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Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation

Author

Listed:
  • Natalie C. Bamford

    (The Hospital for Sick Children
    University of Toronto
    University of Dundee)

  • François Le Mauff

    (McGill University
    Research Institute of McGill University Health Center
    McGill Interdisciplinary Initiative in Infection and Immunity)

  • Jaime C. Van Loon

    (The Hospital for Sick Children
    University of Toronto)

  • Hanna Ostapska

    (McGill University
    Research Institute of McGill University Health Center
    McGill Interdisciplinary Initiative in Infection and Immunity)

  • Brendan D. Snarr

    (McGill University
    Research Institute of McGill University Health Center
    McGill Interdisciplinary Initiative in Infection and Immunity)

  • Yongzhen Zhang

    (Leiden University)

  • Elena N. Kitova

    (University of Alberta)

  • John S. Klassen

    (University of Alberta)

  • Jeroen D. C. Codée

    (Leiden University)

  • Donald C. Sheppard

    (McGill University
    Research Institute of McGill University Health Center
    McGill Interdisciplinary Initiative in Infection and Immunity)

  • P. Lynne Howell

    (The Hospital for Sick Children
    University of Toronto)

Abstract

The exopolysaccharide galactosaminogalactan (GAG) is an important virulence factor of the fungal pathogen Aspergillus fumigatus. Deletion of a gene encoding a putative deacetylase, Agd3, leads to defects in GAG deacetylation, biofilm formation, and virulence. Here, we show that Agd3 deacetylates GAG in a metal-dependent manner, and is the founding member of carbohydrate esterase family CE18. The active site is formed by four catalytic motifs that are essential for activity. The structure of Agd3 includes an elongated substrate-binding cleft formed by a carbohydrate binding module (CBM) that is the founding member of CBM family 87. Agd3 homologues are encoded in previously unidentified putative bacterial exopolysaccharide biosynthetic operons and in other fungal genomes.

Suggested Citation

  • Natalie C. Bamford & François Le Mauff & Jaime C. Van Loon & Hanna Ostapska & Brendan D. Snarr & Yongzhen Zhang & Elena N. Kitova & John S. Klassen & Jeroen D. C. Codée & Donald C. Sheppard & P. Lynne, 2020. "Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16144-5
    DOI: 10.1038/s41467-020-16144-5
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    Cited by:

    1. Courtney J. Mycroft-West & Sahar Abdelkarim & Helen M. E. Duyvesteyn & Neha S. Gandhi & Mark A. Skidmore & Raymond J. Owens & Liang Wu, 2024. "Structural and mechanistic characterization of bifunctional heparan sulfate N-deacetylase-N-sulfotransferase 1," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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