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The Rhipicephalus (Boophilus) microplus tick is the main ectoparasite of cattle in tropical and subtropical regions worldwide. Resistance to chemical acaricides has become widespread affirming the need for new drugs to tick control. Terpenes have become a promising alternative for cattle tick control, however the mechanism of action of these compounds is still controversial. Inhibition of acetylcholinesterase (AChE) is a well established mechanism of action of organophosphate and carbamate acaricides, but the possible action of terpenes on tick AChEs has seldom been studied in resistant and sensitive strains of R. (B.) microplus. The aim of the present study was to evaluate terpene inhibition of AChE from resistant and sensitive strains of R. (B.) microplus in correlation with their acaricidal activity. Among the terpenes used in the present study, p-cymene, thymol, carvacrol, and citral displayed acaricidal activity with LC of 1.75, 1.54, 1.41, and 0.38 mg.mL for the susceptible strain, and LC of 1.40, 1.81, 1.10, and 1.13 mg.mL for the resistant strain. Thymol and carvacrol inhibited the AChE of the susceptible strain larvae with IC of 0.93 and 0.04 mg.mL, respectively. The IC exhibited by eucalyptol, carvacrol and thymol for AChE of the resistant strain larvae were 0.36, 0.28, and 0.13 mg.mL, respectively. This was the first study to investigate the action of terpenes on AChE from susceptible and resistant R. (B.) microplus. As not all terpenes with acaridical activity showed AChE inhibition, the participation of AChE in the acaricidal activity of terpenes needs further investigation.
This article was published in the following journal.
Name: Veterinary parasitology
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A species of protozoa that is a cause of bovine babesiosis. Ticks of the genera Boophilus, Rhipicephalus, and IXODES are the chief vectors.
Conditions characterized by impaired transmission of impulses at the NEUROMUSCULAR JUNCTION. This may result from disorders that affect receptor function, pre- or postsynaptic membrane function, or ACETYLCHOLINESTERASE activity. The majority of diseases in this category are associated with autoimmune, toxic, or inherited conditions.
An organophosphorus insecticide that inhibits acetylcholinesterase.
An adaptor protein, consisting of seven WD REPEATS along its length, that functions as a component of the MECHANISTIC TARGET OF RAPAMYCIN COMPLEX 1 and MTORC2 COMPLEX. It interacts directly with MTOR to enhance its kinase activity and stabilizes the MTOR-RPTOR PROTEIN interaction in nutrient-poor conditions, favoring RPTOR inhibition of MTOR activity.
An organophosphate insecticide that inhibits monoamine oxidase and acetylcholinesterase. It has been shown to be genotoxic.
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