Mutational analyses of the BbCRASP-1 protein of Borrelia burgdorferi identify residues relevant for the architecture and binding of host complement regulators FHL-1 and factor H.

Journal article

Borrelia burgdorferi exploits multiple strategies to evade host immune responses. One central immune escape mechanism is the inactivation of the host complement attack by acquisition host complement regulators FHL-1 and factor H via complement regulator-acquiring surface proteins (BbCRASPs). The BbCRASP-1 protein is the first bacterial factor H/FHL-1-binding protein for which the atomic structure has been solved. Previously, 3 regions including the C terminus were identified as putative conta...

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Authors: Kraiczy, P; Hanssen-Hübner, C; Kitiratschky, V; Brenner, C; Besier, S

• Publication status: Published
• Journal: International journal of medical microbiology : IJMM
• Volume: 299
• Issue: 4
• Pages: 255-268
• Publication date: 2009-04-01
• DOI: 10.1016/j.ijmm.2008.09.002
• EISSN: 1618-0607
• ISSN: 1438-4221
• Language: English
• Keywords: Protein Interaction Mapping; Membrane Proteins; Complement C3b Inactivator Proteins; Models, Molecular; Complement Factor H; DNA Mutational Analysis; Mutagenesis, Site-Directed; Protein Binding; Bacterial Proteins; Protein Structure, Tertiary; Borrelia burgdorferi; Amino Acid Substitution