BINDING OF C-REACTIVE PROTEIN TO C-CARBOHYDRATE AND PC-SUBSTITUTED PROTEIN

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Abstract
Human CRP and the CRPs of other species bind Ca2+ ion. After binding of the divalent cation, CRP binds all phosphate monoesters with a stochiometry of one mole per mole of CRP subunit. Replacement of the phosphate monoester group by other acidic groups or by conversion to a phosphodiester markedly diminishes or abolishes the ability to bind. Phosphorylcholine is bound by CRP with much higher affinity than other phosphate monoesters speaking for a second binding site with specificity for the positively charged trimethylammonium group. The distance separating the phosphate from the positively charged group may be relevant. Protein that has been coupled with phosphorylcholine or phosphorylethanolamine is able to precipitate with CRP. Several natural substances including pneumococcal-C polysaccharide which react with CRP have been found to contain phosphorylcholine. In addition CRP has another binding site accounting for its ability to react with depyruvylated type 4 pneumococcal polysaccharide which does not contain phosphate or choline.