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Glycobiology Advance Access published online on October 30, 2002
Glycobiology, doi:10.1093/glycob/cwg002
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Submitted on June 26, 2002
Revised on August 20, 2002
Accepted on August 23, 2002

© 2002 Oxford University Press

ORIGINAL ARTICLES

Carbohydrate-binding properties of human neoCRP and its relationship to phosphorylcholine-binding site

Reiko T. Lee 1 Yuan C. Lee 1*

1 Department of Biology, The Johns Hopkins University, Baltimore, MD 21218, USA

* To whom correspondence should be addressed. E-mail: reiko.lee{at}jhu.edu.

Abstract

Binding characteristics of two types of ligands for human neo-C-reactive protein (neoCRP), which is a conformationally altered but physiologically relevant form of CRP, were studied fluorometrically by probing CRP immobilized on polystyrene surface with europium-labeled ligands. Two Eu-ligands used were bovine serum albumin (BSA) derivatives that contain on the average 40 residues of ligand structures, one derivative containing phosphorylcholine (PC) and the other lactosyl residues. The PC-containing ligands required the presence of calcium for binding, whereas galactose-containing derivatives bound in the absence of calcium. The optimal pH for the PC-dependent binding was broad (pH 6-8), whereas the best binding pH for the galactose-dependent binding was around 6. The carbohydrate-mediated binding is rather non-specific: the binding site prefers galactose configuration but other hexoses can be accommodated. The two best monosaccharide inhibitors at this site were galactose-6-phosphate and galacturonic acid, suggesting the importance of having a negatively charged group at C-6 position of galactose. In fact, the phosphate-binding site is common to both PC and sugar phosphates, and the choline- and the sugar-binding sites are probably located on either side of the phosphate-binding site. Binding characteristics of Eu-labeled PC-BSA to neoCRP are quite similar to that found for native CRP in solution phase [Lee et al. (2002) J. Biol. Chem. 277, 225-232], whereas binding of sugar phosphates by neoCRP shows considerably less stringent requirement compared to native CRP. For instance, galactose-{alpha}1-phosphate was not inhibitory at all in the native CRP binding assay, whereas it was a good inhibitor in the neoCRP assay.


Key word: Carbohydrate ligand/ C-reactive protein (CRP)/ fluorometric determination/neo-CRP/phosphoryl choline
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