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Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action

Author

Listed:
  • Pedro Bule

    (University of York)

  • Léa Chuzel

    (New England Biolabs)

  • Elena Blagova

    (University of York)

  • Liang Wu

    (University of York)

  • Melissa A. Gray

    (Stanford University)

  • Bernard Henrissat

    (Institut National Agronomique (INRA, USC 1408) and Aix-Marseille Université (AMU))

  • Erdmann Rapp

    (Max Planck Institute for Dynamics of Complex Technical Systems
    glyXera GmbH)

  • Carolyn R. Bertozzi

    (Stanford University
    Stanford University)

  • Christopher H. Taron

    (New England Biolabs)

  • Gideon J. Davies

    (University of York)

Abstract

Sialic acids are a family of related sugars that play essential roles in many biological events intimately linked to cellular recognition in both health and disease. Sialidases are therefore orchestrators of cellular biology and important therapeutic targets for viral infection. Here, we sought to define if uncharacterized sialidases would provide distinct paradigms in sialic acid biochemistry. We show that a recently discovered sialidase family, whose first member EnvSia156 was isolated from hot spring metagenomes, defines an unusual structural fold and active centre constellation, not previously described in sialidases. Consistent with an inverting mechanism, EnvSia156 reveals a His/Asp active center in which the His acts as a Brønsted acid and Asp as a Brønsted base in a single-displacement mechanism. A predominantly hydrophobic aglycone site facilitates accommodation of a variety of 2-linked sialosides; a versatility that offers the potential for glycan hydrolysis across a range of biological and technological platforms.

Suggested Citation

  • Pedro Bule & Léa Chuzel & Elena Blagova & Liang Wu & Melissa A. Gray & Bernard Henrissat & Erdmann Rapp & Carolyn R. Bertozzi & Christopher H. Taron & Gideon J. Davies, 2019. "Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12684-7
    DOI: 10.1038/s41467-019-12684-7
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    Cited by:

    1. Bashar Shuoker & Michael J. Pichler & Chunsheng Jin & Hiroka Sakanaka & Haiyang Wu & Ana Martínez Gascueña & Jining Liu & Tine Sofie Nielsen & Jan Holgersson & Eva Nordberg Karlsson & Nathalie Juge & , 2023. "Sialidases and fucosidases of Akkermansia muciniphila are crucial for growth on mucin and nutrient sharing with mucus-associated gut bacteria," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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