Evidence map›Paper›PMID 27280286›Full record

ArticlePLoS biology2016

Dihydrostreptomycin Directly Binds to, Modulates, and Passes through the MscL Channel Pore.

Robin Wray, Irene Iscla, Ya Gao, Hua Li, Junmei Wang, Paul Blount

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

29 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
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  7. Sonogenetics in the Treatment of Chronic Diseases: A New Method for Cell Regulation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
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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

6 authors at 2 institutions in 2 countries.

Robin WrayDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas, United States of America.
Irene IsclaDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas, United States of America.
Ya GaoSchool of Pharmacy, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Hua LiSchool of Pharmacy, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Junmei WangGreen Center for Systems Biology and Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, United States of America.
Paul BlountDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas, United States of America.
The University of Texas Southwestern Medical Center · USHuazhong University of Science and Technology · CN

Funding

MOLECULAR MECHANISMS OF MECHANOSENSITIVE CHANNEL GATINGR01GM061028 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI BLOUNT, PAUL · 2000 to 2017
$4.7M
NIGMS NIH HHS R01 GM061028
6 · The paper itself

Abstract

The primary mechanism of action of the antibiotic dihydrostreptomycin is binding to and modifying the function of the bacterial ribosome, thus leading to decreased and aberrant translation of proteins; however, the routes by which it enters the bacterial cell are largely unknown. The mechanosensitive channel of large conductance, MscL, is found in the vast majority of bacterial species, where it serves as an emergency release valve rescuing the cell from sudden decreases in external osmolarity. While it is known that MscL expression increases the potency of dihydrostreptomycin, it has remained unclear if this effect is due to a direct interaction. Here, we use a combination of genetic screening, MD simulations, and biochemical and mutational approaches to determine if dihydrostreptomycin directly interacts with MscL. Our data strongly suggest that dihydrostreptomycin binds to a specific site on MscL and modifies its conformation, thus allowing the passage of K+ and glutamate out of, and dihydrostreptomycin into, the cell.

Indexed as

Anti-Bacterial AgentsBinding SitesCell MembraneCysteineDihydrostreptomycin SulfateEscherichia coliEscherichia coli ProteinsGlutamic AcidIon Channel GatingIon ChannelsMechanoreceptorsMolecular Docking SimulationMolecular Dynamics SimulationMutationPotassiumProtein BindingAnti-Bacterial AgentsCysteineDihydrostreptomycin SulfateEscherichia coli ProteinsGlutamic AcidIon ChannelsMscL protein, E coliPotassium

Identifiers

PMID27280286
PMCPMC4900634
OpenAlexW2418802224

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.