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

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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Cite

BibTeX RIS

BibTeX

@article{kandola2026functional,
  title = {{Functional characterization of a 3-O-sulfate tolerant heparin lyase from Bacteroides eggerthii}},
  author = {Taran K Kandola and Courtney J Mycroft-West and Marcelo A Lima and Abigail Turner and Cristina Gardini and Elena Urso and Thomas A Torode and Gavin J Miller and Antonella Bisio and Edwin A Yates and Marco Guerrini and Mark A Skidmore and Liang Wu},
  journal = {Glycobiology},
  year = {2026},
  month = oct,
  doi = {10.1093/glycob/cwag097},
  url = {https://doi.org/10.1093/glycob/cwag097},
  note = {CC BY 4.0},
}

RIS

TY  - JOUR
TI  - Functional characterization of a 3-O-sulfate tolerant heparin lyase from Bacteroides eggerthii
AU  - Taran K Kandola
AU  - Courtney J Mycroft-West
AU  - Marcelo A Lima
AU  - Abigail Turner
AU  - Cristina Gardini
AU  - Elena Urso
AU  - Thomas A Torode
AU  - Gavin J Miller
AU  - Antonella Bisio
AU  - Edwin A Yates
AU  - Marco Guerrini
AU  - Mark A Skidmore
AU  - Liang Wu
PY  - 2026
DA  - 2026/10/13
JO  - Glycobiology
DO  - 10.1093/glycob/cwag097
UR  - https://doi.org/10.1093/glycob/cwag097
AB  - 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.
SN  - 0959-6658
SN  - 1460-2423
ER  -

Abstract

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