ArticleACS nano2015
Binding forces of Streptococcus mutans P1 adhesin.
Article in ACS nano, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 73 citations in OpenAlex.
- Investigation of Bacterial Curli Production and Adhesion Using AFM.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Advances in scanning probe microscopy for biological systems.Biophysics reports · 2026Article
- Recent advances in membrane vesicles ofJournal of oral microbiology · 2026Review
- Standardization of extraction, identification, and characterization of an immunoglobulin Y antibody: A potential inhibitor of cariogenic and endodontic microbiome.Journal of conservative dentistry and endodontics · 2025Article
- Single-Cell Force Spectroscopy Uncovers Root Zone- and Bacteria-Specific Interactions.Angewandte Chemie (International ed. in English) · 2025Article
- Review
- Structure and composition of early biofilms formed on dental implants are complex, diverse, subject-specific and dynamic.NPJ biofilms and microbiomes · 2024Article
- Trans, Trans-Farnesol Enhances the Anti-Bacterial and Anti-Biofilm Effect of Arachidonic Acid on the Cariogenic BacteriaInternational journal of molecular sciences · 2024Article
- Influence of Polymerization Protocol on Adhesion and Proliferation ofBiomedicines · 2024Article
- The role of filamentous matrix molecules in shaping the architecture and emergent properties of bacterial biofilms.The Biochemical journal · 2024Review
- Multiple biological characteristics and functions of intestinal biofilm extracellular polymers: friend or foe?Frontiers in microbiology · 2024Review
- Using Knock-Out Mutants to Investigate the Adhesion ofInternational journal of molecular sciences · 2021Article
- Amyloid Aggregation of Streptococcus mutans Cnm Influences Its Collagen-Binding Activity.Applied and environmental microbiology · 2021Article
- Bacterial extracellular matrix as a natural source of biotechnologically multivalent materials.Computational and structural biotechnology journal · 2021Review
- Bioadhesion in the oral cavity and approaches for biofilm management by surface modifications.Clinical oral investigations · 2020Review
- Using Atomic Force Microscopy To Illuminate the Biophysical Properties of Microbes.ACS applied bio materials · 2020Article
- The Multifaceted Nature of Streptococcal Antigen I/II Proteins in Colonization and Disease Pathogenesis.Frontiers in microbiology · 2020Review
- Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins.Frontiers in microbiology · 2020Review
- Binding Strength of Gram-Positive Bacterial Adhesins.Frontiers in microbiology · 2020Review
- Microbial adhesion and ultrastructure from the single-molecule to the single-cell levels by Atomic Force Microscopy.Cell surface (Amsterdam, Netherlands) · 2019Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
Streptococcus mutans is a Gram-positive oral bacterium that is a primary etiological agent associated with human dental caries. In the oral cavity, S. mutans adheres to immobilized salivary agglutinin (SAG) contained within the salivary pellicle on the tooth surface. Binding to SAG is mediated by cell surface P1, a multifunctional adhesin that is also capable of interacting with extracellular matrix proteins. This may be of particular importance outside of the oral cavity as S. mutans has been associated with infective endocarditis and detected in atherosclerotic plaque. Despite the biomedical importance of P1, its binding mechanisms are not completely understood. In this work, we use atomic force microscopy-based single-molecule and single-cell force spectroscopy to quantify the nanoscale forces driving P1-mediated adhesion. Single-molecule experiments show that full-length P1, as well as fragments containing only the P1 globular head or C-terminal region, binds to SAG with relatively weak forces (∼50 pN). In contrast, single-cell analyses reveal that adhesion of a single S. mutans cell to SAG is mediated by strong (∼500 pN) and long-range (up to 6000 nm) forces. This is likely due to the binding of multiple P1 adhesins to self-associated gp340 glycoproteins. Such a cooperative, long-range character of the S. mutans-SAG interaction would therefore dramatically increase the strength and duration of cell adhesion. We also demonstrate, at single-molecule and single-cell levels, the interaction of P1 with fibronectin and collagen, as well as with hydrophobic, but not hydrophilic, substrates. The binding mechanism (strong forces, cooperativity, broad specificity) of P1 provides a molecular basis for its multifunctional adhesion properties. Our methodology represents a valuable approach to probe the binding forces of bacterial adhesins and offers a tractable methodology to assess anti-adhesion therapy.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.