Evidence map›Paper›PMID 29209037›Full record

ArticleNature communications2017

Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection.

Charles-Adrien Arnaud, Grégory Effantin, Corinne Vivès, Sylvain Engilberge, Maria Bacia, Pascale Boulanger, Eric Girard, Guy Schoehn, Cécile Breyton

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

61 citing papers in PubMed, 104 citations in OpenAlex.

  1. The Lord of the Rings: Cysteine bonds crosslink the tail of siphovirus.Protein science : a publication of the Protein Society · 2026
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  2. Article
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  4. mBio · 2026
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  7. Computational and structural biotechnology journal · 2026
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  16. iScience · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article

1 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

9 authors at 2 institutions in 1 country.

Charles-Adrien ArnaudUniversité Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS), 38000, Grenoble, France.
Grégory EffantinUniversité Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS), 38000, Grenoble, France.
Corinne VivèsUniversité Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS), 38000, Grenoble, France.
Sylvain EngilbergeUniversité Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS), 38000, Grenoble, France.
Maria BaciaUniversité Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS), 38000, Grenoble, France.
Pascale BoulangerInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91405, Gif-sur-Yvette, France.ORCID http://orcid.org/0000-0003-4912-5392
Eric GirardUniversité Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS), 38000, Grenoble, France.ORCID http://orcid.org/0000-0002-5758-6095
Guy SchoehnUniversité Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS), 38000, Grenoble, France.ORCID http://orcid.org/0000-0002-1459-3201
Cécile BreytonUniversité Grenoble Alpes, CNRS, CEA, Institut for Structural Biology (IBS), 38000, Grenoble, France. Cecile.Breyton@ibs.fr.ORCID http://orcid.org/0000-0002-4382-0434
Centre National de la Recherche Scientifique · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The vast majority of phages, bacterial viruses, possess a tail ensuring host recognition, cell wall perforation and safe viral DNA transfer from the capsid to the host cytoplasm. Long flexible tails are formed from the tail tube protein (TTP) polymerised as hexameric rings around and stacked along the tape measure protein (TMP). Here, we report the crystal structure of T5 TTP pb6 at 2.2 Å resolution. Pb6 is unusual in forming a trimeric ring, although structure analysis reveals homology with all classical TTPs and related tube proteins of bacterial puncturing devices (type VI secretion system and R-pyocin). Structures of T5 tail tubes before and after interaction with the host receptor were determined by cryo-electron microscopy at 6 Å resolution. Comparison of these two structures reveals that host-binding information is not propagated to the capsid through conformational changes in the tail tube, suggesting a role of the TMP in this information transduction process.

Indexed as

BacteriophagesCapsidCryoelectron MicroscopyCytoplasmDNA, ViralEscherichia coliSiphoviridaeStructural Homology, ProteinViral Tail ProteinsDNA, ViralViral Tail Proteins

Identifiers

PMID29209037
PMCPMC5717097
OpenAlexW2769649361

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.