Functional conservation of divergent peptidase_M60 O-glycopeptidases in Enterococcus

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ID: 327838
2026
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Abstract
O-glycopeptidases are proteolytic enzymes that obligately recognize the O-glycans appended to their substrates. Peptidase_M60 proteins comprise a superfamily of putative metal-dependent O-glycopeptidases that were initially described in host-associated bacteria but are now known to be distributed across bacteria occupying both host-associated and environmental niches. Although several members of this superfamily have been shown to possess O-glycopeptidase activity, the family is highly divergent at the amino acid sequence level, making it unclear whether this activity is conserved across all members. Here, we show that two peptidase_M60 enzymes, EfmM60 and EfcM60, from strains of Enterococcus faecium and Enterococcus faecalis, respectively, which are only distantly related at the primary sequence level to previously characterized O-glycopeptidases, exhibit both mucinase and O-glycopeptidase activity. Structural analysis of EfmM60 reveals distinct active-site features relative to previously characterized peptidase_M60 enzymes that provide a molecular basis for its ability to accommodate extended and branched O-glycans. Together, these findings highlight functional conservation within a highly divergent peptidase_M60 family and suggest that enterococcal O-glycopeptidases may contribute to ecological versatility by enabling access to O-glycosylated substrates across diverse biological contexts.
Reference Key
openalex_W7211916520 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Liam Mihalynuk, B. Pluvinage, Olivia Canil, Nicole Thompson, Warren W. Wakarchuk, A.B. Boraston
Journal glycobiology
Year 2026
DOI
10.1093/glycob/cwag076
URL
https://doi.org/10.1093/glycob/cwag076
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