Human Neuraminidases Have Reduced Activity Towards Modified Sialic Acids on Glycoproteins

21 August 2020, Version 2
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

This work investigated the substrate specificity of hNEU enzymes for a glycoprotein substrate (bovine submaxillary mucin) containing 9-O-acetylated and Neu5Gc residues. Using this model substrate, we observe a general trend for hNEU tolerance of Neu5Ac>Neu5Gc>>>Neu5,9Ac2, consistent with our previous results with glycolipid substrates. These results expand our understanding of hNEU enzyme specificity and suggest that naturally occurring modifications of sialic acids can play a role in regulating hNEU activity.

Keywords

neuraminidase
sialidase
acetylated sialic acid
neuraminic acid

Supplementary materials

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hunter.si
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