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Katrin Haupt, Peter Kraiczy, Reinhard Wallich, Volker Brade, Christine Skerka, Peter F. Zipfel, Binding of Human Factor H-Related Protein 1 to Serum-Resistant Borrelia burgdorferi Is Mediated by Borrelial Complement Regulator-Acquiring Surface Proteins, The Journal of Infectious Diseases, Volume 196, Issue 1, 1 July 2007, Pages 124–133, https://doi.org/10.1086/518509
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Abstract
Background. Isolates of Borrelia burgdorferi, the causative agent of Lyme disease, express up to 5 distinct complement regulator-acquiring surface proteins (CRASP-1, -2, -3, -4, and -5).
Methods. By use of ligand affinity blotting, enzyme-linked immunosorbent assay, surface plasmon resonance, and functional complement assays, we have identified factor H-related protein 1 (FHR-1) as a novel protein that binds to the bacterium via CRASP-3, -4, and -5.
Results. When incubated in serum, serum-resistant Borrelia burgdorferi strain LW2 bind FHR-1, an additional member of the human factor H protein family, and, similarly, 2 mouse FHR proteins bind to the surface. Recombinant FHR-1 binds to 3 borrelial surface proteins (CRASP-3, -4, and -5) but not to CRASP-1 and -2. A comparative analysis of the individual CRASPs revealed common as well as distinct binding profiles for the 3 human regulators. FHR-1 binds to 3 CRASPs, and factor H binds to all 5 CRASPs. In addition, factor H-like protein 1 interacts with CRASP-1 and -2 but with no other borrelial proteins.
Conclusions. Thus, by expressing multiple surface proteins with different binding properties, the pathogen can attach a unique combination of host complement regulators to its surface. For the pathogen, this type of surface decoration and specific acquisition of different host plasma proteins allows fine-tuning of the host immune attack.
- lyme disease
- enzyme-linked immunosorbent assay
- borrelia burgdorferi
- complement system proteins
- complement factor h
- fetal heart rate
- ligands
- membrane proteins
- surface plasmon resonance
- bacteria
- mice
- pathogenic organism
- plasma proteins
- affinity
- human factors engineering
- binding (molecular function)
- host (organism)