Evidence map›Paper›PMID 29703974›Full record

ArticleNature communications2018

The ng_ζ1 toxin of the gonococcal epsilon/zeta toxin/antitoxin system drains precursors for cell wall synthesis.

Andrea Rocker, Madeleine Peschke, Tiia Kittilä, Roman Sakson, Clara Brieke, Anton Meinhart

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
1.1field-weighted citation impact, top 26% 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

16 citing papers in PubMed, 1 synthesis or guideline pooled it, 21 citations in OpenAlex.

  1. Pooled it
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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

6 authors at 1 institution in 1 country.

Andrea RockerDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstr. 29, 69120, Heidelberg, Germany.
Madeleine PeschkeDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstr. 29, 69120, Heidelberg, Germany.
Tiia KittiläDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstr. 29, 69120, Heidelberg, Germany.
Roman SaksonDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstr. 29, 69120, Heidelberg, Germany.
Clara BriekeDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstr. 29, 69120, Heidelberg, Germany.
Anton MeinhartDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstr. 29, 69120, Heidelberg, Germany. Anton.Meinhart@imp.ac.at.
Max Planck Institute for Medical Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial toxin-antitoxin complexes are emerging as key players modulating bacterial physiology as activation of toxins induces stasis or programmed cell death by interference with vital cellular processes. Zeta toxins, which are prevalent in many bacterial genomes, were shown to interfere with cell wall formation by perturbing peptidoglycan synthesis in Gram-positive bacteria. Here, we characterize the epsilon/zeta toxin-antitoxin (TA) homologue from the Gram-negative pathogen Neisseria gonorrhoeae termed ng_ɛ1 / ng_ζ1. Contrary to previously studied streptococcal epsilon/zeta TA systems, ng_ɛ1 has an epsilon-unrelated fold and ng_ζ1 displays broader substrate specificity and phosphorylates multiple UDP-activated sugars that are precursors of peptidoglycan and lipopolysaccharide synthesis. Moreover, the phosphorylation site is different from the streptococcal zeta toxins, resulting in a different interference with cell wall synthesis. This difference most likely reflects adaptation to the individual cell wall composition of Gram-negative and Gram-positive organisms but also the distinct involvement of cell wall components in virulence.

Indexed as

Adaptation, PhysiologicalBacterial ToxinsCell WallNeisseria gonorrhoeaePeptidoglycanPhosphorylationSubstrate SpecificityToxin-Antitoxin SystemsVirulenceBacterial ToxinsPeptidoglycan

Identifiers

PMID29703974
PMCPMC5923241
OpenAlexW2800085934

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.