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Molecular cloning and characterization of a glycine-like receptor gene from the cattle tick Rhipicephalus (Boophilus) microplus (Acari: Ixodidae)
The cattle tick Rhipicephalus (Boophilus) microplus is the most economically important ectoparasite affecting the cattle industry in tropical and subtropical areas around the world. The principal method of tick control has relied mainly on the use of chemical acaricides, including ivermectin; howeve...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
EDP Sciences
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4150426/ https://www.ncbi.nlm.nih.gov/pubmed/25174962 http://dx.doi.org/10.1051/parasite/2014047 |
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author | Flores-Fernández, José Miguel Gutiérrez-Ortega, Abel Padilla-Camberos, Eduardo Rosario-Cruz, Rodrigo Hernández-Gutiérrez, Rodolfo Martínez-Velázquez, Moisés |
author_facet | Flores-Fernández, José Miguel Gutiérrez-Ortega, Abel Padilla-Camberos, Eduardo Rosario-Cruz, Rodrigo Hernández-Gutiérrez, Rodolfo Martínez-Velázquez, Moisés |
author_sort | Flores-Fernández, José Miguel |
collection | PubMed |
description | The cattle tick Rhipicephalus (Boophilus) microplus is the most economically important ectoparasite affecting the cattle industry in tropical and subtropical areas around the world. The principal method of tick control has relied mainly on the use of chemical acaricides, including ivermectin; however, cattle tick populations resistant to ivermectin have recently been reported in Brazil, Mexico, and Uruguay. Currently, the molecular basis for ivermectin susceptibility and resistance are not well understood in R. microplus. This prompted us to search for potential molecular targets for ivermectin. Here, we report the cloning and molecular characterization of a R. microplus glycine-like receptor (RmGlyR) gene. The characterized mRNA encodes for a 464-amino acid polypeptide, which contains features common to ligand-gated ion channels, such as a large N-terminal extracellular domain, four transmembrane domains, a large intracellular loop and a short C-terminal extracellular domain. The deduced amino acid sequence showed around 30% identity to GlyRs from some invertebrate and vertebrate organisms. The polypeptide also contains the PAR motif, which is important for forming anion channels, and a conserved glycine residue at the third transmembrane domain, which is essential for high ivermectin sensitivity. PCR analyses showed that RmGlyR is expressed at egg, larval and adult developmental stages. Our findings suggest that the deduced receptor is an additional molecular target to ivermectin and it might be involved in ivermectin resistance in R. microplus. |
format | Online Article Text |
id | pubmed-4150426 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | EDP Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-41504262014-09-11 Molecular cloning and characterization of a glycine-like receptor gene from the cattle tick Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) Flores-Fernández, José Miguel Gutiérrez-Ortega, Abel Padilla-Camberos, Eduardo Rosario-Cruz, Rodrigo Hernández-Gutiérrez, Rodolfo Martínez-Velázquez, Moisés Parasite Research Article The cattle tick Rhipicephalus (Boophilus) microplus is the most economically important ectoparasite affecting the cattle industry in tropical and subtropical areas around the world. The principal method of tick control has relied mainly on the use of chemical acaricides, including ivermectin; however, cattle tick populations resistant to ivermectin have recently been reported in Brazil, Mexico, and Uruguay. Currently, the molecular basis for ivermectin susceptibility and resistance are not well understood in R. microplus. This prompted us to search for potential molecular targets for ivermectin. Here, we report the cloning and molecular characterization of a R. microplus glycine-like receptor (RmGlyR) gene. The characterized mRNA encodes for a 464-amino acid polypeptide, which contains features common to ligand-gated ion channels, such as a large N-terminal extracellular domain, four transmembrane domains, a large intracellular loop and a short C-terminal extracellular domain. The deduced amino acid sequence showed around 30% identity to GlyRs from some invertebrate and vertebrate organisms. The polypeptide also contains the PAR motif, which is important for forming anion channels, and a conserved glycine residue at the third transmembrane domain, which is essential for high ivermectin sensitivity. PCR analyses showed that RmGlyR is expressed at egg, larval and adult developmental stages. Our findings suggest that the deduced receptor is an additional molecular target to ivermectin and it might be involved in ivermectin resistance in R. microplus. EDP Sciences 2014 2014-09-02 /pmc/articles/PMC4150426/ /pubmed/25174962 http://dx.doi.org/10.1051/parasite/2014047 Text en © J.M. Flores-Fernaández et al., published by EDP Sciences, 2014 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Flores-Fernández, José Miguel Gutiérrez-Ortega, Abel Padilla-Camberos, Eduardo Rosario-Cruz, Rodrigo Hernández-Gutiérrez, Rodolfo Martínez-Velázquez, Moisés Molecular cloning and characterization of a glycine-like receptor gene from the cattle tick Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) |
title | Molecular cloning and characterization of a glycine-like receptor gene from the cattle tick Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) |
title_full | Molecular cloning and characterization of a glycine-like receptor gene from the cattle tick Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) |
title_fullStr | Molecular cloning and characterization of a glycine-like receptor gene from the cattle tick Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) |
title_full_unstemmed | Molecular cloning and characterization of a glycine-like receptor gene from the cattle tick Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) |
title_short | Molecular cloning and characterization of a glycine-like receptor gene from the cattle tick Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) |
title_sort | molecular cloning and characterization of a glycine-like receptor gene from the cattle tick rhipicephalus (boophilus) microplus (acari: ixodidae) |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4150426/ https://www.ncbi.nlm.nih.gov/pubmed/25174962 http://dx.doi.org/10.1051/parasite/2014047 |
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