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

Author

Listed:
  • Gaёl M. Vos

    (Utrecht University)

  • Kevin C. Hooijschuur

    (Utrecht University)

  • Zeshi Li

    (Utrecht University)

  • John Fjeldsted

    (Agilent Technologies)

  • Christian Klein

    (Agilent Technologies)

  • Robert P. Vries

    (Utrecht University)

  • Javier Sastre Toraño

    (Utrecht University)

  • Geert-Jan Boons

    (Utrecht University
    Utrecht University
    University of Georgia)

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.

Suggested Citation

  • Gaёl M. Vos & Kevin C. Hooijschuur & Zeshi Li & John Fjeldsted & Christian Klein & Robert P. Vries & Javier Sastre Toraño & Geert-Jan Boons, 2023. "Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-42575-x
    DOI: 10.1038/s41467-023-42575-x
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    References listed on IDEAS

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    1. Anna-Maria T. Baumann & Mark J. G. Bakkers & Falk F. R. Buettner & Maike Hartmann & Melanie Grove & Martijn A. Langereis & Raoul J. de Groot & Martina Mühlenhoff, 2015. "9-O-Acetylation of sialic acids is catalysed by CASD1 via a covalent acetyl-enzyme intermediate," Nature Communications, Nature, vol. 6(1), pages 1-12, November.
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    Cited by:

    1. Shuling Xu & Zhijun Zhu & Daniel G. Delafield & Michael J. Rigby & Gaoyuan Lu & Megan Braun & Luigi Puglielli & Lingjun Li, 2024. "Spatially and temporally probing distinctive glycerophospholipid alterations in Alzheimer’s disease mouse brain via high-resolution ion mobility-enabled sn-position resolved lipidomics," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    2. Leïla Bechtella & Jin Chunsheng & Kerstin Fentker & Güney R. Ertürk & Marc Safferthal & Łukasz Polewski & Michael Götze & Simon Y. Graeber & Gaël M. Vos & Weston B. Struwe & Marcus A. Mall & Philipp M, 2024. "Ion mobility-tandem mass spectrometry of mucin-type O-glycans," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    3. Johannes Helm & Stefan Mereiter & Tiago Oliveira & Anna Gattinger & David M. Markovitz & Josef M. Penninger & Friedrich Altmann & Johannes Stadlmann, 2024. "Non-targeted N-glycome profiling reveals multiple layers of organ-specific diversity in mice," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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    1. Johannes Helm & Stefan Mereiter & Tiago Oliveira & Anna Gattinger & David M. Markovitz & Josef M. Penninger & Friedrich Altmann & Johannes Stadlmann, 2024. "Non-targeted N-glycome profiling reveals multiple layers of organ-specific diversity in mice," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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