Evidence map›Paper›PMID 35567623›Full record

ArticleEuropean biophysics journal : EBJ2022

Cell wall channels of Rhodococcus species: identification and characterization of the cell wall channels of Rhodococcus corynebacteroides and Rhodococcus ruber.

Claudio Piselli, Lorraine Benier, Cornelia Koy, Michael O Glocker, Roland Benz

Open access · hybridAbstract read
In one paragraph

Article in European biophysics journal : EBJ, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 48% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Review
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

5 authors at 2 institutions in 1 country.

Claudio PiselliJacobs University Bremen, Campusring 1, 28759, Bremen, Germany.
Lorraine BenierJacobs University Bremen, Campusring 1, 28759, Bremen, Germany.
Cornelia KoyProteome Center Rostock, University Medicine Rostock, 18059, Rostock, Germany.
Michael O GlockerProteome Center Rostock, University Medicine Rostock, 18059, Rostock, Germany.
Roland BenzJacobs University Bremen, Campusring 1, 28759, Bremen, Germany. r.benz@jacobs-university.de.ORCID http://orcid.org/0000-0002-9510-9265
Constructor University · DEUniversity of Rostock · DE

Funding

Deutsche Forschungsgemeinschaft Be 865/16-2
6 · The paper itself

Abstract

The cell wall of Rhodococcus corynebacteroides formerly known as Nocardia corynebacteroides contains cell wall channels that are responsible for the cell wall permeability of this bacterium. Based on partial sequencing of the polypeptide subunits and a BLAST search, we identified one polypeptide of R. corynebacteroides (PorARc) and two polypeptides (PorARr and PorBRr) from the closely related bacterium Rhodococcus ruber. The corresponding genes, porARc (606 bp), porARr (702 bp), and porBRr (540 bp) are constituents of the known genome of R. corynebacteroides DSM-20151 and R. ruber DSM-43338, respectively. porARr and porBRr of R. ruber are possibly forming a common operon coding for the polypeptide subunits of the cell wall channel. The genes coding for PorARc and for PorARr and PorBRr without signal peptide were separately expressed in the porin-deficient Escherichia coli BL21DE3Omp8 strain and the proteins were purified to homogeneity. All proteins were checked for channel formation in lipid bilayers. PorARc formed channels with characteristics that were very similar to those of a previous study. The proteins PorARr and PorBRr expressed in E. coli could alone create channels in lipid bilayer membranes, despite the possibility that the two corresponding genes form a porin operon and that both subunits possibly form the cell wall channels in vivo. Based on amino acid sequence comparison of a variety of proteins forming cell wall channels in bacteria of the suborder Corynebacterineae, it seems very likely that PorARc, PorARr, and PorBRr are members of a huge family of proteins (PF09203) that form MspA-like cell wall channels.

Indexed as

Escherichia coliRhodococcusCell WallLipid BilayersPeptidesPorinsLipid BilayersPeptidesPorinsCell wall channelChannel formationLipid bilayer membraneOctamerRhodococcus corynebacteroidesRhodococcus ruber

Identifiers

PMID35567623
PMCPMC9233653
OpenAlexW4280514443

What OpenQuestion holds

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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.