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Glycoconj J. 2015 Dec;32(9):729-34. doi: 10.1007/s10719-015-9624-4. Epub 2015 Oct 9.

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

Author information

1
Human Health Therapeutics, National Research Council Canada, 100 Sussex Drive, Ottawa, ON, K1A 0R6, Canada.
2
Department of Chemistry and Biology, Ryerson University, 350 Victoria St., Toronto, ON, M5B 2K3, Canada.
3
Human Health Therapeutics, National Research Council Canada, 6100 Royalmount Avenue, Montreal, QC, H4P 2R2, Canada.
4
Department of Pharmacology, Johns Hopkins School of Medicine, 725 N. Wolfe Street, Baltimore, MD, 21205, USA.
5
Human Health Therapeutics, National Research Council Canada, 100 Sussex Drive, Ottawa, ON, K1A 0R6, Canada. michel.gilbert@nrc-cnrc.gc.ca.

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.

KEYWORDS:

GD1a; Human ST6Gal1 sialyltransferase; Interferon-α2b; Porcine ST3Gal1 sialyltransferase; α1-antitrypsin

PMID:
26452603
DOI:
10.1007/s10719-015-9624-4
[Indexed for MEDLINE]

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