ArticleMethods in enzymology2026
Sialylation and fucosylation of mucin-type glycopeptides using recombinant glycosyltransferases.
Article in Methods in enzymology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Mucins are glycoproteins that play fundamental roles in mucus, saliva, and tears, and coat cell surfaces in the glycocalyx. The saccharide component of mucins is essential for their many biophysical and biochemical functions. The composition of mucin glycans is naturally heterogeneous, and precise control over this composition for structure-function studies has been extremely challenging using traditional genetic and biochemical methods. Thus, synthetically generated materials with defined glycosylation are essential for probing mucin biology. Sialic acid and fucose are two sugars typically found in terminal positions on mucin glycans and are implicated in regulating diverse processes, from immunity to cancer. Here, we describe detailed enzymatic methods to install fucose and sialic acids on mucin-type glycopeptides or glycoproteins. Microbe-derived recombinant enzymes can be used to install these sugars with regio- and stereoselectivity that would be extremely challenging to achieve using chemical methods. The methods described here encompass cloning and recombinant expression of the relevant enzymes, conditions for enzymatic glycosylation reactions, and analytical techniques to characterize the sialylated or fucosylated glycopeptide products. Overall, these methods enable researchers to probe mucin biology using glycan-defined materials.
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