Evidence map›Paper›PMID 30872786›Full record

ArticleScientific reports2019

The rsmS (ybaM) mutation causes bypass suppression of the RsmAB post-transcriptional virulence regulation system in enterobacterial phytopathogens.

Rita E Monson, Katinka Apagyi, Steven D Bowden, Natalie Simpson, Neil R Williamson, Marion F Cubitt, Steve Harris, Ian K Toth, George P C Salmond

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.2field-weighted citation impact, top 16% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

9 authors at 4 institutions in 2 countries.

Rita E MonsonDepartment of Biochemistry, Hopkins Building, Tennis Court Road, University of Cambridge, Cambridge, CB2 1QW, UK.ORCID 0000-0001-7066-840X
Katinka ApagyiDepartment of Biochemistry, Hopkins Building, Tennis Court Road, University of Cambridge, Cambridge, CB2 1QW, UK.
Steven D BowdenDepartment of Biochemistry, Hopkins Building, Tennis Court Road, University of Cambridge, Cambridge, CB2 1QW, UK.
Natalie SimpsonDepartment of Biochemistry, Hopkins Building, Tennis Court Road, University of Cambridge, Cambridge, CB2 1QW, UK.
Neil R WilliamsonDepartment of Biochemistry, Hopkins Building, Tennis Court Road, University of Cambridge, Cambridge, CB2 1QW, UK.
Marion F CubittDepartment of Biochemistry, Hopkins Building, Tennis Court Road, University of Cambridge, Cambridge, CB2 1QW, UK.
Steve HarrisDepartment of Biochemistry, Hopkins Building, Tennis Court Road, University of Cambridge, Cambridge, CB2 1QW, UK.
Ian K TothCell and Molecular Sciences, James Hutton Institute, Invergowrie, Dundee, DD2 5DA, UK.
George P C SalmondDepartment of Biochemistry, Hopkins Building, Tennis Court Road, University of Cambridge, Cambridge, CB2 1QW, UK. gpcs2@cam.ac.uk.
University of Cambridge · GBJames Hutton Institute · GBLoughborough University · GBUniversity of Minnesota · US

Funding

Biotechnology and Biological Sciences Research Council BB/F009666/1Biotechnology and Biological Sciences Research Council BB/H013261/1Biotechnology and Biological Sciences Research Council BB/N008081/1Medical Research Council
6 · The paper itself

Abstract

Plant cell wall degrading enzymes (PCWDEs) are the primary virulence determinants of soft rotting bacteria such as the potato pathogen, Pectobacterium atrosepticum. The regulation of secondary metabolite (Rsm) system controls production of PCWDEs in response to changing nutrient conditions. This work identified a new suppressor of an rsmB mutation - ECA1172 or rsmS (rsmB suppressor). Mutants defective in rsmB (encoding a small regulatory RNA), show reduced elaboration of the quorum sensing molecule (N-3-oxohexanoyl-homoserine lactone; OHHL) and PCWDEs. However, OHHL and PCWDE production were partially restored in an rsmB, rsmS double mutant. Single rsmS mutants, overproduced PCWDEs and OHHL relative to wild type P. atrosepticum and exhibited hypervirulence in potato. RsmS overproduction also resulted in increased PCWDEs and OHHL. Homology searches revealed rsmS conservation across pathogens such as Escherichia coli (ybaM), Dickeya solani, Klebsiella pneumoniae and Shigella flexneri. An rsmS mutant of Pectobacterium carotovorum ATCC39048 showed bypass of rsmB-dependent repression of PCWDEs and OHHL production. P. carotovorum ATCC39048 produces the β-lactam antibiotic, 1-carbapen-2-em-3-carboxylic acid (a carbapenem). Production of the antibiotic was repressed in an rsmB mutant but partially restored in an rsmB, rsmS double mutant. This work highlights the importance of RsmS, as a conserved pleiotropic regulator of virulence and antibiotic biosynthesis.

Indexed as

4-ButyrolactoneAmino Acid SequenceBacterial ProteinsCarbapenemsGene Expression Regulation, BacterialMutationPectobacteriumPeptide HydrolasesSequence AlignmentSolanum tuberosumVirulence4-ButyrolactoneBacterial ProteinsCarbapenemshomoserine lactonePeptide Hydrolases

Identifiers

PMID30872786
PMCPMC6418279
OpenAlexW2921872640

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.