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

David C. Watson, Warren W. Wakarchuk, Christian Gervais, Yves Durocher, Anna Robotham, Steve M. Fernandes, Ronald L. Schnaar, N. Martin Young, Michel Gilbert

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)729-734
Number of pages6
JournalGlycoconjugate Journal
Issue number9
StatePublished - Dec 1 2015


  • GD1a
  • Human ST6Gal1 sialyltransferase
  • Interferon-α2b
  • Porcine ST3Gal1 sialyltransferase
  • α-antitrypsin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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