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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Auteurs principaux:	David Vela-Corcía, Diego Romero, Antonio de Vicente, Alejandro Pérez-García
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2018
Sujets:	Medicine R Science Q
Accès en ligne:	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
_version_	1718395650688679936

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

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