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

Pedro Bule, Léa Chuzel, Elena Blagova, Liang Wu, Melissa A. Gray, Bernard Henrissat, Erdmann Rapp, Carolyn R. Bertozzi, Christopher H. Taron () and Gideon J. Davies ()
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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
Carolyn R. Bertozzi: Stanford University
Christopher H. Taron: New England Biolabs
Gideon J. Davies: University of York

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-12684-7

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