Human Neuraminidases Have Reduced Activity Towards Modified Sialic Acids on Glycoproteins

Carmanah
D. Hunter; Elizabeth Porter; Christopher Cairo

doi:10.26434/chemrxiv.12510011.v1

Biological and Medicinal Chemistry

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Human Neuraminidases Have Reduced Activity Towards Modified Sialic Acids on Glycoproteins

22 June 2020, Version 1

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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

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