Evidence map›Paper›PMID 15465872›Full record

ArticleBiophysical journal2004

Colicin occlusion of OmpF and TolC channels: outer membrane translocons for colicin import.

Stanislav D Zakharov, Veronika Y Eroukova, Tatyana I Rokitskaya, Mariya V Zhalnina, Onkar Sharma, Patrick J Loll, Helen I Zgurskaya, Yuri N Antonenko, William A Cramer

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

44 citing papers in PubMed, 82 citations in OpenAlex.

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  15. Multiple Osmotic Stress Responses inFrontiers in microbiology · 2016
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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

9 authors at 5 institutions in 2 countries.

Stanislav D ZakharovDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana, USA. zakharos@purdue.edu
Veronika Y Eroukova
Tatyana I Rokitskaya
Mariya V Zhalnina
Onkar Sharma
Patrick J Loll
Helen I Zgurskaya
Yuri N Antonenko
William A Cramer
Lomonosov Moscow State University · RUPurdue University West Lafayette · USDrexel University · USInstitute of Basic Biological Problems · RUUniversity of Oklahoma · US

Funding

Transport across two membranes by AcrAB-TolC complexR01AI052293 · NIAID · UNIVERSITY OF OKLAHOMA NORMAN · PI ZGURSKAYA, HELEN I · 2003 to 2024
$7.7M
THE MECHANISM OF ACTION OF COLICIN E1R01GM018457 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI CRAMER, WILLIAM A. · 1985 to 2007
$2.2M
Voltage-Gated Insertion of Colicin into Planar BilayersR03TW001235 · FIC · PURDUE UNIVERSITY WEST LAFAYETTE · PI CRAMER, WILLIAM A. · 2000 to 2005
$222k
FIC NIH HHS R03 TW001235NIAID NIH HHS R01 AI052293NIGMS NIH HHS R01 GM018457
6 · The paper itself

Abstract

The interaction of colicins with target cells is a paradigm for protein import. To enter cells, bactericidal colicins parasitize Escherichia coli outer membrane receptors whose physiological purpose is the import of essential metabolites. Colicins E1 and E3 initially bind to the BtuB receptor, whose beta-barrel pore is occluded by an N-terminal globular "plug". The x-ray structure of a complex of BtuB with the coiled-coil BtuB-binding domain of colicin E3 did not reveal displacement of the BtuB plug that would allow passage of the colicin (Kurisu, G., S. D. Zakharov, M. V. Zhalnina, S. Bano, V. Y. Eroukova, T. I. Rokitskaya, Y. N. Antonenko, M. C. Wiener, and W. A. Cramer. 2003. Nat. Struct. Biol. 10:948-954). This correlates with the inability of BtuB to form ion channels in planar bilayers, shown in this work, suggesting that an additional outer membrane protein(s) is required for colicin import across the outer membrane. The identity and interaction properties of this OMP were analyzed in planar bilayer experiments.OmpF and TolC channels in planar bilayers were occluded by colicins E3 and E1, respectively, from the trans-side of the membrane. Occlusion was dependent upon a cis-negative transmembrane potential. A positive potential reversibly opened OmpF and TolC channels. Colicin N, which uses only OmpF for entry, occludes OmpF in planar bilayers with the same orientation constraints as colicins E1 and E3. The OmpF recognition sites of colicins E3 and N, and the TolC recognition site of colicin E1, were found to reside in the N-terminal translocation domains. These data are considered in the context of a two-receptor translocon model for colicin entry into cells.

Indexed as

Ion Channel GatingProtein TransportBacterial Outer Membrane ProteinsColicinsDiffusionEscherichia coli ProteinsLipid BilayersMembranes, ArtificialMembrane Transport ProteinsPorinsProtein BindingReceptors, PeptideBacterial Outer Membrane ProteinsBtuB protein, E coliColicinsEscherichia coli ProteinsLipid BilayersMembranes, ArtificialMembrane Transport ProteinsOmpF proteinPorinsReceptors, PeptidetolC protein, E coli

Identifiers

PMID15465872
PMCPMC1304901
OpenAlexW2027790619

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.