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Journal of Endotoxin Research
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What's this?

The antimicrobial properties of C-reactive protein (CRP)

Sandra S.H. Tan

Department of Biological Sciences National University of Singapore, Singapore

Patricia M.L. Ng

Department of Biological Sciences National University of Singapore, Singapore

Bow Ho

Department of Microbiology, National University of Singapore, Singapore

Jeak Ling Ding

Department of Biological Sciences National University of Singapore, Singapore, dbsdjl{at}nus.edu.sg

C-reactive protein, CRP, is a predominant pattern-recognition receptor (PRR) in the plasma of the horseshoe crab, which recognizes lipopolysaccharide (LPS). Native CRP2 has previously been shown to exhibit agglutination activity against the polysialic capsule of Escherichia coli K1 but its role in bacterial clearance is not well characterized. In this work, the antimicrobial activity of a recombinant CRP2 isoform (rCRP2) was tested against E. coli, Pseudomonas aeruginosa and Staphylococcus aureus. rCRP2 agglutinates bacteria and exhibits bactericidal activity against Gram-negative bacteria. In addition, the antimicrobial activity of rCRP2 is calcium-independent. GST pulldown experiments suggest that in the naïve physiological state, CRP2 interacts with hemocyanin, native CRPs, a 35-kDa plasma lectin and an as yet unidentified 40-kDa protein. This interaction was enhanced upon Pseudomonas infection. We propose that rCRP2 is a PRR with potent antimicrobial activity and its interacting partners contribute to effective bacterial clearance.

Key Words: C-reactive protein • horseshoe crab • endotoxin • lipopolysaccharide • antimicrobial activity

Journal of Endotoxin Research, Vol. 11, No. 4, 249-256 (2005)
DOI: 10.1177/09680519050110040101
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