]  |
| Kraiczy, Peter [VerfasserIn]  |
| Roversi, Pietro [VerfasserIn]  |
| Simon, Markus M. [VerfasserIn]  |
| Brade, Volker [VerfasserIn]  |
| Jahraus, Oliver [VerfasserIn]  |
| Wallis, Russell [VerfasserIn]  |
| Goodstadt, Leo [VerfasserIn]  |
| Ponting, Chris P. [VerfasserIn]  |
| Skerka, Christine [VerfasserIn]  |
| Zipfel, Peter F. [VerfasserIn]  |
| Wallich, Reinhard [VerfasserIn]  |
| Lea, Susan M. [VerfasserIn]  |
Titel: | Structure-function mapping of BbCRASP-1, the key complement factor H and FHL-1 binding protein of Borrelia burgdorferi |
Verf.angabe: | 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 |
E-Jahr: | 2006 |
Jahr: | 10 March 2006 |
Umfang: | 8 S. |
Fussnoten: | Gesehen am 07.06.2021 |
Titel Quelle: | Enthalten in: International journal of medical microbiology |
Ort Quelle: | München : Elsevier, 2000 |
Jahr Quelle: | 2006 |
Band/Heft Quelle: | 296(2006), Supplement 40, Seite 177-184 |
ISSN Quelle: | 1618-0607 |
Abstract: | 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. |
DOI: | doi:10.1016/j.ijmm.2006.01.011 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1016/j.ijmm.2006.01.011 |
| Volltext: https://www.sciencedirect.com/science/article/abs/pii/S1438422106000129 |
| DOI: https://doi.org/10.1016/j.ijmm.2006.01.011 |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | Amino Acid Sequence |
| Bacterial Proteins |
| Binding Sites |
| Borrelia burgdorferi |
| Complement C3b Inactivator Proteins |
| Complement Factor H |
| Humans |
| Membrane Proteins |
| Models, Molecular |
| Molecular Sequence Data |
| Protein Structure, Secondary |
| Protein Structure, Tertiary |
| Sequence Alignment |
| Structure-Activity Relationship |
K10plus-PPN: | 1759905097 |
Verknüpfungen: | → Zeitschrift |
Structure-function mapping of BbCRASP-1, the key complement factor H and FHL-1 binding protein of Borrelia burgdorferi / Cordes, Frank [VerfasserIn]; 10 March 2006 (Online-Ressource)