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Preliminary Study of Resistance Mechanism of Botrytis cinerea to SYAUP-CN-26

SYAUP-CN-26 (1S, 2R-((3-bromophenethyl)amino)-N-(4-chloro-2-trifluoromethylphenyl) cyclohexane-1-sulfonamide) is a novel sulfonamide compound with excellent activity against Botrytis cinerea. The present study sought to explore the mutant of B. cinerea resistant to SYAUP-CN-26 using SYAUP-CN-26 plat...

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Detalles Bibliográficos
Autores principales: Wang, Kai, Zhang, Huazhong, Zhu, Wanying, Peng, Jingnan, Li, Xinghai, Wang, Yingzi, Qi, Zhiqiu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8839620/
https://www.ncbi.nlm.nih.gov/pubmed/35164201
http://dx.doi.org/10.3390/molecules27030936
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author Wang, Kai
Zhang, Huazhong
Zhu, Wanying
Peng, Jingnan
Li, Xinghai
Wang, Yingzi
Qi, Zhiqiu
author_facet Wang, Kai
Zhang, Huazhong
Zhu, Wanying
Peng, Jingnan
Li, Xinghai
Wang, Yingzi
Qi, Zhiqiu
author_sort Wang, Kai
collection PubMed
description SYAUP-CN-26 (1S, 2R-((3-bromophenethyl)amino)-N-(4-chloro-2-trifluoromethylphenyl) cyclohexane-1-sulfonamide) is a novel sulfonamide compound with excellent activity against Botrytis cinerea. The present study sought to explore the mutant of B. cinerea resistant to SYAUP-CN-26 using SYAUP-CN-26 plates. Moreover, the cell membrane functions of B. cinerea, histidine kinase activity, relative conductivity, triglyceride, and cell membrane structure were determined, and the target gene histidine kinase Bos1 (AF396827.2) of procymidone was amplified and sequenced. The results showed that compared to the sensitive strain, the cell membrane permeability, triglyceride, and histidine kinase activity of the resistant strain showed significant changes. The relative conductivity of the sensitive strain increased by 6.95% and 9.61%, while the relative conductivity of the resistant strain increased by 0.23% and 1.76% with 26.785 µg/mL (EC(95)) and 79.754 µg/mL (MIC) of SYAUP-CN-26 treatment. The triglyceride inhibition rate of the resistant strain was 23.49% and 37.80%, which was 0.23% and 1.76% higher than the sensitive strain. Compared to the sensitive strain, the histidine kinase activity of the resistant strain was increased by 23.07% and 35.61%, respectively. SYAUP-CN-26 significantly damaged the cell membrane structure of the sensitive strain. The sequencing of the Bos1 gene of the sensitive and resistant strains indicated that SYAUP-CN-26 resistance was associated with a single point mutation (P348L) in the Bos1 gene. Therefore, it was inferred that the mutant of B. cinerea resistant to SYAUP-CN-26 might be regulated by the Bos1 gene. This study will provide a theoretical basis for further research and development of sulfonamide compounds for B. cinerea and new agents for the prevention and control of resistant B. cinerea.
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spelling pubmed-88396202022-02-13 Preliminary Study of Resistance Mechanism of Botrytis cinerea to SYAUP-CN-26 Wang, Kai Zhang, Huazhong Zhu, Wanying Peng, Jingnan Li, Xinghai Wang, Yingzi Qi, Zhiqiu Molecules Article SYAUP-CN-26 (1S, 2R-((3-bromophenethyl)amino)-N-(4-chloro-2-trifluoromethylphenyl) cyclohexane-1-sulfonamide) is a novel sulfonamide compound with excellent activity against Botrytis cinerea. The present study sought to explore the mutant of B. cinerea resistant to SYAUP-CN-26 using SYAUP-CN-26 plates. Moreover, the cell membrane functions of B. cinerea, histidine kinase activity, relative conductivity, triglyceride, and cell membrane structure were determined, and the target gene histidine kinase Bos1 (AF396827.2) of procymidone was amplified and sequenced. The results showed that compared to the sensitive strain, the cell membrane permeability, triglyceride, and histidine kinase activity of the resistant strain showed significant changes. The relative conductivity of the sensitive strain increased by 6.95% and 9.61%, while the relative conductivity of the resistant strain increased by 0.23% and 1.76% with 26.785 µg/mL (EC(95)) and 79.754 µg/mL (MIC) of SYAUP-CN-26 treatment. The triglyceride inhibition rate of the resistant strain was 23.49% and 37.80%, which was 0.23% and 1.76% higher than the sensitive strain. Compared to the sensitive strain, the histidine kinase activity of the resistant strain was increased by 23.07% and 35.61%, respectively. SYAUP-CN-26 significantly damaged the cell membrane structure of the sensitive strain. The sequencing of the Bos1 gene of the sensitive and resistant strains indicated that SYAUP-CN-26 resistance was associated with a single point mutation (P348L) in the Bos1 gene. Therefore, it was inferred that the mutant of B. cinerea resistant to SYAUP-CN-26 might be regulated by the Bos1 gene. This study will provide a theoretical basis for further research and development of sulfonamide compounds for B. cinerea and new agents for the prevention and control of resistant B. cinerea. MDPI 2022-01-29 /pmc/articles/PMC8839620/ /pubmed/35164201 http://dx.doi.org/10.3390/molecules27030936 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Wang, Kai
Zhang, Huazhong
Zhu, Wanying
Peng, Jingnan
Li, Xinghai
Wang, Yingzi
Qi, Zhiqiu
Preliminary Study of Resistance Mechanism of Botrytis cinerea to SYAUP-CN-26
title Preliminary Study of Resistance Mechanism of Botrytis cinerea to SYAUP-CN-26
title_full Preliminary Study of Resistance Mechanism of Botrytis cinerea to SYAUP-CN-26
title_fullStr Preliminary Study of Resistance Mechanism of Botrytis cinerea to SYAUP-CN-26
title_full_unstemmed Preliminary Study of Resistance Mechanism of Botrytis cinerea to SYAUP-CN-26
title_short Preliminary Study of Resistance Mechanism of Botrytis cinerea to SYAUP-CN-26
title_sort preliminary study of resistance mechanism of botrytis cinerea to syaup-cn-26
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8839620/
https://www.ncbi.nlm.nih.gov/pubmed/35164201
http://dx.doi.org/10.3390/molecules27030936
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