ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2019
Novel compounds that specifically bind and modulate MscL: insights into channel gating mechanisms.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Non-Equilibrium Molecular Dynamics Simulation Captures Potential New Drug Target: Ec-MscL Gating Mechanism Explored with External Electric Field.Antibiotics (Basel, Switzerland) · 2026Article
- The efficacy of the food-grade antimicrobial xanthorrhizol againstFrontiers in microbiology · 2024Article
- Approaches for the modulation of mechanosensitive MscL channel pores.Frontiers in chemistry · 2023Review
- Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope.Advances in microbial physiology · 2023Article
- Genetic and cellular characterization of MscS-like putative channels in the filamentous fungusChannels (Austin, Tex.) · 2022Article
- Activation of a Bacterial Mechanosensitive Channel, MscL, Underlies the Membrane Permeabilization of Dual-Targeting Antibacterial Compounds.Antibiotics (Basel, Switzerland) · 2022Article
- Roles of Bacterial Mechanosensitive Channels in Infection and Antibiotic Susceptibility.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state.Structure (London, England : 1993) · 2022Article
- In Silico Screen Identifies a New Family of Agonists for the Bacterial Mechanosensitive Channel MscL.Antibiotics (Basel, Switzerland) · 2022Article
- Mechanosensitive Channels Mediate Hypoionic Shock-Induced Aminoglycoside Potentiation against Bacterial Persisters by Enhancing Antibiotic Uptake.Antimicrobial agents and chemotherapy · 2022Article
- Curcumin activation of a bacterial mechanosensitive channel underlies its membrane permeability and adjuvant properties.PLoS pathogens · 2021Article
- Life with Bacterial Mechanosensitive Channels, from Discovery to Physiology to Pharmacological Target.Microbiology and molecular biology reviews : MMBR · 2020Review
- Novel MscL agonists that allow multiple antibiotics cytoplasmic access activate the channel through a common binding site.PloS one · 2020Article
- An agonist of the MscL channel affects multiple bacterial species and increases membrane permeability and potency of common antibiotics.Molecular microbiology · 2019Article
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5 authors.
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Abstract
The bacterial mechanosensitive channel of large conductance (MscL) normally functions as an emergency release valve discharging cytoplasmic solutes upon osmotic stress. Opening the large pore of MscL inappropriately is detrimental to the cell, and thus it has been speculated to be a potential antibiotic target. Although MscL is one of the best studied mechanosensitive channels, no chemical that influenced bacterial growth by modulating MscL is known. We therefore used a high-throughput screen to identify compounds that slowed growth in an MscL-dependent manner. We characterized 2 novel sulfonamide compounds identified in the screen. We demonstrated that, although both increase MscL gating, one of these compounds does not work through the folate pathway, as other antimicrobial sulfonamides; indeed, the sulfonamide portion of the compound is not needed for activity. The only mode of action appears to be MscL activation. The binding pocket is where an α-helix runs along the cytoplasmic membrane and interacts with a neighboring subunit; analogous motifs have been observed in several prokaryotic and eukaryotic channels. The data not only demonstrate that MscL is a viable antibiotic target, but also give insight into the gating mechanisms of MscL, and they may have implications for developing agonists for other channels.-Wray, R., Iscla, I., Kovacs, Z., Wang, J., Blount, P. Novel compounds that specifically bind and modulate MscL: insights into channel gating mechanisms.
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