Evidence map›Paper›PMID 34330923›Full record

ArticleNature communications2021

Toxin import through the antibiotic efflux channel TolC.

Nicholas G Housden, Melissa N Webby, Edward D Lowe, Tarick J El-Baba, Renata Kaminska, Christina Redfield, Carol V Robinson, Colin Kleanthous

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. TheFrontiers in medicine · 2026
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  11. A coevolution experiment betweenMicrobiology (Reading, England) · 2023
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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

8 authors at 1 institution in 1 country.

Nicholas G Housden *Department of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0002-4706-8278
Melissa N Webby *Department of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0001-5721-0381
Edward D LoweDepartment of Biochemistry, University of Oxford, Oxford, UK.
Tarick J El-BabaPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.
Renata KaminskaDepartment of Biochemistry, University of Oxford, Oxford, UK.
Christina RedfieldDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0001-7297-7708
Carol V RobinsonPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.ORCID 0000-0001-7829-5505
Colin KleanthousDepartment of Biochemistry, University of Oxford, Oxford, UK. colin.kleanthous@bioch.ox.ac.uk.ORCID 0000-0002-3273-0302
University of Oxford · GB

Funding

Medical Research Council MR/N020413/1Wellcome TrustWellcome Trust 201505/Z/16/Z
6 · The paper itself

Abstract

Bacteria often secrete diffusible protein toxins (bacteriocins) to kill bystander cells during interbacterial competition. Here, we use biochemical, biophysical and structural analyses to show how a bacteriocin exploits TolC, a major outer-membrane antibiotic efflux channel in Gram-negative bacteria, to transport itself across the outer membrane of target cells. Klebicin C (KlebC), a rRNase toxin produced by Klebsiella pneumoniae, binds TolC of a related species (K. quasipneumoniae) with high affinity through an N-terminal, elongated helical hairpin domain common amongst bacteriocins. The KlebC helical hairpin opens like a switchblade to bind TolC. A cryo-EM structure of this partially translocated state, at 3.1 Å resolution, reveals that KlebC associates along the length of the TolC channel. Thereafter, the unstructured N-terminus of KlebC protrudes beyond the TolC iris, presenting a TonB-box sequence to the periplasm. Association with proton-motive force-linked TonB in the inner membrane drives toxin import through the channel. Finally, we demonstrate that KlebC binding to TolC blocks drug efflux from bacteria. Our results indicate that TolC, in addition to its known role in antibiotic export, can function as a protein import channel for bacteriocins.

Indexed as

Anti-Bacterial AgentsBacterial Outer Membrane ProteinsBacterial ProteinsBacteriocinsBiological TransportCryoelectron MicroscopyIon ChannelsKlebsiellaMembrane Transport ProteinsModels, MolecularProtein BindingProtein ConformationAnti-Bacterial AgentsBacterial Outer Membrane ProteinsBacterial ProteinsBacteriocinsIon ChannelsklebocinMembrane Transport Proteins

Identifiers

PMID34330923
PMCPMC8324772
OpenAlexW3186355098

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.