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Molecular cloning and characterization of a glycine-like receptor gene from the cattle tick Rhipicephalus (Boophilus) microplus (Acari: Ixodidae).

Flores-Fernández JM, Gutiérrez-Ortega A, Padilla-Camberos E, Rosario-Cruz R, Hernández-Gutiérrez R, Martínez-Velázquez M - Parasite (2014)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco, AC, Av. Normalistas 800, Col. Colinas de la Normal, 44270 Guadalajara, Jalisco, México.

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Alignment of the deduced amino acid sequence of GlyR from R. microplus (KJ476181), GlyR from C. Intestinalis (BAI66458), GlyRa (NP_000162) and GlyRb (NP_000815) from H. sapiens, GlyR from B. taurus (NP_776746), and GlyR from D. rerio (NP_571477). The cysteines forming the Cys-loop are highlighted by red shading and the putative membrane domains (TM1–TM4) are highlighted by gray shading. The PAR residues are highlighted in yellow shading. The glycine residue marked in turquoise likely confers upon the receptor high sensitivity to ivermectin. The approximate locations of the glycine binding domains are labeled as A-F. Known residues in human GlyRa that play a role in glycine binding are highlighted in green [22].
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Figure 3: Alignment of the deduced amino acid sequence of GlyR from R. microplus (KJ476181), GlyR from C. Intestinalis (BAI66458), GlyRa (NP_000162) and GlyRb (NP_000815) from H. sapiens, GlyR from B. taurus (NP_776746), and GlyR from D. rerio (NP_571477). The cysteines forming the Cys-loop are highlighted by red shading and the putative membrane domains (TM1–TM4) are highlighted by gray shading. The PAR residues are highlighted in yellow shading. The glycine residue marked in turquoise likely confers upon the receptor high sensitivity to ivermectin. The approximate locations of the glycine binding domains are labeled as A-F. Known residues in human GlyRa that play a role in glycine binding are highlighted in green [22].

Mentions: BLAST analysis showed 32%, 34%, and 32% identities among RmGlyR and GlyRs from Ciona intestinalis, Danio rerio and Bos taurus, respectively, and 33% and 29% with the subunits a and b of GlyR from Homo sapiens, respectively. All compared amino acid sequences contain four transmembrane domains and two cysteine residues that form the characteristic Cys-loop (Fig. 3). The sequences also share the PAR signature at the end of the first intracellular loop (Fig. 3, shaded in yellow). This signature is associated with most anionic Cys-loop (ligand-gated ion channels) LGICs, more specifically in those labeled as alpha subunits.Figure 3.


Molecular cloning and characterization of a glycine-like receptor gene from the cattle tick Rhipicephalus (Boophilus) microplus (Acari: Ixodidae).

Flores-Fernández JM, Gutiérrez-Ortega A, Padilla-Camberos E, Rosario-Cruz R, Hernández-Gutiérrez R, Martínez-Velázquez M - Parasite (2014)

Alignment of the deduced amino acid sequence of GlyR from R. microplus (KJ476181), GlyR from C. Intestinalis (BAI66458), GlyRa (NP_000162) and GlyRb (NP_000815) from H. sapiens, GlyR from B. taurus (NP_776746), and GlyR from D. rerio (NP_571477). The cysteines forming the Cys-loop are highlighted by red shading and the putative membrane domains (TM1–TM4) are highlighted by gray shading. The PAR residues are highlighted in yellow shading. The glycine residue marked in turquoise likely confers upon the receptor high sensitivity to ivermectin. The approximate locations of the glycine binding domains are labeled as A-F. Known residues in human GlyRa that play a role in glycine binding are highlighted in green [22].
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4150426&req=5

Figure 3: Alignment of the deduced amino acid sequence of GlyR from R. microplus (KJ476181), GlyR from C. Intestinalis (BAI66458), GlyRa (NP_000162) and GlyRb (NP_000815) from H. sapiens, GlyR from B. taurus (NP_776746), and GlyR from D. rerio (NP_571477). The cysteines forming the Cys-loop are highlighted by red shading and the putative membrane domains (TM1–TM4) are highlighted by gray shading. The PAR residues are highlighted in yellow shading. The glycine residue marked in turquoise likely confers upon the receptor high sensitivity to ivermectin. The approximate locations of the glycine binding domains are labeled as A-F. Known residues in human GlyRa that play a role in glycine binding are highlighted in green [22].
Mentions: BLAST analysis showed 32%, 34%, and 32% identities among RmGlyR and GlyRs from Ciona intestinalis, Danio rerio and Bos taurus, respectively, and 33% and 29% with the subunits a and b of GlyR from Homo sapiens, respectively. All compared amino acid sequences contain four transmembrane domains and two cysteine residues that form the characteristic Cys-loop (Fig. 3). The sequences also share the PAR signature at the end of the first intracellular loop (Fig. 3, shaded in yellow). This signature is associated with most anionic Cys-loop (ligand-gated ion channels) LGICs, more specifically in those labeled as alpha subunits.Figure 3.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco, AC, Av. Normalistas 800, Col. Colinas de la Normal, 44270 Guadalajara, Jalisco, México.

Show MeSH