ArticleJournal of biomolecular NMR2016
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
Article in Journal of biomolecular NMR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Backbone NMR resonance assignments for the C2 domain of the Streptococcus mutans adhesin P1.Biomolecular NMR assignments · 2025Article
- Backbone NMR resonance assignments for the C terminal domain of the Streptococcus mutans adhesin P1.Biomolecular NMR assignments · 2023Article
- Drug sensitivity and genome-wide analysis of two strains ofFrontiers in microbiology · 2023Article
- Article
- Amyloid Aggregates Are Localized to the Nonadherent Detached Fraction of Aging Streptococcus mutans Biofilms.Microbiology spectrum · 2022Article
- Solid-State NMR Investigations of Extracellular Matrixes and Cell Walls of Algae, Bacteria, Fungi, and Plants.Chemical reviews · 2022Review
- Novel antimicrobial agents targeting theFrontiers in cellular and infection microbiology · 2022Review
- Anti-Biofilm Molecules Targeting Functional Amyloids.Antibiotics (Basel, Switzerland) · 2021Review
- Characterization of an intermolecular quaternary interaction between discrete segments of the Streptococcus mutans adhesin P1 by NMR spectroscopy.The FEBS journal · 2020Article
- Enhanced purification coupled with biophysical analyses shows cross-β structure as a core building block for Streptococcus mutans functional amyloids.Scientific reports · 2020Article
- The Multifaceted Nature of Streptococcal Antigen I/II Proteins in Colonization and Disease Pathogenesis.Frontiers in microbiology · 2020Review
- The Role of Exopolysaccharides in Oral Biofilms.Journal of dental research · 2019Review
- Microbial functional amyloids serve diverse purposes for structure, adhesion and defence.Biophysical reviews · 2019Review
- Article
- The Role of Functional Amyloids in Bacterial Virulence.Journal of molecular biology · 2018Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The P1 adhesin (aka Antigen I/II or PAc) of the cariogenic bacterium Streptococcus mutans is a cell surface-localized protein involved in sucrose-independent adhesion and colonization of the tooth surface. The immunoreactive and adhesive properties of S. mutans suggest an unusual functional quaternary ultrastructure comprised of intact P1 covalently attached to the cell wall and interacting with non-covalently associated proteolytic fragments thereof, particularly the ~57-kDa C-terminal fragment C123 previously identified as Antigen II. S. mutans is capable of amyloid formation when grown in a biofilm and P1 is among its amyloidogenic proteins. The C123 fragment of P1 readily forms amyloid fibers in vitro suggesting it may play a role in the formation of functional amyloid during biofilm development. Using wild-type and P1-deficient strains of S. mutans, we demonstrate that solid state NMR (ssNMR) spectroscopy can be used to (1) globally characterize cell walls isolated from a Gram-positive bacterium and (2) characterize the specific binding of heterologously expressed, isotopically-enriched C123 to cell wall-anchored P1. Our results lay the groundwork for future high-resolution characterization of the C123/P1 ultrastructure and subsequent steps in biofilm formation via ssNMR spectroscopy, and they support an emerging model of S. mutans colonization whereby quaternary P1-C123 interactions confer adhesive properties important to binding to immobilized human salivary agglutinin.
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