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Glycobiology Advance Access originally published online on August 7, 2003
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Glycobiology, 2003, Vol. 13, No. 11 785-794
© 2003 Oxford University Press

Biosynthesis of 3-O-sulfated heparan sulfate: unique substrate specificity of heparan sulfate 3-O-sulfotransferase isoform 5

Jinghua Chen2, Michael B. Duncan2, Kevin Carrick3, R. Marshall Pope3 and Jian Liu1,2

2 Division of Medicinal Chemistry and Natural Products, School of Pharmacy, CB#7360, University of North Carolina, Chapel Hill, NC 27599; and 3 Proteomic Core Facility, Department of Biochemistry, University of North Carolina, Chapel Hill, NC 27599

Received on June 5, 2003; revised on July 9, 2003; accepted on July 10, 2003

Heparan sulfate 3-O-sulfotransferase transfers sulfate to the 3-OH position of a glucosamine to generate 3-O-sulfated heparan sulfate (HS), which is a rare component in HS from natural sources. We previously reported that 3-O- sulfotransferase isoform 5 (3-OST-5) generates both an antithrombin-binding site to exhibit anticoagulant activity and a binding site for herpes simplex virus 1 glycoprotein D to serve as an entry receptor for herpes simplex virus. In this study, we characterize the substrate specificity of 3-OST-5 using the purified enzyme. The enzyme was expressed in insect cells using the baculovirus expression approach and was purified by using heparin-Sepharose and 3',5'-ADP- agarose chromatographies. As expected, the purified enzyme generates both an antithrombin binding site and a glycoprotein D binding site. We isolated IdoUA-AnMan3S and IdoUA-AnMan3S6S from nitrous acid–degraded 3-OST-5-modified HS (pH 1.5), suggesting that 3-OST-5 enzyme sulfates the glucosamine residue that is linked to an iduronic acid residue at the nonreducing end. We also isolated a disaccharide with a structure of {Delta}UA2S-GlcNS3S and a tetrasaccharide with a structure of {Delta}UA2S-GlcNS-IdoUA2S-GlcNH23S6S from heparin lyases–digested 3-OST-5-modified HS. Our results suggest that 3-OST-5 enzyme sulfates both N-sulfated glucosamine and N-unsubstituted glucosamine residues. Taken together, the results indicate that 3-OST-5 has broader substrate specificity than those of 3-OST-1 and 3-OST-3. The unique substrate specificity of 3-OST-5 serves as an additional tool to study the mechanism for the biosynthesis of biologically active HS.

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


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