Evidence map›Paper›PMID 25723169›Full record

ArticleCell2015

Structure of the type VI secretion system contractile sheath.

Mikhail Kudryashev, Ray Yu-Ruei Wang, Maximilian Brackmann, Sebastian Scherer, Timm Maier, David Baker, Frank DiMaio, Henning Stahlberg, Edward H Egelman, Marek Basler

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.

0numbers the graph read from it
0cells of the map it votes in
152citing papers in PubMed
27.9field-weighted citation impact, top 1% 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

152 citing papers in PubMed, 246 citations in OpenAlex.

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  18. Science advances · 2025
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92 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

10 authors at 2 institutions in 2 countries.

Mikhail KudryashevFocal Area Infection Biology, Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland; Center for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, Mattenstrasse 26, CH-4058 Basel, Switzerland.
Ray Yu-Ruei WangDepartment of Biochemistry, University of Washington, 1705 NE Pacific Street, Seattle, WA 98195, USA; Graduate Program in Biological Physics, Structure and Design, University of Washington, Box 357350, Seattle, WA 98195, USA.
Maximilian BrackmannFocal Area Infection Biology, Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland.
Sebastian SchererCenter for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, Mattenstrasse 26, CH-4058 Basel, Switzerland.
Timm MaierFocal Area Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland.
David BakerDepartment of Biochemistry, University of Washington, 1705 NE Pacific Street, Seattle, WA 98195, USA.
Frank DiMaioDepartment of Biochemistry, University of Washington, 1705 NE Pacific Street, Seattle, WA 98195, USA.
Henning StahlbergCenter for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, Mattenstrasse 26, CH-4058 Basel, Switzerland.
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908, USA. Electronic address: egelman@virginia.edu.
Marek BaslerFocal Area Infection Biology, Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland. Electronic address: marek.basler@unibas.ch.
University of Basel · CHUniversity of Washington · US

Funding

Methods for the Analysis of Helical Macromolecular ComplexesR01EB001567 · NIBIB · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI EGELMAN, EDWARD H. · 2003 to 2014
$3.6M
High resolution structure modeling with RosettaR01GM092802 · NIGMS · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID · 2010 to 2017
$2.3M
NIBIB NIH HHS EB001567NIBIB NIH HHS R01 EB001567NIGMS NIH HHS R01 GM092802NIGMS NIH HHS R01GM092802
6 · The paper itself

Abstract

Bacteria use rapid contraction of a long sheath of the type VI secretion system (T6SS) to deliver effectors into a target cell. Here, we present an atomic-resolution structure of a native contracted Vibrio cholerae sheath determined by cryo-electron microscopy. The sheath subunits, composed of tightly interacting proteins VipA and VipB, assemble into a six-start helix. The helix is stabilized by a core domain assembled from four β strands donated by one VipA and two VipB molecules. The fold of inner and middle layers is conserved between T6SS and phage sheaths. However, the structure of the outer layer is distinct and suggests a mechanism of interaction of the bacterial sheath with an accessory ATPase, ClpV, that facilitates multiple rounds of effector delivery. Our results provide a mechanistic insight into assembly of contractile nanomachines that bacteria and phages use to translocate macromolecules across membranes.

Indexed as

Bacterial Secretion SystemsAmino Acid SequenceBacterial ProteinsCryoelectron MicroscopyModels, MolecularMolecular Sequence DataSequence AlignmentVibrio choleraeBacterial ProteinsBacterial Secretion Systems

Identifiers

PMID25723169
PMCPMC4359589
OpenAlexW2040721088

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.