A New Enzyme for Remove Sialic Acids on Glycoproteins

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  • Published date: October 22, 2022
    • United States
A New Enzyme for Remove Sialic Acids on Glycoproteins
A New Enzyme for Remove Sialic Acids on Glycoproteins

Glycosylation plays a crucial role in protein folding, trafficking, stability, and cellular activities such as receptor binding, cell signaling, immune recognition, inflammation, and pathogenesis. N-glycosylation and O-glycosylation are the two primary forms of glycosylation modification. N-linked glycans are linked to the amide side chains of asparagine (Asn) residues on the protein with a core; in contrast, O-linked glycans have a disaccharide core of Core 1 or Core 3 attached to the hydroxyl side chains of Ser or Thr residues.

The terminal residues on these N- or O-glycan chains are usually sialic acids. An essential first step in glycosylation studies of glycoproteins is usually the removal of all non-reducing terminal sialic terminal acid residues. The sialic acid at the end has a severe impact on the function of the antibody. The higher the content of sialic acid, the lower the affinity of IgG and Fc receptors. The reason may be that the large space occupied by sialic acid reduces the elasticity of the hinge region of the antibody, thereby reducing the receptor binding ability. The level of sialylation may affect the metabolism of protein drugs, so desialylation is very important.
https://www.profacgen.com/platform/drug-discovery/biosimilar-testing-services/a-new-enzyme-for-remove-sialic-acids-on-glycoproteins

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