Functional characterization of a 3-O-sulfate tolerant heparin lyase from Bacteroides eggerthii

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ID: 332211
2026
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Abstract
Abstract Heparin is a sulfated glycosaminoglycan, and the most used pharmaceutical anticoagulant worldwide. Heparin is isolated primarily from porcine sources, and possesses a complex variable structure, wherein anticoagulant activity is principally derived from the pentasaccharide GlcNS6S-GlcA-GlcNS3S6S-IdoA2S-GlcNS6S (AGA*IA) motif, containing an infrequent 3-O-sulfated glucosamine that enhances antithrombin stabilization. Pedobacter heparinus heparin lyases are currently widely employed for characterization of heparin and its derivatives, but have limited activity near regions of 3-O-sulfation, hindering analyses of anticoagulation relevant sequences. Here, using a panel of biophysical and structural techniques, we show that Bacteroides eggerthii lyase I liberates ΔUA-GlcNS3S6S disaccharides from the defined pentasaccharide, fondaparinux. This activity provides improved access to 3-O-sulfated heparin standards, with potential to aid heparin quality control.
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Authors Taran Kaur Kandola, Courtney J. Mycroft‐West, Marcelo A. Lima, Abigail Turner, Cristina Gardini, Elena Urso, Thomas A. Torode, Gavin J Miller, Antonella Bisio, Edwin Alexander Yates, Marco Guerrini, Mark Andrew Skidmore, Liang Wu
Journal glycobiology
Year 2026
DOI
10.1093/glycob/cwag097
URL
https://doi.org/10.1093/glycob/cwag097
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