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Regulation of complement activation by C-reactive protein.
C Mold1, H Gewurz, T W Du Clos
1Department of Molecular Genetics and Microbiology, University of New Mexico, Albuquerque 87131, USA.
Immunopharmacology
|July 17, 1999
Summary
C-reactive protein (CRP) regulates innate immunity by binding to damaged cells and microbes. Surface-bound CRP recruits factor H, limiting complement system overactivation and inflammation.
Area of Science:
- Immunology
- Biochemistry
- Complement System
Background:
- C-reactive protein (CRP) is a key mediator of innate immunity.
- CRP binds to microbial polysaccharides and damaged cell ligands.
- CRP initiates complement activation via the classical pathway.
Purpose of the Study:
- To investigate the interaction between CRP and factor H.
- To elucidate the role of surface-bound CRP in regulating complement pathways.
- To identify the specific region of CRP involved in factor H binding.
Main Methods:
- Enzyme-linked immunosorbent assay (ELISA) to demonstrate factor H binding to CRP and C3b.
- Use of CRP peptides to map factor H binding sites.
- Analysis of complement pathway activation and regulation.
Main Results:
- Surface-bound CRP directly binds factor H.
- Factor H binding to CRP is independent of ligand binding sites but is mediated by a specific 13-amino acid peptide region.
- CRP-bound factor H regulates alternative pathway amplification and C5 convertases, limiting C5b-9 generation.
Conclusions:
- Surface-bound CRP acts as a docking site for factor H, enhancing complement regulation.
- This interaction limits excessive complement activation, reducing inflammatory damage.
- CRP plays a crucial role in balancing immune response and self-protection.