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<p><i>Akkermansia muciniphila</i> is a human microbial symbiont residing in the mucosal layer of the large intestine. Its main carbon source is the highly heterogeneous mucin glycoprotein, and it uses an array of carbohydrate-active enzymes and sulfatases to access this complex energy source. Here we describe the biochemical characterization of 54 glycoside hydrolases, 11 sulfatases and 1 polysaccharide lyase from <i>A. muciniphila</i> to provide a holistic understanding of their carbohydrate-degrading activities. This was achieved using a variety of liquid chromatography techniques, mass spectrometry, enzyme kinetics and thin-layer chromatography. These results are supported with <i>A. muciniphila</i> growth and whole-cell assays. We find that these enzymes can act synergistically to degrade the <i>O</i>-glycans on the mucin polypeptide to completion, down to the core <i>N</i>-acetylgalactosaime. In addition, these enzymes can break down human breast milk oligosaccharide, ganglioside and globoside glycan structures, showing their capacity to target a variety of host glycans. These data provide a resource to understand the full degradative capability of the gut microbiome member <i>A. muciniphila</i>.</p>

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Carbohydrate-active enzymes from Akkermansia muciniphila break down mucin O-glycans to completion

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年1月31日

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  • Cassie R. Bakshani,
  • Taiwo O. Ojuri,
  • Bo Pilgaard,
  • Jesper Holck,
  • Ross McInnes,
  • Radoslaw P. Kozak,
  • Maria Zakhour,
  • Sara Çakaj,
  • Manon Kerouedan,
  • Emily Newton,
  • David N. Bolam,
  • Lucy I. Crouch

摘要

Akkermansia muciniphila is a human microbial symbiont residing in the mucosal layer of the large intestine. Its main carbon source is the highly heterogeneous mucin glycoprotein, and it uses an array of carbohydrate-active enzymes and sulfatases to access this complex energy source. Here we describe the biochemical characterization of 54 glycoside hydrolases, 11 sulfatases and 1 polysaccharide lyase from A. muciniphila to provide a holistic understanding of their carbohydrate-degrading activities. This was achieved using a variety of liquid chromatography techniques, mass spectrometry, enzyme kinetics and thin-layer chromatography. These results are supported with A. muciniphila growth and whole-cell assays. We find that these enzymes can act synergistically to degrade the O-glycans on the mucin polypeptide to completion, down to the core N-acetylgalactosaime. In addition, these enzymes can break down human breast milk oligosaccharide, ganglioside and globoside glycan structures, showing their capacity to target a variety of host glycans. These data provide a resource to understand the full degradative capability of the gut microbiome member A. muciniphila.