Evidence map›Paper›PMID 27327765›Full record

ArticlePLoS pathogens2016

Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals.

Agustina Taglialegna, Susanna Navarro, Salvador Ventura, James A Garnett, Steve Matthews, José R Penades, Iñigo Lasa, Jaione Valle

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

101 citing papers in PubMed, 182 citations in OpenAlex.

  1. Review
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  14. Thymoquinone/β-Frontiers in cellular and infection microbiology · 2025
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  15. Cross-Kingdom Pathogenesis ofMicroorganisms · 2024
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  18. Review
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  20. Natural compounds in the fight againstFrontiers in pharmacology · 2024
    Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 5 institutions in 2 countries.

Agustina TaglialegnaLaboratory of Microbial Biofilms, Idab-CSIC-Universidad Pública de Navarra-Gobierno de Navarra and Dpto Producción Agraria, Pamplona, Spain.
Susanna NavarroInstitut de Biotecnologia i de Biomedicina and Departament de Bioquimica i Biologia Molecular, Universitat Autonoma de Barcelona, Bellaterra, Spain.
Salvador VenturaInstitut de Biotecnologia i de Biomedicina and Departament de Bioquimica i Biologia Molecular, Universitat Autonoma de Barcelona, Bellaterra, Spain.
James A GarnettSchool of Biological and Chemical Sciences, Queen Mary University of London, London, United Kingdom.
Steve MatthewsDepartment of Life Sciences, Imperial College London, London, United Kingdom.
José R PenadesInstitute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
Iñigo LasaLaboratory of Microbial Biofilms, Idab-CSIC-Universidad Pública de Navarra-Gobierno de Navarra and Dpto Producción Agraria, Pamplona, Spain.
Jaione ValleLaboratory of Microbial Biofilms, Idab-CSIC-Universidad Pública de Navarra-Gobierno de Navarra and Dpto Producción Agraria, Pamplona, Spain.
Universidad Publica de Navarra · ESUniversitat Autònoma de Barcelona · ESImperial College London · GBQueen Mary University of London · GBUniversity of Glasgow · GB

Funding

Medical Research Council G1001664Medical Research Council MR/J006874/1Wellcome Trust 100280Wellcome Trust 104933
6 · The paper itself

Abstract

Biofilms are communities of bacteria that grow encased in an extracellular matrix that often contains proteins. The spatial organization and the molecular interactions between matrix scaffold proteins remain in most cases largely unknown. Here, we report that Bap protein of Staphylococcus aureus self-assembles into functional amyloid aggregates to build the biofilm matrix in response to environmental conditions. Specifically, Bap is processed and fragments containing at least the N-terminus of the protein become aggregation-prone and self-assemble into amyloid-like structures under acidic pHs and low concentrations of calcium. The molten globule-like state of Bap fragments is stabilized upon binding of the cation, hindering its self-assembly into amyloid fibers. These findings define a dual function for Bap, first as a sensor and then as a scaffold protein to promote biofilm development under specific environmental conditions. Since the pH-driven multicellular behavior mediated by Bap occurs in coagulase-negative staphylococci and many other bacteria exploit Bap-like proteins to build a biofilm matrix, the mechanism of amyloid-like aggregation described here may be widespread among pathogenic bacteria.

Indexed as

Amyloidogenic ProteinsAnimalsBacterial ProteinsBiofilmsDisease Models, AnimalImmunoblottingMiceMicroscopy, FluorescencePolymerase Chain ReactionStaphylococcal InfectionsStaphylococcus aureusAmyloidogenic ProteinsBacterial ProteinsBap protein, Staphylococcus aureus

Identifiers

PMID27327765
PMCPMC4915627
OpenAlexW2468157290

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.