Recognition of protein-linked glycans as a determinant of peptidase activity
Open accessAbstract
Significance: Protein glycosylation is one of the most abundant and important posttranslational modifications where the protein-linked glycans can impart specific physiochemical properties to the glycoprotein and/or the glycans themselves can mediate particular biological functions. The degradation of glycosylated proteins in normal or pathogenic processes, therefore, is an important biological process. This study reveals the molecular basis of how peptidases can use the O-glycans present on glycoproteins as a critical determinant of peptidase activity and, in doing so, provides unique insight into how peptidases may directly use posttranslational modifications present on their substrates to influence recognition and peptide bond cleavage.
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Different mucin-degrading proteases have been described in Bacteroides, a common commensal of the human intestine.
“Different mucin-degrading proteases have been also described in Bacteroides, a common commensal of the human intestine.”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [126]
Mucin-degrading proteases in Bacteroides include proteases in B. thetaiotaomicron (BT4244) or Bacteroides caccae.
“These include proteases in B. thetaiotaomicron (BT4244) or Bacteroides caccae.126,127”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [126]
The M60-like protease family cleaves the mucin glycoprotein backbone in a manner dependent on the presence of specific glycan sidechain structures.
“the M60-like protease family cleaves the mucin glycoprotein backbone in a manner that is dependent on the presence of specific glycan sidechain structures.125,126”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [126]
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- Authors
- Noach, I., Ficko-Blean, E., Pluvinage, B., Stuart, C., Jenkins, M. L., Brochu, D., Buenbrazo, N., Wakarchuk, W., Burke, J. E., Gilbert, M., & Boraston, A. B.
- Affiliations
- University of Victoria (CA)
- Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada;
- National Research Council Canada (CA)
- Toronto Metropolitan University (CA)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2017-01-17
- Volume
- 114
- Issue
- 5
- Pages
- E679-E688
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC5293097
- OpenAlex
- W2579867384
- Cited by
- 89
- References
- 50
- Citations by year
- 2026: 10 · 2025: 9 · 2024: 10 · 2023: 10 · 2022: 18 · 2021: 6 · 2020: 14 · 2019: 9 · 2018: 3
- FWCI
- 2.90
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- NPARC (submittedVersion)
- Funders
- Gouvernement du Canada | Canadian Institutes of Health Research (MOP 130305)
- Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada (NSERC‐2014‐05218)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- O-glycosylation, metalloproteinases, post-translational modification, glycoprotein degradation, peptide bond cleavage
- MeSH terms
- Escherichia coli, Glycopeptides, Glycosylation, Mucins, Peptide Hydrolases, Polysaccharides, Protein Conformation, Protein Processing, Post-Translational, Fetuins
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