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

Anna-Maria T. Baumann, Mark J. G. Bakkers, Falk F. R. Buettner, Maike Hartmann, Melanie Grove, Martijn A. Langereis, Raoul J. de Groot and Martina Mühlenhoff ()
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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

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms8673

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