| Literature DB >> 26452603 |
David C Watson1, Warren W Wakarchuk2, Christian Gervais3, Yves Durocher3, Anna Robotham1, Steve M Fernandes4, Ronald L Schnaar4, N Martin Young1, Michel Gilbert5.
Abstract
Legionaminic 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.Entities:
Keywords: GD1a; Human ST6Gal1 sialyltransferase; Interferon-α2b; Porcine ST3Gal1 sialyltransferase; α1-antitrypsin
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Year: 2015 PMID： 26452603 DOI： 10.1007/s10719-015-9624-4
Source DB: PubMed Journal: Glycoconj J ISSN： 0282-0080 Impact factor: 2.916