Relationship between acaricide resistance and acetylcholinesterase gene polymorphisms in the cattle tick Rhipicephalus microplus

In this study, we aimed to develop a comprehensive methodology for identifying amino acid polymorphisms in acetylcholinesterase transcript 2 (AChE2) in acaricide-resistant Rhipicephalus microplus ticks. This included assessing AChE2 expression levels through qPCR and conducting 3D modeling to evalua...

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Main Authors: Cossio-Bayugar Raquel, Martinez-Ibañez Francisco, Aguilar-Diaz Hugo, Miranda-Miranda Estefan
Format: Article
Language:English
Published: EDP Sciences 2024-01-01
Series:Parasite
Subjects:
Online Access:https://www.parasite-journal.org/articles/parasite/full_html/2024/01/parasite230118/parasite230118.html
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author Cossio-Bayugar Raquel
Martinez-Ibañez Francisco
Aguilar-Diaz Hugo
Miranda-Miranda Estefan
author_facet Cossio-Bayugar Raquel
Martinez-Ibañez Francisco
Aguilar-Diaz Hugo
Miranda-Miranda Estefan
author_sort Cossio-Bayugar Raquel
collection DOAJ
description In this study, we aimed to develop a comprehensive methodology for identifying amino acid polymorphisms in acetylcholinesterase transcript 2 (AChE2) in acaricide-resistant Rhipicephalus microplus ticks. This included assessing AChE2 expression levels through qPCR and conducting 3D modeling to evaluate the interaction between acaricides and AChE2 using docking techniques. The study produced significant results, demonstrating that acaricide-resistant R. microplus ticks exhibit significantly higher levels of AChE expression than susceptible reference ticks. In terms of amino acid sequence, we identified 9 radical amino acid substitutions in AChE2 from acaricide-resistant ticks, when compared to the gene sequence of the susceptible reference strain. To further understand the implications of these substitutions, we utilized 3D acaricide-AChE2 docking modeling to examine the interaction between the acaricide and the AChE2 catalytic site. Our models suggest that these amino acid polymorphisms alter the configuration of the binding pocket, thereby contributing to differences in acaricide interactions and ultimately providing insights into the acaricide-resistance phenomenon in R. microplus.
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spelling doaj.art-a40787a87cb1474c885cfce5ce3e47b82024-02-13T08:35:18ZengEDP SciencesParasite1776-10422024-01-0131310.1051/parasite/2024003parasite230118Relationship between acaricide resistance and acetylcholinesterase gene polymorphisms in the cattle tick Rhipicephalus microplusCossio-Bayugar Raquel0https://orcid.org/0000-0003-3681-2492Martinez-Ibañez Francisco1https://orcid.org/0000-0003-0422-3482Aguilar-Diaz Hugo2https://orcid.org/0000-0002-6497-6462Miranda-Miranda Estefan3https://orcid.org/0000-0002-0464-3666Centro Nacional de Investigación Disciplinaria en Salud Animal e Inocuidad, Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias INIFAPDepartamento de Ectoparásitos y Dípteros. Servicio Nacional de Sanidad, Inocuidad y Calidad Agroalimentaria SADERCentro Nacional de Investigación Disciplinaria en Salud Animal e Inocuidad, Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias INIFAPCentro Nacional de Investigación Disciplinaria en Salud Animal e Inocuidad, Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias INIFAPIn this study, we aimed to develop a comprehensive methodology for identifying amino acid polymorphisms in acetylcholinesterase transcript 2 (AChE2) in acaricide-resistant Rhipicephalus microplus ticks. This included assessing AChE2 expression levels through qPCR and conducting 3D modeling to evaluate the interaction between acaricides and AChE2 using docking techniques. The study produced significant results, demonstrating that acaricide-resistant R. microplus ticks exhibit significantly higher levels of AChE expression than susceptible reference ticks. In terms of amino acid sequence, we identified 9 radical amino acid substitutions in AChE2 from acaricide-resistant ticks, when compared to the gene sequence of the susceptible reference strain. To further understand the implications of these substitutions, we utilized 3D acaricide-AChE2 docking modeling to examine the interaction between the acaricide and the AChE2 catalytic site. Our models suggest that these amino acid polymorphisms alter the configuration of the binding pocket, thereby contributing to differences in acaricide interactions and ultimately providing insights into the acaricide-resistance phenomenon in R. microplus.https://www.parasite-journal.org/articles/parasite/full_html/2024/01/parasite230118/parasite230118.htmlrt-pcrprotein 3d modelingpesticide-resistancecattle tick
spellingShingle Cossio-Bayugar Raquel
Martinez-Ibañez Francisco
Aguilar-Diaz Hugo
Miranda-Miranda Estefan
Relationship between acaricide resistance and acetylcholinesterase gene polymorphisms in the cattle tick Rhipicephalus microplus
Parasite
rt-pcr
protein 3d modeling
pesticide-resistance
cattle tick
title Relationship between acaricide resistance and acetylcholinesterase gene polymorphisms in the cattle tick Rhipicephalus microplus
title_full Relationship between acaricide resistance and acetylcholinesterase gene polymorphisms in the cattle tick Rhipicephalus microplus
title_fullStr Relationship between acaricide resistance and acetylcholinesterase gene polymorphisms in the cattle tick Rhipicephalus microplus
title_full_unstemmed Relationship between acaricide resistance and acetylcholinesterase gene polymorphisms in the cattle tick Rhipicephalus microplus
title_short Relationship between acaricide resistance and acetylcholinesterase gene polymorphisms in the cattle tick Rhipicephalus microplus
title_sort relationship between acaricide resistance and acetylcholinesterase gene polymorphisms in the cattle tick rhipicephalus microplus
topic rt-pcr
protein 3d modeling
pesticide-resistance
cattle tick
url https://www.parasite-journal.org/articles/parasite/full_html/2024/01/parasite230118/parasite230118.html
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