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

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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Publication Details

Journal
Glycobiology
Published
2026-10-13
DOI
https://doi.org/10.1093/glycob/cwag097
Primary Topic
Proteoglycans and glycosaminoglycans research
Type
article
Field-Weighted Citation Impact
0.00

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article

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

Mark Andrew Skidmore, Antonella Bisio, Cristina Gardini, Thomas A. Torode et al.
Glycobiology
Proteoglycans and glycosaminoglycans research
article

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

Mark Andrew Skidmore, Antonella Bisio, Cristina Gardini, Thomas A. Torode, Elena Urso, Liang Wu, Courtney J. Mycroft‐West, Edwin Alexander Yates, Marco Guerrini, Taran Kaur Kandola, Marcelo A. Lima, Gavin J Miller, Abigail Turner
article en

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.

Glycobiology
Universiti Sains Malaysia (MY), University of Liverpool (GB), University of Manchester (GB), University of Oxford (GB), Rosalind Franklin Institute (GB), Istituto di Ricerche Chimiche e Biochimiche G. Ronzoni (IT), Keele University (GB), Manchester University (US)
Wellcome Trust, National Natural Science Foundation of China, Directorate for Biological Sciences, Medical Research Council, Engineering and Physical Sciences Research Council
Openalex Percentile: Top 17%
Proteoglycans and glycosaminoglycans research
DOIOpen Access PDFOpenAlex
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