Applications of a highly α2, 6-selective pseudosialidase. (28th February 2018)

• Record Type: Journal Article
• Authors: Both, Peter; Riese, Michel; Gray, Christopher J; Huang, Kun; Pallister, Edward G; Kosov, Iaroslav; Conway, Louis P; Voglmeir, Josef; Flitsch, Sabine L
• Is Part Of: Glycobiology. Volume 28:Number 5(2018)
• Page Start: 261
• Page End: 268
• Publication Date: 2018-02-28
• Subjects: HILIC -- ion mobility -- mass spectrometry -- sialidase -- sialyltransferase; Glycoproteins -- Periodicals; Glycolipids -- Periodicals; Glycoconjugates -- Periodicals; 572.567
• DOI: 10.1093/glycob/cwy016
• Languages: English
• ISSNs: 0959-6658

Abstract

Abstract: Within human biology, combinations of regioisomeric motifs of α2, 6- or α2, 3-sialic acids linked to galactose are frequently observed attached to glycoconjugates. These include glycoproteins and glycolipids, with each linkage carrying distinct biological information and function. Microbial linkage-specific sialidases have become important tools for studying the role of these sialosides in complex biological settings, as well as being used as biocatalysts for glycoengineering. However, currently, there is no α2, 6-specific sialidase available. This gap has been addressed herein by exploiting the ability of a Photobacterium sp. α2, 6-sialyltransferase to catalyze trans-sialidation reversibly and in a highly linkage-specific manner, acting as a pseudosialidase in the presence of cytidine monophosphate. Selective, near quantitative removal of α2, 6-linked sialic acids was achieved from a wide range of sialosides including small molecules conjugates, simple glycan, glycopeptide and finally complex glycoprotein including both linkages.