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Inhibition profile of trifludimoxazin towards PPO2 target site mutations

BACKGROUND: Target site resistance to herbicides that inhibit protoporphyrinogen IX oxidase (PPO; EC 1.3.3.4) has been described mainly in broadleaf weeds based on mutations in the gene designated protoporphyrinogen oxidase 2 (PPO2) and in one monocot weed species in protoporphyrinogen oxidase 1 (PP...

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Autores principales: Porri, Aimone, Betz, Michael, Seebruck, Kathryn, Knapp, Michael, Johnen, Philipp, Witschel, Matthias, Aponte, Raphael, Liebl, Rex, Tranel, Patrick J., Lerchl, Jens
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Ltd. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10092844/
https://www.ncbi.nlm.nih.gov/pubmed/36178376
http://dx.doi.org/10.1002/ps.7216
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author Porri, Aimone
Betz, Michael
Seebruck, Kathryn
Knapp, Michael
Johnen, Philipp
Witschel, Matthias
Aponte, Raphael
Liebl, Rex
Tranel, Patrick J.
Lerchl, Jens
author_facet Porri, Aimone
Betz, Michael
Seebruck, Kathryn
Knapp, Michael
Johnen, Philipp
Witschel, Matthias
Aponte, Raphael
Liebl, Rex
Tranel, Patrick J.
Lerchl, Jens
author_sort Porri, Aimone
collection PubMed
description BACKGROUND: Target site resistance to herbicides that inhibit protoporphyrinogen IX oxidase (PPO; EC 1.3.3.4) has been described mainly in broadleaf weeds based on mutations in the gene designated protoporphyrinogen oxidase 2 (PPO2) and in one monocot weed species in protoporphyrinogen oxidase 1 (PPO1). To control PPO target site resistant weeds in future it is important to design new PPO‐inhibiting herbicides that can control problematic weeds expressing mutant PPO enzymes. In this study, we assessed the efficacy of a new triazinone‐type inhibitor, trifludimoxazin, to inhibit PPO2 enzymes carrying target site mutations in comparison with three widely used PPO‐inhibiting herbicides. RESULTS: Mutated Amaranthus spp. PPO2 enzymes were expressed in Escherichia coli, purified and measured biochemically for activity and inhibition kinetics, and used for complementation experiments in an E. coli hemG mutant that lacks the corresponding microbial PPO gene function. In addition, we used ectopic expression in Arabidopsis and structural PPO protein modeling to support the enzyme inhibition study. The generated data strongly suggest that trifludimoxazin is a strong inhibitor both at the enzyme level and in transgenics Arabidopsis ectopically expressing PPO2 target site mutations. CONCLUSION: Trifludimoxazin is a potent PPO‐inhibiting herbicide that inhibits various PPO2 enzymes carrying target site mutations and could be used as a chemical‐based control strategy to mitigate the widespread occurrence of PPO target site resistance as well as weeds that have evolved resistance to other herbicide mode of actions. © 2022 BASF SE and The Authors. Pest Management Science published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.
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spelling pubmed-100928442023-04-13 Inhibition profile of trifludimoxazin towards PPO2 target site mutations Porri, Aimone Betz, Michael Seebruck, Kathryn Knapp, Michael Johnen, Philipp Witschel, Matthias Aponte, Raphael Liebl, Rex Tranel, Patrick J. Lerchl, Jens Pest Manag Sci Research Articles BACKGROUND: Target site resistance to herbicides that inhibit protoporphyrinogen IX oxidase (PPO; EC 1.3.3.4) has been described mainly in broadleaf weeds based on mutations in the gene designated protoporphyrinogen oxidase 2 (PPO2) and in one monocot weed species in protoporphyrinogen oxidase 1 (PPO1). To control PPO target site resistant weeds in future it is important to design new PPO‐inhibiting herbicides that can control problematic weeds expressing mutant PPO enzymes. In this study, we assessed the efficacy of a new triazinone‐type inhibitor, trifludimoxazin, to inhibit PPO2 enzymes carrying target site mutations in comparison with three widely used PPO‐inhibiting herbicides. RESULTS: Mutated Amaranthus spp. PPO2 enzymes were expressed in Escherichia coli, purified and measured biochemically for activity and inhibition kinetics, and used for complementation experiments in an E. coli hemG mutant that lacks the corresponding microbial PPO gene function. In addition, we used ectopic expression in Arabidopsis and structural PPO protein modeling to support the enzyme inhibition study. The generated data strongly suggest that trifludimoxazin is a strong inhibitor both at the enzyme level and in transgenics Arabidopsis ectopically expressing PPO2 target site mutations. CONCLUSION: Trifludimoxazin is a potent PPO‐inhibiting herbicide that inhibits various PPO2 enzymes carrying target site mutations and could be used as a chemical‐based control strategy to mitigate the widespread occurrence of PPO target site resistance as well as weeds that have evolved resistance to other herbicide mode of actions. © 2022 BASF SE and The Authors. Pest Management Science published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry. John Wiley & Sons, Ltd. 2022-10-17 2023-02 /pmc/articles/PMC10092844/ /pubmed/36178376 http://dx.doi.org/10.1002/ps.7216 Text en © 2022 BASF SE and The Authors. Pest Management Science published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Porri, Aimone
Betz, Michael
Seebruck, Kathryn
Knapp, Michael
Johnen, Philipp
Witschel, Matthias
Aponte, Raphael
Liebl, Rex
Tranel, Patrick J.
Lerchl, Jens
Inhibition profile of trifludimoxazin towards PPO2 target site mutations
title Inhibition profile of trifludimoxazin towards PPO2 target site mutations
title_full Inhibition profile of trifludimoxazin towards PPO2 target site mutations
title_fullStr Inhibition profile of trifludimoxazin towards PPO2 target site mutations
title_full_unstemmed Inhibition profile of trifludimoxazin towards PPO2 target site mutations
title_short Inhibition profile of trifludimoxazin towards PPO2 target site mutations
title_sort inhibition profile of trifludimoxazin towards ppo2 target site mutations
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10092844/
https://www.ncbi.nlm.nih.gov/pubmed/36178376
http://dx.doi.org/10.1002/ps.7216
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