Evidence map›Paper›PMID 19074394›Full record

ArticleJournal of bacteriology2009

Growth deficiencies of Neisseria meningitidis pfs and luxS mutants are not due to inactivation of quorum sensing.

Karin Heurlier, Agnès Vendeville, Nigel Halliday, Andrew Green, Klaus Winzer, Christoph M Tang, Kim R Hardie

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Karin HeurlierInstitute of Infection, Inflammation and Immunity, Centre for Biomolecular Sciences, University of Nottingham, Nottingham NG7 2RD, United Kingdom. Karin.heurlier@nottingham.ac.uk
Agnès Vendeville
Nigel Halliday
Andrew Green
Klaus Winzer
Christoph M Tang
Kim R Hardie
University of Nottingham · GBImperial College London · GBUniversity of Edinburgh · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D007038/1Wellcome Trust
6 · The paper itself

Abstract

The activated methyl cycle (AMC) is a central metabolic pathway used to generate (and recycle) several important metabolites and enable methylation. Pfs and LuxS are considered integral components of this pathway because they convert S-adenosylhomocysteine (SAH) to S-ribosylhomocysteine (SRH) and S-ribosylhomocysteine to homocysteine (HCY), respectively. The latter reaction has a second function since it also generates the precursor of the quorum-sensing molecule autoinducer 2 (AI-2). By demonstrating that there was a complete lack of AI-2 production in pfs mutants of the causative agent of meningitis and septicemia, Neisseria meningitidis, we showed that the Pfs reaction is the sole intracellular source of the AI-2 signal. Analysis of lacZ reporters and real-time PCR experiments indicated that pfs is expressed constitutively from a promoter immediately upstream, and careful study of the pfs mutants revealed a growth defect that could not be attributed to a lack of AI-2. Metabolite profiling of the wild type and of a pfs mutant under various growth conditions revealed changes in the concentrations of several AMC metabolites, particularly SRH and SAH and under some conditions also HCY. Similar studies established that an N. meningitidis luxS mutant also has metabolite pool changes and growth defects in line with the function of LuxS downstream of Pfs in the AMC. Thus, the observed growth defect of N. meningitidis pfs and luxS mutants is not due to quorum sensing but is probably due to metabolic imbalance and, in the case of pfs inactivation, is most likely due to toxic accumulation of SAH.

Indexed as

Bacterial ProteinsCarbon-Sulfur LyasesGene Expression Regulation, BacterialHomoserineLactonesMutationNeisseria meningitidisN-Glycosyl HydrolasesQuorum Sensingadenosylhomocysteine nucleosidaseBacterial ProteinsCarbon-Sulfur LyasesHomoserineLactonesLuxS protein, BacteriaN-Glycosyl HydrolasesN-octanoylhomoserine lactone

Identifiers

PMID19074394
PMCPMC2632006
OpenAlexW2164892862

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.