The sialate O-acetylesterase EstA from gut Bacteroidetes species enables sialidase-mediated cross-species foraging of 9-O-acetylated sialoglycans.

The Journal of Biological Chemistry
Lloyd S RobinsonAmanda L Lewis

Abstract

The gut harbors many symbiotic, commensal, and pathogenic microbes that break down and metabolize host carbohydrates. Sialic acids are prominent outermost carbohydrates on host glycoproteins called mucins and protect underlying glycan chains from enzymatic degradation. Sialidases produced by some members of the colonic microbiota can promote the expansion of several potential pathogens (e.g. Clostridium difficile, Salmonella, and Escherichia coli) that do not produce sialidases. O-Acetyl ester modifications of sialic acids help resist the action of many sialidases and are present at high levels in the mammalian colon. However, some gut bacteria, in turn, produce sialylate-O-acetylesterases to remove them. Here, we investigated O-acetyl ester removal and sialic acid degradation by Bacteroidetes sialate-O-acetylesterases and sialidases, respectively, and subsequent utilization of host sialic acids by both commensal and pathogenic E. coli strains. In vitro foraging studies demonstrated that sialidase-dependent E. coli growth on mucin is enabled by Bacteroides EstA, a sialate O-acetylesterase acting on glycosidically linked sialylate-O-acetylesterase substrates, particularly at neutral pH. Biochemical studies suggested that spontan...Continue Reading

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Citations

Aug 3, 2019·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Naama Geva-ZatorskySven Pettersson
Apr 10, 2019·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Qianyun FuGuangli Yu
Jul 22, 2018·Bioscience, Biotechnology, and Biochemistry·Hisashi AshidaKenji Yamamoto
Oct 13, 2020·Glycobiology·Andrew Bell, Nathalie Juge
Jun 23, 2021·The Journal of Biological Chemistry·Eline A VisserChristian Büll

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Methods Mentioned

BETA
-acetylation
biopsy
PCR
protein assay

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