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Glycobiology Advance Access originally published online on March 24, 2004
Glycobiology 2004 14(7):635-645; doi:10.1093/glycob/cwh077
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Glycobiology vol. 14 no. 7 © Oxford University Press 2004; all rights reserved.

Structural characterization of the bovine tracheal chondroitin sulfate chains and binding of Plasmodium falciparum–infected erythrocytes

Arivalagan Muthusamy, Rajeshwara N. Achur, Manojkumar Valiyaveettil, Subbarao V. Madhunapantula, Ikuko Kakizaki, Veer P. Bhavanandan and Channe D. Gowda1

Department of Biochemistry and Molecular Biology, Pennsylvania State University College of Medicine, 500 University Drive, Hershey, PA 17033

Received on January 21, 2004; accepted on March 10, 2004

Sequestration of Plasmodium falciparum–infected red blood cells (IRBCs) in the human placenta is mediated by chondroitin 4-sulfate (C4S). A cytoadherence assay using chondroitin sulfate proteoglycans (CSPGs) is widely used for studying C4S–IRBC interactions. Bovine tracheal chondroitin sulfate A (CSA) preparation lacking a major portion of core protein has been frequently used for the assay. Here the CSPG purified from bovine trachea and CSA were assessed for IRBC binding and the CS chains studied in detail for structure–activity relationship. The IRBCs bound at significantly higher density to the CSPG than CSA. The CS chains of CSPG/CSA are heterogeneous with varying levels of 4- and 6-sulfates, which are distributed such that ~80% of the 4-sulfated disaccharides are present as single and blocks of two or three separated by one to three 6-sulfated disaccharides. The remainder of the 4-sulfated disaccharides is present in blocks composed of 4–12 units, separated by 6-sulfated disaccharides. In the IRBC adherence inhibition analysis, CSA fragments with 88%–92% 4-sulfate were significantly less inhibitory than the intact CSA, indicating that the regions consisting of shorter 4-sulfated blocks efficiently bind IRBCs despite the presence of relatively high levels of 6-sulfate. This is because the 6-sulfated disaccharides have unsubstituted C-4 hydroxyls that are crucial for IRBC binding. The presence of high levels of 6-sulfate, however, significantly interfere with the IRBC binding activity of CSA, which otherwise would more efficiently bind IRBCs. Thus our study revealed the distribution pattern of 4- and 6-sulfate in bovine tracheal CSA and structural basis for IRBC binding.

1 To whom correspondence should be addressed; e-mail: gowda{at}psu.edu


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