ArticleScientific reports2018
Characterization of the pgf operon involved in the posttranslational modification of Streptococcus mutans surface proteins.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Genomic instability and biofilm determinants inJournal of bacteriology · 2026Article
- Genomic instability and biofilm determinants inbioRxiv : the preprint server for biology · 2026Article
- Article
- Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci.Nature communications · 2025Article
- Glycosylation of oral bacteria in modulating adhesion and biofilm formation.Journal of oral microbiology · 2025Review
- Post-translational modification by the Pgf glycosylation machinery modulates Streptococcus mutans OMZ175 physiology and virulence.Molecular microbiology · 2024Article
- Involvement of the Streptococcus mutans PgfE and GalE 4-epimerases in protein glycosylation, carbon metabolism, and cell division.Glycobiology · 2023Article
- Amyloid Aggregates Are Localized to the Nonadherent Detached Fraction of Aging Streptococcus mutans Biofilms.Microbiology spectrum · 2022Article
- Glycan-mediated molecular interactions in bacterial pathogenesis.Trends in microbiology · 2022Review
- Amyloid Aggregation of Streptococcus mutans Cnm Influences Its Collagen-Binding Activity.Applied and environmental microbiology · 2021Article
- Post-translational Modifications in Oral Bacteria and Their Functional Impact.Frontiers in microbiology · 2021Review
- Quantitative Proteomics Uncovers the Interaction between a Virulence Factor and Mutanobactin Synthetases inmSphere · 2019Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Protein glycosylation has been described as the most abundant and complex post-translational modification occurring in nature. Recent studies have enhanced our view of how this modification occurs in bacteria highlighting the role of protein glycosylation in various processes such as biofilm formation, virulence and host-microbe interactions. We recently showed that the collagen- and laminin-binding adhesin Cnm of the dental pathogen Streptococcus mutans is post-translationally modified by the PgfS glycosyltransferase. Following this initial identification of Cnm as a glycoprotein, we have now identified additional genes (pgfM1, pgfE and pgfM2) that are also involved in the posttranslational modification of Cnm. Similar to the previously characterized ΔpgfS strain, inactivation of pgfM1, pgfE or pgfM2 directly impacts Cnm by altering its migration pattern, proteolytic stability and function. In addition, we identified the wall-associated protein A (WapA) as an additional substrate of Pgf-dependent modification. We conclude that the pgS-pgfM1-pgfE-pgfM2 operon encodes for a protein machinery that can modify, likely through the addition of glycans, both core and non-core gene products in S. mutans.
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