Analysis of β-tubulin-carbendazim interaction reveals that binding site for MBC fungicides does not include residues involved in fungicide resistance

Abstract Methyl benzimidazole carbamate (MBC) fungicides are fungicidal compounds that exert their biological activities by preventing cell division through the inhibition of tubulin polymerization, which is the major component of microtubules. Several mutations in the β-tubulin gene contribute to M...

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Autores principales: David Vela-Corcía, Diego Romero, Antonio de Vicente, Alejandro Pérez-García
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Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/729189f47e3149a6a20735532b1500dc
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spelling oai:doaj.org-article:729189f47e3149a6a20735532b1500dc2021-12-02T11:40:25ZAnalysis of β-tubulin-carbendazim interaction reveals that binding site for MBC fungicides does not include residues involved in fungicide resistance10.1038/s41598-018-25336-52045-2322https://doaj.org/article/729189f47e3149a6a20735532b1500dc2018-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-25336-5https://doaj.org/toc/2045-2322Abstract Methyl benzimidazole carbamate (MBC) fungicides are fungicidal compounds that exert their biological activities by preventing cell division through the inhibition of tubulin polymerization, which is the major component of microtubules. Several mutations in the β-tubulin gene contribute to MBC resistance, the most common and significant of which occur at residues 198 and 200. Despite nearly 50 years of agricultural use, the binding site of MBCs and the precise mechanism by which those mutations affect fungicide efficacy have not been determined. The aim of this work was to clarify the mode of action and the mechanism of resistance to MBC fungicides in Podosphaera xanthii, the primary causal agent of cucurbit powdery mildew, using a combination of biochemical, biophysical and computational approaches. The results allow us to propose an MBC binding site in β-tubulin that lies close to the GTP binding site and does not include residue 198 involved in MBC resistance.David Vela-CorcíaDiego RomeroAntonio de VicenteAlejandro Pérez-GarcíaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-12 (2018)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
David Vela-Corcía
Diego Romero
Antonio de Vicente
Alejandro Pérez-García
Analysis of β-tubulin-carbendazim interaction reveals that binding site for MBC fungicides does not include residues involved in fungicide resistance
description Abstract Methyl benzimidazole carbamate (MBC) fungicides are fungicidal compounds that exert their biological activities by preventing cell division through the inhibition of tubulin polymerization, which is the major component of microtubules. Several mutations in the β-tubulin gene contribute to MBC resistance, the most common and significant of which occur at residues 198 and 200. Despite nearly 50 years of agricultural use, the binding site of MBCs and the precise mechanism by which those mutations affect fungicide efficacy have not been determined. The aim of this work was to clarify the mode of action and the mechanism of resistance to MBC fungicides in Podosphaera xanthii, the primary causal agent of cucurbit powdery mildew, using a combination of biochemical, biophysical and computational approaches. The results allow us to propose an MBC binding site in β-tubulin that lies close to the GTP binding site and does not include residue 198 involved in MBC resistance.
format article
author David Vela-Corcía
Diego Romero
Antonio de Vicente
Alejandro Pérez-García
author_facet David Vela-Corcía
Diego Romero
Antonio de Vicente
Alejandro Pérez-García
author_sort David Vela-Corcía
title Analysis of β-tubulin-carbendazim interaction reveals that binding site for MBC fungicides does not include residues involved in fungicide resistance
title_short Analysis of β-tubulin-carbendazim interaction reveals that binding site for MBC fungicides does not include residues involved in fungicide resistance
title_full Analysis of β-tubulin-carbendazim interaction reveals that binding site for MBC fungicides does not include residues involved in fungicide resistance
title_fullStr Analysis of β-tubulin-carbendazim interaction reveals that binding site for MBC fungicides does not include residues involved in fungicide resistance
title_full_unstemmed Analysis of β-tubulin-carbendazim interaction reveals that binding site for MBC fungicides does not include residues involved in fungicide resistance
title_sort analysis of β-tubulin-carbendazim interaction reveals that binding site for mbc fungicides does not include residues involved in fungicide resistance
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/729189f47e3149a6a20735532b1500dc
work_keys_str_mv AT davidvelacorcia analysisofbtubulincarbendaziminteractionrevealsthatbindingsiteformbcfungicidesdoesnotincluderesiduesinvolvedinfungicideresistance
AT diegoromero analysisofbtubulincarbendaziminteractionrevealsthatbindingsiteformbcfungicidesdoesnotincluderesiduesinvolvedinfungicideresistance
AT antoniodevicente analysisofbtubulincarbendaziminteractionrevealsthatbindingsiteformbcfungicidesdoesnotincluderesiduesinvolvedinfungicideresistance
AT alejandroperezgarcia analysisofbtubulincarbendaziminteractionrevealsthatbindingsiteformbcfungicidesdoesnotincluderesiduesinvolvedinfungicideresistance
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