ArticleThe Journal of biological chemistry2015
Identification of a supramolecular functional architecture of Streptococcus mutans adhesin P1 on the bacterial cell surface.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 46 citations in OpenAlex.
- Backbone NMR resonance assignments for the C2 domain of the Streptococcus mutans adhesin P1.Biomolecular NMR assignments · 2025Article
- Trans, Trans-Farnesol Enhances the Anti-Bacterial and Anti-Biofilm Effect of Arachidonic Acid on the Cariogenic BacteriaInternational journal of molecular sciences · 2024Article
- Backbone NMR resonance assignments for the C terminal domain of the Streptococcus mutans adhesin P1.Biomolecular NMR assignments · 2023Article
- Article
- Amyloid Aggregates Are Localized to the Nonadherent Detached Fraction of Aging Streptococcus mutans Biofilms.Microbiology spectrum · 2022Article
- [Research Updates: Cariogenic Mechanism ofSichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2022Review
- Small molecule targeting amyloid fibrils inhibits Streptococcus mutans biofilm formation.AMB Express · 2021Article
- Anti-Biofilm Molecules Targeting Functional Amyloids.Antibiotics (Basel, Switzerland) · 2021Review
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- Multifunctional Amyloids in the Biology of Gram-Positive Bacteria.Microorganisms · 2020Review
- 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
- Using Atomic Force Microscopy To Illuminate the Biophysical Properties of Microbes.ACS applied bio materials · 2020Article
- Microbial Interactions in Oral Communities Mediate Emergent Biofilm Properties.Journal of dental research · 2020Article
- The Multifaceted Nature of Streptococcal Antigen I/II Proteins in Colonization and Disease Pathogenesis.Frontiers in microbiology · 2020Review
- Diversity of SpaP in genetic and salivary agglutinin mediated adherence among Streptococcus mutans strains.Scientific reports · 2019Article
- Effect of flavonoids on antimicrobial activity of microorganisms present in dental plaque.Heliyon · 2019Article
- Microbial functional amyloids serve diverse purposes for structure, adhesion and defence.Biophysical reviews · 2019Review
- The Role of Functional Amyloids in Bacterial Virulence.Journal of molecular biology · 2018Review
- Glucan Binding Protein C of Streptococcus mutans Mediates both Sucrose-Independent and Sucrose-Dependent Adherence.Infection and immunity · 2018Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
P1 (antigen I/II) is a sucrose-independent adhesin of Streptococcus mutans whose functional architecture on the cell surface is not fully understood. S. mutans cells subjected to mechanical extraction were significantly diminished in adherence to immobilized salivary agglutinin but remained immunoreactive and were readily aggregated by fluid-phase salivary agglutinin. Bacterial adherence was restored by incubation of postextracted cells with P1 fragments that contain each of the two known adhesive domains. In contrast to untreated cells, glutaraldehyde-treated bacteria gained reactivity with anti-C-terminal monoclonal antibodies (mAbs), whereas epitopes recognized by mAbs against other portions of the molecule were masked. Surface plasmon resonance experiments demonstrated the ability of apical and C-terminal fragments of P1 to interact. Binding of several different anti-P1 mAbs to unfixed cells triggered release of a C-terminal fragment from the bacterial surface, suggesting a novel mechanism of action of certain adherence-inhibiting antibodies. We also used atomic force microscopy-based single molecule force spectroscopy with tips bearing various mAbs to elucidate the spatial organization and orientation of P1 on living bacteria. The similar rupture lengths detected using mAbs against the head and C-terminal regions, which are widely separated in the tertiary structure, suggest a higher order architecture in which these domains are in close proximity on the cell surface. Taken together, our results suggest a supramolecular organization in which additional P1 polypeptides, including the C-terminal segment originally identified as antigen II, associate with covalently attached P1 to form the functional adhesive layer.
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