Preparation of legionaminic acid analogs of sialo-glycoconjugates by means of mammalian sialyltransferases

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DOIResolve DOI: http://doi.org/10.1007/s10719-015-9624-4
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TypeArticle
Journal titleGlycoconjugate Journal
ISSN0282-0080
1573-4986
Volume32
Issue9
Pages729734; # of pages: 6
Subjectα1-antitrypsin; GD1a; human ST6Gal1 sialyltransferase; interferon-α2b; porcine ST3Gal1 sialyltransferase
AbstractLegionaminic acids are analogs of sialic acid that occur in several bacteria. The most commonly occurring form is Leg5Ac7Ac, which differs from Neu5Ac only at the C7 (acetamido) and C9 (deoxy) positions. While these differences greatly reduce the susceptibility of Leg compounds to sialidases, several sialyltransferases have been identified that can use CMP-Leg5Ac7Ac as a donor (Watson et al. 2011). We report the successful modification with Leg5Ac7Ac of a glycolipid, GM1a, and two glycoproteins, interferon-α2b and α1-antitrypsin, by means of two mammalian sialyltransferases, namely porcine ST3Gal1 and human ST6Gal1. The Leg5Ac7Ac form of GD1a was not recognized by the myelin-associated glycoprotein (MAG, Siglec-4), confirming the importance of the glycerol moiety in the interaction of sialo-glycans with Siglecs.
Publication date
LanguageEnglish
AffiliationHuman Health Therapeutics; National Research Council Canada
Peer reviewedYes
NPARC number21276378
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Record identifiere3764399-a50a-4468-948e-930d1cbb45ef
Record created2015-10-07
Record modified2016-05-09
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