Evidence map›Paper›PMID 32339530›Full record

ArticleJournal of molecular biology2020

Targeted Killing of Pseudomonas aeruginosa by Pyocin G Occurs via the Hemin Transporter Hur.

Iva Atanaskovic, Khedidja Mosbahi, Connor Sharp, Nicholas G Housden, Renata Kaminska, Daniel Walker, Colin Kleanthous

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

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  11. iScience · 2022
    Article
  12. Article
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  14. Review
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

7 authors at 2 institutions in 1 country.

Iva AtanaskovicDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Khedidja MosbahiInstitute of Infection, Immunity, and Inflammation, College of Medical, Veterinary, and Life Sciences, University of Glasgow, G12 8QQ Glasgow, UK.
Connor SharpDepartment of Zoology, University of Oxford, 11a Mansfield Rd, Oxford OX1 3SZ, UK.
Nicholas G HousdenDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Renata KaminskaDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Daniel WalkerInstitute of Infection, Immunity, and Inflammation, College of Medical, Veterinary, and Life Sciences, University of Glasgow, G12 8QQ Glasgow, UK.
Colin KleanthousDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: colin.kleanthous@bioch.ox.ac.uk.
University of Oxford · GBUniversity of Glasgow · GB

Funding

Wellcome TrustWellcome Trust 201505/Z/16/Z
6 · The paper itself

Abstract

Pseudomonas aeruginosa is a priority pathogen for the development of new antibiotics, particularly because multi-drug-resistant strains of this bacterium cause serious nosocomial infections and are the leading cause of death in cystic fibrosis patients. Pyocins, bacteriocins of P. aeruginosa, are potent and diverse protein antibiotics that are deployed during bacterial competition. Pyocins are produced by more than 90% of P. aeruginosa strains and may have utility as last resort antibiotics against this bacterium. In this study, we explore the antimicrobial activity of a newly discovered pyocin called pyocin G (PyoG). We demonstrate that PyoG has broad killing activity against a collection of clinical P. aeruginosa isolates and is active in a Galleria mellonella infection model. We go on to identify cell envelope proteins that are necessary for the import of PyoG and its killing activity. PyoG recognizes bacterial cells by binding to Hur, an outer-membrane TonB-dependent transporter. Both pyocin and Hur interact with TonB1, which in complex with ExbB-ExbD links the proton motive force generated across the inner membrane with energy-dependent pyocin translocation across the outer membrane. Inner-membrane translocation of PyoG is dependent on the conserved inner-membrane AAA+ ATPase/protease, FtsH. We also report a functional exploration of the PyoG receptor. We demonstrate that Hur can bind to hemin in vitro and that this interaction is blocked by PyoG, confirming the role of Hur in hemin acquisition.

Indexed as

Anti-Bacterial AgentsATPases Associated with Diverse Cellular ActivitiesBacterial ProteinsBacteriocinsDrug Resistance, MultipleHeminHumansMembrane ProteinsProtein BindingPseudomonas aeruginosaPseudomonas InfectionsPyocinsAnti-Bacterial AgentsATPases Associated with Diverse Cellular ActivitiesBacterial ProteinsBacteriocinsHeminMembrane ProteinsPyocinstonB protein, BacteriabacteriocinFtsHprotein antibioticprotein importTonB-dependent transporter

Identifiers

PMID32339530
PMCPMC7322526
OpenAlexW3020288999

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.