Buchumschlag

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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Hauptverfasser: 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)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 10 March 2006
In: International journal of medical microbiology
Year: 2006, Jahrgang: 296, Pages: 177-184
ISSN:1618-0607
DOI:10.1016/j.ijmm.2006.01.011
Online-Zugang: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
Volltext
Verfasserangaben: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
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 07.06.2021
Beschreibung:Online Resource
ISSN:1618-0607
DOI:10.1016/j.ijmm.2006.01.011

Ähnliche Einträge