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Dual functional POGases from bacteria encompassing broader O-glycanase and adhesin activities

Author

Listed:
  • Linjiao Zhou

    (Food and Drug Administration)

  • Uriel Ortega-Rodriguez

    (Food and Drug Administration)

  • Matthew J. Flores

    (Food and Drug Administration)

  • Yasuyuki Matsumoto

    (Food and Drug Administration)

  • John Q. Bettinger

    (Food and Drug Administration)

  • Wells W. Wu

    (Food and Drug Administration)

  • Yaqin Zhang

    (Food and Drug Administration)

  • Su-Ryun Kim

    (Food and Drug Administration)

  • Thomas G. Biel

    (Food and Drug Administration)

  • Jordan D. Pritts

    (Food and Drug Administration)

  • Rong-Fong Shen

    (Food and Drug Administration)

  • V. Ashutosh Rao

    (Food and Drug Administration)

  • Tongzhong Ju

    (Food and Drug Administration)

Abstract

Mucin-type O-glycans on glycoproteins are pivotal for biology and impact the quality of biotherapeutics. Furthermore, glycans on host cells serve as ligands for lectins/adhesins on bacteria for bacterium-host interactions in the colonization or attachment/invasion of bacteria. Defining the structure-function relationship of O-glycans is hindered by a lack of enzyme(s) to release sialylated O-glycans from glycoproteins. Here we show identification of endo-α-N-acetylgalactosaminidases (O-glycanases, GH101) with broad substrate specificities, termed Peptide:O-Glycosidase (POGase). In 5 POGase orthologs identified, we characterize one that releases sialylated O-glycans from glycopeptides, glycoproteins and biotherapeutics. Three peptide motifs differentiate the POGase existing in phylum Actinomycetota from known O-glycanases in other bacteria. While the GH101 domain classifies POGases, other domains confer the efficient enzyme activity and binding to major glycans decorating epithelial cells. The dual functional POGases encompassing broader O-glycanase and adhesin activities will facilitate the study of O-glycomics, quality assessment of biotherapeutics, and development of microbiology and medicine.

Suggested Citation

  • Linjiao Zhou & Uriel Ortega-Rodriguez & Matthew J. Flores & Yasuyuki Matsumoto & John Q. Bettinger & Wells W. Wu & Yaqin Zhang & Su-Ryun Kim & Thomas G. Biel & Jordan D. Pritts & Rong-Fong Shen & V. A, 2025. "Dual functional POGases from bacteria encompassing broader O-glycanase and adhesin activities," Nature Communications, Nature, vol. 16(1), pages 1-19, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-57143-8
    DOI: 10.1038/s41467-025-57143-8
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    References listed on IDEAS

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    1. Anna G. Green & Hadeer Elhabashy & Kelly P. Brock & Rohan Maddamsetti & Oliver Kohlbacher & Debora S. Marks, 2021. "Large-scale discovery of protein interactions at residue resolution using co-evolution calculated from genomic sequences," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
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