Evidence map›Paper›PMID 31598959›Full record

ArticleFEBS letters2020

The gelatinase biosynthesis-activating pheromone binds and stabilises the FsrB membrane protein in Enterococcus faecalis quorum sensing.

Sean Littlewood, Helena Tattersall, Charlotte S Hughes, Rohanah Hussain, Pikyee Ma, Stephen E Harding, Jiro Nakayama, Mary K Phillips-Jones

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

2 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
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 5 institutions in 2 countries.

Sean LittlewoodSchool of Pharmacy and Biomedical Sciences, University of Central Lancashire, Preston, UK.
Helena TattersallSchool of Pharmacy and Biomedical Sciences, University of Central Lancashire, Preston, UK.
Charlotte S HughesSchool of Pharmacy and Biomedical Sciences, University of Central Lancashire, Preston, UK.
Rohanah HussainDiamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, UK.
Pikyee MaAstbury Centre for Structural Molecular Biology, University of Leeds, UK.ORCID 0000-0003-4080-2908
Stephen E HardingNational Centre for Macromolecular Hydrodynamics, School of Biosciences, University of Nottingham, Sutton Bonington, UK.
Jiro NakayamaDepartment of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka, Japan.
Mary K Phillips-JonesNational Centre for Macromolecular Hydrodynamics, School of Biosciences, University of Nottingham, Sutton Bonington, UK.ORCID 0000-0002-0362-4690
University of Lancashire · GBUniversity of Nottingham · GBDiamond Light Source · GBKyushu University · JPUniversity of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D001641/1
6 · The paper itself

Abstract

Quorum-sensing mechanisms regulate gene expression in response to changing cell-population density detected through pheromones. In Enterococcus faecalis, Fsr quorum sensing produces and responds to the gelatinase biosynthesis-activating pheromone (GBAP). Here we establish that the enterococcal FsrB membrane protein has a direct role connected with GBAP by showing that GBAP binds to purified FsrB. Far-UV CD measurements demonstrated a predominantly α-helical protein exhibiting a small level of conformational flexibility. Fivefold (400 μm) GBAP stabilised FsrB (80 μm) secondary structure. FsrB thermal denaturation in the presence and absence of GBAP revealed melting temperatures of 70.1 and 60.8 °C, respectively, demonstrating GBAP interactions and increased thermal stability conferred by GBAP. Addition of GBAP also resulted in tertiary structural changes, confirming GBAP binding.

Indexed as

Amino Acid SequenceBacterial ProteinsEnterococcus faecalisLactonesPeptides, CyclicProtein BindingProtein Conformation, alpha-HelicalProtein StabilityQuorum SensingAgrCfs protein, Enterococcus faecalisBacterial Proteinsgelatinase biosynthesis-activating pheromoneLactonesPeptides, Cycliccircular dichroismEnterococcus faecalisFsrBquorum sensing

Identifiers

PMID31598959
PMCPMC7028047
OpenAlexW2979690702

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.