Sialyltransferases with enhanced legionaminic acid transferase activity for the preparation of analogs of sialoglycoconjugates

From National Research Council Canada

Download	View accepted manuscript: Sialyltransferases with enhanced legionaminic acid transferase activity for the preparation of analogs of sialoglycoconjugates (PDF, 1 MB)
DOI	Resolve DOI: https://doi.org/10.1093/glycob/cwv017
Author	Search for: Watson, David C.¹; Search for: Wakarchuk, Warren W.; Search for: Leclerc, Sonia¹; Search for: Schur, Melissa J.¹; Search for: Schoenhofen, Ian C.¹; Search for: Young, N. Martin¹; Search for: Gilbert, Michel¹
Name affiliation	National Research Council Canada. Human Health Therapeutics
Format	Text
Type	Article
Journal title	Glycobiology
ISSN	0959-6658 1460-2423
Volume	25
Issue	7
Pages	767–773; # of pages: 7
Subject	Neisseria gonorrhoeae; Neisseria meningitidis; Pasteurella multocida; Photobacterium; legionaminic acid; sialyltransferase
Abstract	Legionaminic acids (Leg) are bacterial analogs of neuraminic acid, with the same stereochemistry but different substituents at C5, C7 and C9. Hence they may be incorporated into useful analogs of sialoglycoconjugates, and we previously reported two sialyltransferases that could utilize cytidine monophosphate (CMP)-Leg5Ac7Ac for preparation of Leg glycoconjugates, which were resistant to sialidases [Watson DC, Leclerc S, Wakarchuk WW, Young NM. 2011. Enzymatic synthesis and properties of glycoconjugates with legionaminic acid as a replacement for neuraminic acid. Glycobiology. 21:99–108.]. These were the porcine ST3Gal1 and Pasteurella multocida sialyltransferases. We now report two additional sialyltransferases with superior Leg-transferase properties to the previous two. These are (i) a truncated form of a Photobacterium α2,6-sialyltransferase with an Ala-Met mutation in its active site, and (ii) an α2,3-sialyltransferase from Neisseria meningitidis MC58 with a higher transferase activity than the P. multocida enzyme, with either CMP-Neu5Ac or CMP-Leg5Ac7Ac as the donor. These enzymes will enable the production of useful Leg5Ac7Ac glycoconjugate derivatives with either α2,6 or α2,3 linkages and unique biological properties.
Publication date	2015-04-03
Publisher	Oxford University Press
Language	English
Peer reviewed	Yes
NRC number	NRC-HHT-53278
NPARC number	21275311
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Record identifier	6327016d-eec7-4d80-a058-c7e557abde42
Record created	2015-06-05
Record modified	2020-02-06

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Date modified:: 2020-03-30