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Borrelia burgdorferi has evolved many mechanisms of evading the different immune systems across its range of reservoir hosts, including the capture and presentation of host complement regulators factor H and factor H-like protein-1 (FHL-1). Acquisition is mediated by a family of complement regulator-acquiring surface proteins (CRASPs), of which the atomic structure of CspA (BbCRASP-1) is known and shows the formation of a homodimeric species which is required for binding. Mutagenesis studies have mapped a putative factor H binding site to a cleft between the two subunits. Presented here is a new atomic structure of CspA which shows a degree of flexibility between the subunits which may be critical for factor H scavenging by increasing access to the binding interface and allows the possibility that the assembly can clamp around the bound complement regulators.

Original publication




Journal article


Acta Crystallogr Sect F Struct Biol Cryst Commun

Publication Date





629 - 633


BbCRASP-1, Borrelia burgdorferi, CspA, complement, factor H, Bacterial Proteins, Borrelia burgdorferi, Complement Factor H, Crystallography, X-Ray, Membrane Proteins, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary