Chapter category: Immunology
C-Reactive Protein: Structure, Synthesis and Function
Immunobiology of Carbohydrates
Edited by: Simon Y.C. Wong and Gemma ArsequellISBN: 0-306-47844-7
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Chapter authors:
Terry W. Du Clos and Carolyn Mold
C-reactive protein (CRP) is an acute phase serum protein in man and a member of the pentraxin family of proteins. The pentraxins are conserved on an evolutionary basis having shared structural features across invertebrate and vertebrate species. The pentraxins share a novel cyclic pentameric structure that is resistant to heat and protease attack. Each of the five identical subunits has a shallow binding pocket on the binding face that binds phosphocholine and other ligands in a calcium-dependent manner. The other face of the pentraxin is responsible for receptor and C1q binding. CRP shares many properties with the adaptive immune system mediator, immunoglobulin. CRP binds to bacterial polysaccharides and glycolipids, damaged membranes and exposed nuclear antigens. This leads to binding of C1q and activation of the classical complement cascade resulting in the fixation of prophagocytic complement split products. CRP also has been shown to bind to the Fc receptors and to enhance phagocytosis of particulate antigens and microorganisms. The interaction of CRP with receptor-bearing cells is a stimulus for cytokine production. CRP is therefore one of the prototypic members of the innate immune system providing a recognition molecule for altered self material and foreign invaders. Through fixation of complement and interaction with Fc receptors clearance of effete cells or foreign invaders is enhanced in a noninflammatory manner. Thus CRP is a multifunctional protein whose roles in inflammation, host defense and autoimmunity are being intensively explored.
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