Evidence map›Paper›PMID 23082034›Full record

ArticleMicrobiology (Reading, England)2012

Functional amyloid formation by Streptococcus mutans.

M W Oli, H N Otoo, P J Crowley, K P Heim, M M Nascimento, C B Ramsook, P N Lipke, L J Brady

Abstract read
In one paragraph

Article in Microbiology (Reading, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

84 citing papers in PubMed, 144 citations in OpenAlex.

  1. The microbiota-proteostasis axis: implications in neurodegenerative diseases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. Virtual Screening of Inhibitors ofACS medicinal chemistry letters · 2024
    Article
  10. Review
  11. Article
  12. Review
  13. Amyloid Fibrils Produced byInternational journal of molecular sciences · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Bacterial biofilms in the human body: prevalence and impacts on health and disease.Frontiers in cellular and infection microbiology · 2023
    Review

24 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

8 authors at 2 institutions in 1 country.

M W OliUniversity of Florida, Department of Oral Biology, Gainesville, FL, USA.
H N OtooUniversity of Florida, Department of Oral Biology, Gainesville, FL, USA.
P J CrowleyUniversity of Florida, Department of Oral Biology, Gainesville, FL, USA.
K P HeimUniversity of Florida, Department of Oral Biology, Gainesville, FL, USA.
M M NascimentoUniversity of Florida, Department of Oral Biology, Gainesville, FL, USA.
C B RamsookDepartment of Biology, Brooklyn College of the City University of New York, NY, USA.
P N LipkeDepartment of Biology, Brooklyn College of the City University of New York, NY, USA.
L J BradyUniversity of Florida, Department of Oral Biology, Gainesville, FL, USA.
University of Florida · USBrooklyn College · US

Funding

MEMBRANES OF THE DENTAL PATHOGEN STREPTOCOCCUS MUTANSR01DE008007 · NIDCR · UNIVERSITY OF FLORIDA · PI L. Jeannine Brady, Surabhi Mishra · 1986 to 2026
$8.6M
Functional Amyloid Formation in Streptococcus mutansR01DE021789 · NIDCR · UNIVERSITY OF FLORIDA · PI BRADY, L. JEANNINE, LONG, JOANNA R · 2012 to 2021
$3.7M
Amyloid-like Interactions in Yeast Cell AdhesionSC1GM083756 · NIGMS · BROOKLYN COLLEGE · PI LIPKE, PETER N · 2008 to 2011
$1.7M
Diversity Supplement to R01 GM 098616 for Ivor JosephR01GM098616 · NIGMS · BROOKLYN COLLEGE · PI LIPKE, PETER N · 2012 to 2015
$1.5M
Conformational regulation of arrestin-mediated signalingR01GM081756 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2008 to 2011
$1.5M
NIDCR NIH HHS R01 DE008007NIDCR NIH HHS R01 DE021789NIDCR NIH HHS R01DE08007NIDCR NIH HHS R01DE21789NIGMS NIH HHS R01 GM081756NIGMS NIH HHS R01 GM098616NIGMS NIH HHS R01GM098616NIGMS NIH HHS SC1 GM083756NIGMS NIH HHS SC1GM81756
6 · The paper itself

Abstract

Dental caries is a common infectious disease associated with acidogenic and aciduric bacteria, including Streptococcus mutans. Organisms that cause cavities form recalcitrant biofilms, generate acids from dietary sugars and tolerate acid end products. It has recently been recognized that micro-organisms can produce functional amyloids that are integral to biofilm development. We now show that the S. mutans cell-surface-localized adhesin P1 (antigen I/II, PAc) is an amyloid-forming protein. This conclusion is based on the defining properties of amyloids, including binding by the amyloidophilic dyes Congo red (CR) and Thioflavin T (ThT), visualization of amyloid fibres by transmission electron microscopy and the green birefringent properties of CR-stained protein aggregates when viewed under cross-polarized light. We provide evidence that amyloid is present in human dental plaque and is produced by both laboratory strains and clinical isolates of S. mutans. We provide further evidence that amyloid formation is not limited to P1, since bacterial colonies without this adhesin demonstrate residual green birefringence. However, S. mutans lacking sortase, the transpeptidase enzyme that mediates the covalent linkage of its substrates to the cell-wall peptidoglycan, including P1 and five other proteins, is not birefringent when stained with CR and does not form biofilms. Biofilm formation is inhibited when S. mutans is cultured in the presence of known inhibitors of amyloid fibrillization, including CR, Thioflavin S and epigallocatechin-3-gallate, which also inhibited ThT uptake by S. mutans extracellular proteins. Taken together, these results indicate that S. mutans is an amyloid-forming organism and suggest that amyloidogenesis contributes to biofilm formation by this oral microbe.

Indexed as

Adhesins, BacterialAmyloidBenzothiazolesBiofilmsCongo RedMicroscopy, Electron, TransmissionStaining and LabelingStreptococcus mutansThiazolesAdhesins, BacterialAmyloidBenzothiazolesCongo RedThiazolesthioflavin T

Identifiers

PMID23082034
PMCPMC4083658
OpenAlexW2088965395

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.