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

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. Ashutosh Rao and Tongzhong Ju ()
Additional contact information
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

Nature Communications, 2025, vol. 16, issue 1, 1-19

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-57143-8

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