Evidence map›Paper›PMID 34728631›Full record

ArticleNature communications2021

CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage.

Rebecca Conners, Mathew McLaren, Urszula Łapińska, Kelly Sanders, M Rhia L Stone, Mark A T Blaskovich, Stefano Pagliara, Bertram Daum, Jasna Rakonjac, Vicki A M Gold

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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

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  15. AncientProceedings. Biological sciences · 2023
    Article
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  17. Using AlphaFold Predictions in Viral Research.Current issues in molecular biology · 2023
    Review
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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

10 authors at 3 institutions in 3 countries.

Rebecca ConnersLiving Systems Institute, University of Exeter, Exeter, UK.ORCID http://orcid.org/0000-0002-8653-1771
Mathew McLarenLiving Systems Institute, University of Exeter, Exeter, UK.
Urszula ŁapińskaLiving Systems Institute, University of Exeter, Exeter, UK.
Kelly SandersLiving Systems Institute, University of Exeter, Exeter, UK.
M Rhia L StoneCentre for Superbug Solutions, Institute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, Australia.
Mark A T BlaskovichCentre for Superbug Solutions, Institute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland, Australia.ORCID http://orcid.org/0000-0001-9447-2292
Stefano PagliaraLiving Systems Institute, University of Exeter, Exeter, UK.
Bertram DaumLiving Systems Institute, University of Exeter, Exeter, UK.ORCID http://orcid.org/0000-0002-3767-264X
Jasna RakonjacSchool of Fundamental Sciences, Massey University, Palmerston North, New Zealand.ORCID http://orcid.org/0000-0002-6756-4682
Vicki A M GoldLiving Systems Institute, University of Exeter, Exeter, UK. v.a.m.gold@exeter.ac.uk.ORCID http://orcid.org/0000-0002-6908-0745
University of Exeter · GBThe University of Queensland · AUMassey University · NZ

Funding

Biotechnology and Biological Sciences Research Council BB/R000484/1Biotechnology and Biological Sciences Research Council BB/R008639/1Biotechnology and Biological Sciences Research Council BB/V008021/1Medical Research Council MC_PC_17189Medical Research Council MCPC17189Wellcome TrustWellcome Trust 202904/Z/16/ZWellcome Trust 206181/Z/17/ZWellcome Trust 210363/Z/18/Z
6 · The paper itself

Abstract

The Ff family of filamentous bacteriophages infect gram-negative bacteria, but do not cause lysis of their host cell. Instead, new virions are extruded via the phage-encoded pIV protein, which has homology with bacterial secretins. Here, we determine the structure of pIV from the f1 filamentous bacteriophage at 2.7 Å resolution by cryo-electron microscopy, the first near-atomic structure of a phage secretin. Fifteen f1 pIV subunits assemble to form a gated channel in the bacterial outer membrane, with associated soluble domains projecting into the periplasm. We model channel opening and propose a mechanism for phage egress. By single-cell microfluidics experiments, we demonstrate the potential for secretins such as pIV to be used as adjuvants to increase the uptake and efficacy of antibiotics in bacteria. Finally, we compare the f1 pIV structure to its homologues to reveal similarities and differences between phage and bacterial secretins.

Indexed as

Amino Acid SequenceBiological TransportCryoelectron MicroscopyInovirusProtein Structural ElementsSecretinSequence AlignmentViral Nonstructural ProteinspIV protein, Enterobacteria phage f1SecretinViral Nonstructural Proteins

Identifiers

PMID34728631
PMCPMC8563730
OpenAlexW3209565305

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.