Evidence map›Paper›PMID 26606672›Full record

ArticlePloS one2015

OmpW of Caulobacter crescentus Functions as an Outer Membrane Channel for Cations.

Roland Benz, Michael D Jones, Farhan Younas, Elke Maier, Niraj Modi, Reinhard Mentele, Friedrich Lottspeich, Ulrich Kleinekathöfer, John Smit

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

8 citing papers in PubMed, 19 citations in OpenAlex.

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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 4 institutions in 2 countries.

Roland BenzDepartment of Life Sciences and Chemistry, Jacobs University, Campus ring 1, 28759, Bremen, Germany.
Michael D JonesDepartment of Microbiology and Immunology, Life Sciences Centre, 2509-2350 Health Sciences Mall, University of British Columbia, Vancouver, British Columbia, V6T 1Z3, Canada.
Farhan YounasDepartment of Life Sciences and Chemistry, Jacobs University, Campus ring 1, 28759, Bremen, Germany.
Elke MaierRudolf-Virchow-Center, DFG-Research Center for Experimental Biomedicine, University of Würzburg, 97078, Würzburg, Germany.
Niraj ModiDepartment of Physics and Earth Sciences, Jacobs University, Campus ring 1, 28759, Bremen, Germany.
Reinhard MenteleMax-Planck Institute of Biochemistry, Department for Protein Analytics, Am Klopferspitz 18A, 82152, Martinsried, Germany.
Friedrich LottspeichMax-Planck Institute of Biochemistry, Department for Protein Analytics, Am Klopferspitz 18A, 82152, Martinsried, Germany.
Ulrich KleinekathöferDepartment of Physics and Earth Sciences, Jacobs University, Campus ring 1, 28759, Bremen, Germany.
John SmitDepartment of Microbiology and Immunology, Life Sciences Centre, 2509-2350 Health Sciences Mall, University of British Columbia, Vancouver, British Columbia, V6T 1Z3, Canada.
Constructor University · DEMax Planck Institute of Biochemistry · DEUniversity of British Columbia · CAUniversity of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Caulobacter crescentus is an oligotrophic bacterium that lives in dilute organic environments such as soil and freshwater. This bacterium represents an interesting model for cellular differentiation and regulation because daughter cells after division have different forms: one is motile while the other is non-motile and can adhere to surfaces. Interestingly, the known genome of C. crescentus does not contain genes predicted to code for outer membrane porins of the OmpF/C general diffusion type present in enteric bacteria or those coding for specific porins selective for classes of substrates. Instead, genes coding for 67 TonB-dependent outer membrane receptors have been identified, suggesting that active transport of specific nutrients may be the norm. Here, we report that high channel-forming activity was observed with crude outer membrane extracts of C. crescentus in lipid bilayer experiments, indicating that the outer membrane of C. crescentus contained an ion-permeable channel with a single-channel conductance of about 120 pS in 1M KCl. The channel-forming protein with an apparent molecular mass of about 20 kDa was purified to homogeneity. Partial protein sequencing of the protein indicated it was a member of the OmpW family of outer membrane proteins from Gram-negative bacteria. This channel was not observed in reconstitution experiments with crude outer membrane extracts of an OmpW deficient C. crescentus mutant. Biophysical analysis of the C. crescentus OmpW suggested that it has features that are special for general diffusion porins of Gram-negative outer membranes because it was not a wide aqueous channel. Furthermore, OmpW of C. crescentus seems to be different to known OmpW porins and has a preference for ions, in particular cations. A putative model for OmpW of C. crescentus was built on the basis of the known 3D-structures of OmpW of Escherichia coli and OprG of Pseudomonas aeruginosa using homology modeling. A comparison of the two known structures with the model of OmpW of C. crescentus suggested that it has a more hydrophilic interior and possibly a larger diameter.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsCationsCaulobacter crescentusGene Knockdown TechniquesIon ChannelsMutationBacterial Outer Membrane ProteinsCationsIon Channels

Identifiers

PMID26606672
PMCPMC4659666
OpenAlexW2179099740

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.