Evidence map›Paper›PMID 28141493›Full record

ArticleMicrobiology (Reading, England)2017

Functional amyloids in Streptococcus mutans, their use as targets of biofilm inhibition and initial characterization of SMU_63c.

Richard N Besingi, Iwona B Wenderska, Dilani B Senadheera, Dennis G Cvitkovitch, Joanna R Long, Zezhang T Wen, L Jeannine Brady

Open access · greenAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
4.5field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

67 citing papers in PubMed, 99 citations in OpenAlex.

  1. Review
  2. Review
  3. Recent advances in membrane vesicles ofJournal of oral microbiology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Amyloid Fibrils Produced byInternational journal of molecular sciences · 2023
    Article
  14. Article
  15. Article
  16. An apparent lack of synergy between degradative enzymes againstbioRxiv : the preprint server for biology · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Growth with Commensal Streptococci AltersJournal of dental research · 2023
    Article

7 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

Richard N BesingiDepartment of Oral Biology, University of Florida, Gainesville, FL, USA.
Iwona B WenderskaDepartment of Oral Microbiology, Faculty of Dentistry, University of Toronto, Toronto, ON, Canada.
Dilani B SenadheeraDepartment of Oral Microbiology, Faculty of Dentistry, University of Toronto, Toronto, ON, Canada.
Dennis G CvitkovitchDepartment of Oral Microbiology, Faculty of Dentistry, University of Toronto, Toronto, ON, Canada.
Joanna R LongDepartment of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL, USA.
Zezhang T WenDepartment of Comprehensive Dentistry and Biomaterials and Center of Excellence in Oral and Craniofacial Biology, Louisiana State University Health Sciences Center, New Orleans, LA, USA.
L Jeannine BradyDepartment of Oral Biology, University of Florida, Gainesville, FL, USA.
University of Florida · USUniversity of Toronto · CALouisiana State University Health Sciences Center New Orleans · US

Funding

Comprehensive Training Program in Oral BiologyT90DE021990 · NIDCR · UNIVERSITY OF FLORIDA · PI Jose A Lemos · 2011 to 2026
$8.2M
BrpA in Virulence Modulation of Streptococcus mutansR01DE019452 · NIDCR · LSU HEALTH SCIENCES CENTER · PI ZEZHANG TOM WEN, Hui Wu · 2009 to 2026
$6.3M
Role of the Spx Regulator in Streptococcus mutansR01DE019783 · NIDCR · UNIVERSITY OF ROCHESTER · PI LEMOS, JOSE A · 2010 to 2020
$3.7M
Functional Amyloid Formation in Streptococcus mutansR01DE021789 · NIDCR · UNIVERSITY OF FLORIDA · PI BRADY, L. JEANNINE, LONG, JOANNA R · 2012 to 2021
$3.7M
eDNA Secretion and eDNA-Cell Interactions in Biofilm FormationR21DE025348 · NIDCR · LSU HEALTH SCIENCES CENTER · PI BRADY, L. JEANNINE, WEN, ZEZHANG TOM · 2016 to 2017
$419k
NIDCR NIH HHS R01 DE019452NIDCR NIH HHS R01 DE019783NIDCR NIH HHS R01 DE021789NIDCR NIH HHS R21 DE025348NIDCR NIH HHS T90 DE021990
6 · The paper itself

Abstract

Amyloids have been identified as functional components of the extracellular matrix of bacterial biofilms. Streptococcus mutans is an established aetiologic agent of dental caries and a biofilm dweller. In addition to the previously identified amyloidogenic adhesin P1 (also known as AgI/II, PAc), we show that the naturally occurring antigen A derivative of S. mutans wall-associated protein A (WapA) and the secreted protein SMU_63c can also form amyloid fibrils. P1, WapA and SMU_63c were found to significantly influence biofilm development and architecture, and all three proteins were shown by immunogold electron microscopy to reside within the fibrillar extracellular matrix of the biofilms. We also showed that SMU_63c functions as a negative regulator of biofilm cell density and genetic competence. In addition, the naturally occurring C-terminal cleavage product of P1, C123 (also known as AgII), was shown to represent the amyloidogenic moiety of this protein. Thus, P1 and WapA both represent sortase substrates that are processed to amyloidogenic truncation derivatives. Our current results suggest a novel mechanism by which certain cell surface adhesins are processed and contribute to the amyloidogenic capability of S. mutans. We further demonstrate that the polyphenolic small molecules tannic acid and epigallocatechin-3-gallate, and the benzoquinone derivative AA-861, which all inhibit amyloid fibrillization of C123 and antigen A in vitro, also inhibit S. mutans biofilm formation via P1- and WapA-dependent mechanisms, indicating that these proteins serve as therapeutic targets of anti-amyloid compounds.

Indexed as

Adhesins, BacterialAmyloidAntigens, BacterialBacterial AdhesionBacterial ProteinsBiofilmsExtracellular MatrixStreptococcus mutansTanninsAdhesins, BacterialAmyloidAntigens, BacterialBacterial ProteinsTanninswapA protein, Bacillus subtilis

Identifiers

PMID28141493
PMCPMC5775903
OpenAlexW2595890601

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.