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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| Format: | Article |
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Nature Portfolio
2018-05-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-018-25336-5 |
| _version_ | 1818431459372826624 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-14T15:49:38Z |
| format | Article |
| id | doaj.art-729189f47e3149a6a20735532b1500dc |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-14T15:49:38Z |
| publishDate | 2018-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-729189f47e3149a6a20735532b1500dc2022-12-21T22:55:24ZengNature PortfolioScientific Reports2045-23222018-05-018111210.1038/s41598-018-25336-5Analysis of β-tubulin-carbendazim interaction reveals that binding site for MBC fungicides does not include residues involved in fungicide resistanceDavid Vela-Corcía0Diego Romero1Antonio de Vicente2Alejandro Pérez-García3Instituto de Hortofruticultura Subtropical y Mediterránea “La Mayora”, Universidad de Málaga-Consejo Superior de Investigaciones Científicas (IHSM-UMA-CSIC), Departamento de Microbiología, Universidad de MálagaInstituto de Hortofruticultura Subtropical y Mediterránea “La Mayora”, Universidad de Málaga-Consejo Superior de Investigaciones Científicas (IHSM-UMA-CSIC), Departamento de Microbiología, Universidad de MálagaInstituto de Hortofruticultura Subtropical y Mediterránea “La Mayora”, Universidad de Málaga-Consejo Superior de Investigaciones Científicas (IHSM-UMA-CSIC), Departamento de Microbiología, Universidad de MálagaInstituto de Hortofruticultura Subtropical y Mediterránea “La Mayora”, Universidad de Málaga-Consejo Superior de Investigaciones Científicas (IHSM-UMA-CSIC), Departamento de Microbiología, Universidad de MálagaAbstract 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.https://doi.org/10.1038/s41598-018-25336-5 |
| spellingShingle | 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 Scientific Reports |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s41598-018-25336-5 |
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