Evidence map›Paper›PMID 31384001›Full record

ArticleNature microbiology2019

Atomic structures of an entire contractile injection system in both the extended and contracted states.

Ambroise Desfosses, Hariprasad Venugopal, Tapan Joshi, Jan Felix, Matthew Jessop, Hyengseop Jeong, Jaekyung Hyun, J Bernard Heymann, Mark R H Hurst, Irina Gutsche and 1 more

Open access · greenAbstract read
In one paragraph

Article in Nature microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

54 citing papers in PubMed, 84 citations in OpenAlex.

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  12. The spike tip protein of bacteriophage T4.bioRxiv : the preprint server for biology · 2025
    Article
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  16. Viruses · 2025
    Article
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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

11 authors at 6 institutions in 6 countries.

Ambroise DesfossesSchool of Biological Sciences, University of Auckland, Auckland, New Zealand.
Hariprasad VenugopalSchool of Biological Sciences, University of Auckland, Auckland, New Zealand.
Tapan JoshiSchool of Biological Sciences, University of Auckland, Auckland, New Zealand.
Jan FelixInstitut de Biologie Structurale (IBS), University Grenoble Alpes, CEA, CNRS, Grenoble, France.ORCID http://orcid.org/0000-0002-8436-9467
Matthew JessopSchool of Biological Sciences, University of Auckland, Auckland, New Zealand.ORCID http://orcid.org/0000-0001-8880-4481
Hyengseop JeongElectron Microscopy Research Center, Korea Basic Science Institute, Cheongju-si, Republic of Korea.
Jaekyung HyunElectron Microscopy Research Center, Korea Basic Science Institute, Cheongju-si, Republic of Korea.
J Bernard HeymannLaboratory for Structural Biology Research, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD, USA.ORCID http://orcid.org/0000-0002-8872-5326
Mark R H HurstForage Science, AgResearch, Lincoln Research Centre, Christchurch, New Zealand. mark.hurst@agresearch.co.nz.ORCID http://orcid.org/0000-0001-5826-5253
Irina GutscheInstitut de Biologie Structurale (IBS), University Grenoble Alpes, CEA, CNRS, Grenoble, France. irina.gutsche@ibs.fr.ORCID http://orcid.org/0000-0002-1908-3921
Alok K MitraSchool of Biological Sciences, University of Auckland, Auckland, New Zealand. a.mitra@auckland.ac.nz.ORCID http://orcid.org/0000-0003-0891-5697
Centre National de la Recherche Scientifique · FRUniversity of Auckland · NZAgResearch · NZKorea Basic Science Institute · KRNational Institutes of Health · USOkinawa Institute of Science and Technology Graduate University · JP

Funding

European Research Council 647784
6 · The paper itself

Abstract

Contractile injection systems are sophisticated multiprotein nanomachines that puncture target cell membranes. Although the number of atomic-resolution insights into contractile bacteriophage tails, bacterial type six secretion systems and R-pyocins is rapidly increasing, structural information on the contraction of bacterial phage-like protein-translocation structures directed towards eukaryotic hosts is scarce. Here, we characterize the antifeeding prophage AFP from Serratia entomophila by cryo-electron microscopy. We present the high-resolution structure of the entire AFP particle in the extended state, trace 11 protein chains de novo from the apical cap to the needle tip, describe localization variants and perform specific structural comparisons with related systems. We analyse inter-subunit interactions and highlight their universal conservation within contractile injection systems while revealing the specificities of AFP. Furthermore, we provide the structure of the AFP sheath-baseplate complex in a contracted state. This study reveals atomic details of interaction networks that accompany and define the contraction mechanism of toxin-delivery tailocins, offering a comprehensive framework for understanding their mode of action and for their possible adaptation as biocontrol agents.

Indexed as

Cryoelectron MicroscopyProphagesProtein ConformationSerratiaType VI Secretion SystemsViral ProteinsType VI Secretion SystemsViral Proteins

Identifiers

PMID31384001
PMCPMC6817355
OpenAlexW2965117640

What OpenQuestion holds

Textmetadata
LicenceTDM
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.