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9-O-Acetylation of sialic acids is catalysed by CASD1 via a covalent acetyl-enzyme intermediate

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  • Anna-Maria T. Baumann

    (Institute of Cellular Chemistry, Hannover Medical School)

  • Mark J. G. Bakkers

    (Faculty of Veterinary Medicine, Utrecht University)

  • Falk F. R. Buettner

    (Institute of Cellular Chemistry, Hannover Medical School)

  • Maike Hartmann

    (Institute of Cellular Chemistry, Hannover Medical School)

  • Melanie Grove

    (Institute of Cellular Chemistry, Hannover Medical School)

  • Martijn A. Langereis

    (Faculty of Veterinary Medicine, Utrecht University)

  • Raoul J. de Groot

    (Faculty of Veterinary Medicine, Utrecht University)

  • Martina Mühlenhoff

    (Institute of Cellular Chemistry, Hannover Medical School)

Abstract

Sialic acids, terminal sugars of glycoproteins and glycolipids, play important roles in development, cellular recognition processes and host–pathogen interactions. A common modification of sialic acids is 9-O-acetylation, which has been implicated in sialoglycan recognition, ganglioside biology, and the survival and drug resistance of acute lymphoblastic leukaemia cells. Despite many functional implications, the molecular basis of 9-O-acetylation has remained elusive thus far. Following cellular approaches, including selective gene knockout by CRISPR/Cas genome editing, we here show that CASD1—a previously identified human candidate gene—is essential for sialic acid 9-O-acetylation. In vitro assays with the purified N-terminal luminal domain of CASD1 demonstrate transfer of acetyl groups from acetyl-coenzyme A to CMP-activated sialic acid and formation of a covalent acetyl-enzyme intermediate. Our study provides direct evidence that CASD1 is a sialate O-acetyltransferase and serves as key enzyme in the biosynthesis of 9-O-acetylated sialoglycans.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8673
    DOI: 10.1038/ncomms8673
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    Cited by:

    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.
    2. 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.

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