Evidence map›Paper›PMID 24465005›Full record

ArticleNucleic acids research2014

A widespread bacteriophage abortive infection system functions through a Type IV toxin-antitoxin mechanism.

Ron L Dy, Rita Przybilski, Koen Semeijn, George P C Salmond, Peter C Fineran

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 179 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
179citing papers in PubMed, 1 pooled it
11.8field-weighted citation impact, top 1% 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

179 citing papers in PubMed, 1 synthesis or guideline pooled it, 305 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Bacterial immune systems.Antonie van Leeuwenhoek · 2026
    Review
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  12. Genomic profiling ofMicrobiology spectrum · 2026
    Article
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  19. Article
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119 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 2 countries.

Ron L DyDepartment of Microbiology and Immunology, University of Otago, 720 Cumberland Street, PO Box 56, Dunedin 9054, New Zealand and Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK.
Rita Przybilski
Koen Semeijn
George P C Salmond
Peter C Fineran
University of Cambridge · GBUniversity of Otago · NZ

Funding

Biotechnology and Biological Sciences Research Council BB/H002677/1
6 · The paper itself

Abstract

Bacterial abortive infection (Abi) systems are 'altruistic' cell death systems that are activated by phage infection and limit viral replication, thereby providing protection to the bacterial population. Here, we have used a novel approach of screening Abi systems as a tool to identify and characterize toxin-antitoxin (TA)-acting Abi systems. We show that AbiE systems are encoded by bicistronic operons and function via a non-interacting (Type IV) bacteriostatic TA mechanism. The abiE operon was negatively autoregulated by the antitoxin, AbiEi, a member of a widespread family of putative transcriptional regulators. AbiEi has an N-terminal winged-helix-turn-helix domain that is required for repression of abiE transcription, and an uncharacterized bi-functional C-terminal domain, which is necessary for transcriptional repression and sufficient for toxin neutralization. The cognate toxin, AbiEii, is a predicted nucleotidyltransferase (NTase) and member of the DNA polymerase β family. AbiEii specifically bound GTP, and mutations in conserved NTase motifs (I-III) and a newly identified motif (IV), abolished GTP binding and subsequent toxicity. The AbiE systems can provide phage resistance and enable stabilization of mobile genetic elements, such as plasmids. Our study reveals molecular insights into the regulation and function of the widespread bi-functional AbiE Abi-TA systems and the biochemical properties of both toxin and antitoxin proteins.

Indexed as

Bacterial ProteinsBacterial ToxinsBacteriophagesDNA-Binding ProteinsGene Expression Regulation, BacterialGenome, BacterialGuanosine TriphosphateInverted Repeat SequencesLactococcus lactisMutationNucleotidyltransferasesPlasmidsPromoter Regions, GeneticProtein Structure, TertiaryRepressor ProteinsStreptococcus agalactiaeBacterial ProteinsBacterial ToxinsDNA-Binding ProteinsGuanosine TriphosphateNucleotidyltransferasesRepressor Proteins

Identifiers

PMID24465005
PMCPMC3985639
OpenAlexW2146276053

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.