Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry

Gaёl M Vos; Kevin C Hooijschuur; Zeshi Li; John Fjeldsted; Christian Klein; Robert P de Vries; Javier Sastre Toraño; Geert-Jan Boons

doi:10.1038/s41467-023-42575-x

Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry

Gaёl M Vos, Kevin C Hooijschuur, Zeshi Li, John Fjeldsted, Christian Klein, Robert P de Vries, Javier Sastre Toraño, Geert-Jan Boons

Agilent Technologies

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

O-acetylation is a common modification of sialic acids that has been implicated in a multitude of biological and disease processes. A lack of analytical methods that can determine exact structures of sialic acid variants is a hurdle to determine roles of distinct O-acetylated sialosides. Here, we describe a drift tube ion mobility-mass spectrometry approach that can elucidate exact O-acetylation patterns as well as glycosidic linkage types of sialosides isolated from complex biological samples. It is based on the use of a library of synthetic O-acetylated sialosides to establish intrinsic collision cross section (CCS) values of diagnostic fragment ions. The CCS values were used to characterize O-acetylated sialosides from mucins and N-linked glycans from biologicals as well as equine tracheal and nasal tissues. It uncovered contrasting sialic acid linkage types of acetylated and non-acetylated sialic acids and provided a rationale for sialic acid binding preferences of equine H7 influenza A viruses.

Original language	English
Article number	6795
Pages (from-to)	1-13
Number of pages	13
Journal	Nature Communications
Volume	14
Issue number	1
Early online date	25 Oct 2023
DOIs	https://doi.org/10.1038/s41467-023-42575-x
Publication status	Published - Dec 2023

Bibliographical note

Publisher Copyright:
© 2023, Springer Nature Limited.

Funding

We thank E. Mastrobattista and E.M. Redout for providing Aflibercept and Myozyme. This research was supported by an Agilent Technologies Applications and Core Technology University Research grant (ACT-UR-4725 to J.S.T.), the European Commission (grants 101020769 and 802780 to G.J.B. and R.P.V., respectively), Health~Holland (TKI-LSHM21030 to G.J.B.), and the Mizutani Foundation for Glycoscience (to R.P.V.).

Funders	Funder number
Agilent Technologies Applications
Core Technology University	ACT-UR-4725
Mizutani Foundation for Glycoscience
European Commission	101020769, 802780, TKI-LSHM21030

Keywords

Animals
Horses
N-Acetylneuraminic Acid/metabolism
Glycosides
Acetylation
Sialic Acids/metabolism
Cardiac Glycosides
Mass Spectrometry

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abstract = "O-acetylation is a common modification of sialic acids that has been implicated in a multitude of biological and disease processes. A lack of analytical methods that can determine exact structures of sialic acid variants is a hurdle to determine roles of distinct O-acetylated sialosides. Here, we describe a drift tube ion mobility-mass spectrometry approach that can elucidate exact O-acetylation patterns as well as glycosidic linkage types of sialosides isolated from complex biological samples. It is based on the use of a library of synthetic O-acetylated sialosides to establish intrinsic collision cross section (CCS) values of diagnostic fragment ions. The CCS values were used to characterize O-acetylated sialosides from mucins and N-linked glycans from biologicals as well as equine tracheal and nasal tissues. It uncovered contrasting sialic acid linkage types of acetylated and non-acetylated sialic acids and provided a rationale for sialic acid binding preferences of equine H7 influenza A viruses.",

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Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry

Abstract

Bibliographical note

Funding

Keywords

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