Evidence map›Paper›PMID 23857636›Full record

ArticleThe Journal of biological chemistry2013

Three-dimensional structure of the toxin-delivery particle antifeeding prophage of Serratia entomophila.

J Bernard Heymann, Joseph D Bartho, Daria Rybakova, Hari P Venugopal, Dennis C Winkler, Anindito Sen, Mark R H Hurst, Alok K Mitra

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
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  8. Tyrosine-modifying glycosylation by Yersinia effectors.The Journal of biological chemistry · 2024
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  19. TheeLife · 2019
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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 3 institutions in 2 countries.

J Bernard HeymannFrom the NIAMS, National Institutes of Health, Bethesda, Maryland 20892.
Joseph D BarthoSchool of Biological Sciences, University of Auckland, Auckland 1142, New Zealand, and.
Daria RybakovaInnovative Farm Systems, Agresearch, Lincoln, Christchurch 8140, New Zealand.
Hari P VenugopalSchool of Biological Sciences, University of Auckland, Auckland 1142, New Zealand, and.
Dennis C WinklerFrom the NIAMS, National Institutes of Health, Bethesda, Maryland 20892.
Anindito SenSchool of Biological Sciences, University of Auckland, Auckland 1142, New Zealand, and.
Mark R H HurstInnovative Farm Systems, Agresearch, Lincoln, Christchurch 8140, New Zealand.
Alok K MitraSchool of Biological Sciences, University of Auckland, Auckland 1142, New Zealand, and. Electronic address: a.mitra@auckland.ac.nz.
University of Auckland · NZAgResearch · NZNational Institutes of Health · US

Funding

Intramural NIH HHS
6 · The paper itself

Abstract

The Serratia entomophila antifeeding prophage (Afp) is a bullet-shaped toxin-delivery apparatus similar to the R-pyocins of Pseudomonas aeruginosa. Morphologically it resembles the sheathed tail of bacteriophages such as T4, including a baseplate at one end. It also shares features with the type VI secretion systems. Cryo-electron micrographs of tilted Afp specimens (up to 60 degrees) were analyzed to determine the correct cyclic symmetry to overcome the limitation imposed by exclusively side views in nominally untilted specimens. An asymmetric reconstruction shows clear 6-fold cyclic symmetry contrary to a previous conclusion of 4-fold symmetry based on analysis of only the preferred side views (Sen, A., Rybakova, D., Hurst, M. R., and Mitra, A. K. (2010) J. Bacteriol. 192, 4522-4525). Electron tomography of negatively stained Afp revealed right-handed helical striations in many of the particles, establishing the correct hand. Higher quality micrographs of untilted specimens were processed to produce a reconstruction at 2.0-nm resolution with imposed 6-fold symmetry. The helical parameters of the sheath were determined to be 8.14 nm for the subunit rise along and 40.5° for the rotation angle around the helix. The sheath is similar to that of the T4 phage tail but with a different arrangement of the subdomain of the polymerizing sheath protein(s). The central tube is similar to the diameter and axial width of the Hcp1 hexamer of P. aeruginosa type VI secretion system. The tube extends through the baseplate into a needle resembling the "puncture device" of the T4 tail. The tube contains density that may be the toxin and/or a length-determining protein.

Indexed as

Bacterial Secretion SystemsBacteriophagesSerratiaBacterial Secretion SystemsBacterial PathogenesisBacteriophage Tail SheathCryo-electron MicroscopyElectron Microscopy (EM)Electron TomographyNegative Stain TomographySingle Particle AnalysisStructural Biology

Identifiers

PMID23857636
PMCPMC3757192
OpenAlexW2037319657

What OpenQuestion holds

Textmetadata
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.