Identification and functional characterisation of
Complement Regulator Acquiring,Surface Protein-1 of serum
resistant Borrelia garinii OspA serotype 4.

BMC Microbiol. 2010 Feb 10;10(1):43 [Epub ahead of print]

Identification and functional characterisation of Complement
Regulator Acquiring Surface Protein-1 of serum resistant Borrelia
garinii OspA serotype 4.

van Burgel ND, Kraiczy P, Schuijt TJ, Zipfel PF, van Dam AP.

ABSTRACT: BACKGROUND: B. burgdorferi sensu lato (sl) is the
etiological agent of Lyme borreliosis in humans. Spirochetes have
adapted themselves to the human immune system in many distinct
ways. One important immune escape mechanism for evading
complement activation is the binding of complement regulators
Factor H
(CFH) or Factor H-like protein1 (FHL-1) to Complement
Regulator-Acquiring Surface Proteins (CRASPs).
RESULTS: We demonstrate that B. garinii OspA serotype
(ST4) PBi resist complement-mediated killing by binding of FHL-1.
To identify the primary ligands of FHL-1 four CspA orthologs from
B. garinii ST4 PBi were cloned and tested for binding to human
CFH and FHL-1. Orthologs BGA66 and BGA71 were found to be able to
bind both complement regulators but with different intensities.
In addition, all CspA orthologs were tested for binding to
mammalian and avian CFH. Distinct orthologs were able to bind to
CFH of different animal origins.
CONCLUSIONS: B. garinii ST4 PBi is able to evade complement
killing and can bind FHL-1 to membrane expressed proteins.
Recombinant proteins BGA66 can bind FHL-1 and human CFH, while
BGA71 can bind only FHL-1. All recombinant CspA orthologs from B.
garinii ST4 PBi can bind CFH from different animal origins. This
partly explains the wide variety of animals that can be infected
by B. garinii.

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PMID: 20146822 [PubMed - as supplied by publisher]