Alterations in EPSPS enzyme active site : Changes in position and reduced interaction energy contributing to glyphosate resistance in Amaranthus hybridus

Copyright © 2025 Elsevier Masson SAS. All rights reserved.

Détails bibliographiques
Publié dans:Plant physiology and biochemistry : PPB. - 1991. - 227(2025) vom: 01. Sept., Seite 110164
Auteur principal: Resende, Laís Sousa (Auteur)
Autres auteurs: Dos Reis, Gabriel Lasmar, Netto, Acácio Gonçalves, Borsato, Eliana Fernandes, Penckowski, Luís Henrique, Alvarenga, Joyce Pereira, Sales, Thais Aparecida, de Castro Ramalho, Teodorico, Christoffoleti, Pedro Jacob, Chalfun-Junior, Antonio
Format: Article en ligne
Langue:English
Publié: 2025
Accès à la collection:Plant physiology and biochemistry : PPB
Sujets:Journal Article Amaranthaceae Docking EPSPS triple mutation Number of EPSPS copies Glyphosate 4632WW1X5A Glycine TE7660XO1C 3-Phosphoshikimate 1-Carboxyvinyltransferase plus... EC 2.5.1.19 Herbicides Plant Proteins
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520 |a Glyphosate-resistant weeds are widespread in agricultural regions in the world, posing significant challenges to weed management and agricultural practices. Amaranthus hybridus, a common annual weed, has been detected in Argentina with a great glyphosate-resistant level. In Brazil, this species is also a prevalent weed, with glyphosate-resistant biotypes already identified in the southern region. Understanding the resistance mechanisms in these A. hybridus biotypes is essential to define effective management strategies and preventing further spread to other locations. This study aimed to characterize the resistance mechanisms related to the site of action of the EPSPS enzyme (5-enolpyruvylshikimate-3-phosphate synthase) in glyphosate-resistant A. hybridus biotypes from southern Brazil. Using molecular analysis and protein modeling techniques we characterized the resistance mechanisms in detail. Our results confirmed the presence of the triple mutation (TAP-IVS: T102I, A103V, and P106S) in the EPSPS enzyme, alongside an increase in copy number (2), elevated expression levels of the EPSPS gene in all resistant biotypes examined and the appearance of a new silent mutation. Additionally, the resistant biotypes were found to be heterozygous, indicating a recent mutation event. Theoretical studies of the enzyme structure revealed alterations in the position and interaction energy of amino acids with glyphosate, leading to a reduced active site cavity and destabilized interactions between glyphosate and the mutant EPSPS enzyme. These findings provide a deeper understanding of the molecular basis of glyphosate resistance in A. hybridus and highlight the need for adaptive management strategies 
650 4 |a Journal Article 
650 4 |a Amaranthaceae 
650 4 |a Docking 
650 4 |a EPSPS triple mutation 
650 4 |a Number of EPSPS copies 
650 7 |a Glyphosate  |2 NLM 
650 7 |a 4632WW1X5A  |2 NLM 
650 7 |a Glycine  |2 NLM 
650 7 |a TE7660XO1C  |2 NLM 
650 7 |a 3-Phosphoshikimate 1-Carboxyvinyltransferase  |2 NLM 
650 7 |a EC 2.5.1.19  |2 NLM 
650 7 |a Herbicides  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
700 1 |a Dos Reis, Gabriel Lasmar  |e verfasserin  |4 aut 
700 1 |a Netto, Acácio Gonçalves  |e verfasserin  |4 aut 
700 1 |a Borsato, Eliana Fernandes  |e verfasserin  |4 aut 
700 1 |a Penckowski, Luís Henrique  |e verfasserin  |4 aut 
700 1 |a Alvarenga, Joyce Pereira  |e verfasserin  |4 aut 
700 1 |a Sales, Thais Aparecida  |e verfasserin  |4 aut 
700 1 |a de Castro Ramalho, Teodorico  |e verfasserin  |4 aut 
700 1 |a Christoffoleti, Pedro Jacob  |e verfasserin  |4 aut 
700 1 |a Chalfun-Junior, Antonio  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Plant physiology and biochemistry : PPB  |d 1991  |g 227(2025) vom: 01. Sept., Seite 110164  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnas 
773 1 8 |g volume:227  |g year:2025  |g day:01  |g month:09  |g pages:110164 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2025.110164  |3 Volltext 
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