Evidence map›Paper›PMID 23797422›Full record

ArticleThe Journal of general physiology2013

The mechanoelectrical response of the cytoplasmic membrane of Vibrio cholerae.

Ian Rowe, Merina Elahi, Anwar Huq, Sergei Sukharev

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Cyclodextrins increase membrane tension and are universal activators of mechanosensitive channels.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

4 authors at 1 institution in 1 country.

Ian RoweDepartment of Biology, Maryland Pathogen Institute, University of Maryland, College Park, MD 20742, USA.
Merina Elahi
Anwar Huq
Sergei Sukharev
University of Maryland, College Park · US

Funding

The bacterial mechanosentitive channel as a multimodal sensor deviceR01GM107652 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI ANISHKIN, ANDRIY, SINTIM, HERMAN O · 2013 to 2016
$1.1M
The electrophysiology of facultative pathogensR21AI105655 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI HUQ, ANWAR, SUKHAREV, SERGEI I · 2013 to 2014
$357k
NIAID NIH HHS R21 AI105655NIAID NIH HHS R21 AI105655-01NIGMS NIH HHS R01 GM107652PHS HHS R01 A1039129-11A2
6 · The paper itself

Abstract

Persistence of Vibrio cholerae in waters of fluctuating salinity relies on the capacity of this facultative enteric pathogen to adapt to varying osmotic conditions. In an event of osmotic downshift, osmolytes accumulated inside the bacterium can be quickly released through tension-activated channels. With the newly established procedure of giant spheroplast preparation from V. cholerae, we performed the first patch-clamp characterization of its cytoplasmic membrane and compared tension-activated currents with those in Esherichia coli. Saturating pressure ramps revealed two waves of activation belonging to the ∼1-nS mechanosensitive channel of small conductance (MscS)-like channels and ∼3-nS mechanosensitive channel of large conductance (MscL)-like channels, with a pressure midpoint ratio p0.5MscS/p0.5MscL of 0.48. We found that MscL-like channels in V. cholerae present at a density three times higher than in E. coli, and yet, these vibrios were less tolerant to large osmotic downshocks. The Vibrio MscS-like channels exhibit characteristic inward rectification and subconductive states at depolarizing voltages; they also adapt and inactivate at subsaturating tensions and recover within 2 s upon tension release, just like E. coli MscS. Trehalose, a compatible internal osmolyte accumulated under hypertonic conditions, significantly shifts activation curves of both MscL- and MscS-like channels toward higher tensions, yet does not freely partition into the channel pore. Direct electrophysiology of V. cholerae offers new avenues for the in situ analysis of membrane components critical for osmotic survival and electrogenic transport in this pathogen.

Indexed as

Action PotentialsMechanotransduction, CellularCell MembraneEscherichia coliEscherichia coli ProteinsIon ChannelsOsmotic PressurePressureSpheroplastsVibrio choleraeEscherichia coli ProteinsIon ChannelsMscL protein, E coliMscS protein, E coli

Identifiers

PMID23797422
PMCPMC3691451
OpenAlexW2101087347

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.