Histochemical Localization of Esterases in the Integument of the Female Boophilus microplus (Acari: Ixodidae) Tick

Department of Veterinary Pathobiology, College of Veterinary Medicine, Texas A&M University, College Station 77845-4467, USA.
Journal of Medical Entomology (Impact Factor: 1.95). 12/2001; 38(6):780-2. DOI: 10.1603/0022-2585-38.6.780
Source: PubMed


The cattle tick Boophilus microplus (Canestrini) is one of the most important ectoparasites affecting tropical cattle with worldwide distribution. Application of organophosphate compounds (OP) is extensively used as a tick control method. However, the appearance of ticks resistant to the OP decreases the therapeutic efficacy of such compounds. Esterases have been implicated as potential biochemical mechanisms for detoxification in B. microplus larvae. We found increased esterase activity in the inner layers of the integument of OP resistant adult female B. microplus ticks as compared with the OP susceptible ticks. We discuss the potential role of these enzymes during acaricide metabolism and propose future research.

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    • "Although evidence of esterase activity related to acaricide resistance in B. microplus larvae has been previously described (Rosario-Cruz et al. 1997, Jamroz et al. 2000), several esterases were mentioned, but no not speciÞc esterase was identiÞed as a potential detoxiÞcation enzyme. We previously detected a 64 Kd B-esterase highly active in organophosphate resistant larvae (Villarino et al. 2000) and identiÞed the presence of different amounts of esterase activity between OP-resistant and susceptible strains of adult female integuments (Villarino et al. 2001). "
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    ABSTRACT: Esterase activity was present in the integument of adult female Boophilus microplus (Canestrini) ticks that are resistant to organophosphates (OP). Three esterases were purified from adult integument, which hydrolyze the substrates p-nitrophenylacetate and beta-naphthyl acetate after comparison of OP-resistant strain and an OP-susceptible strains. The esterases purified by ion-exchange chromatography were characterized using different esterase inhibitors; eserine sulfate, diethyl p-nitrophenyl phosphate (paraoxon), para-hydroxyl-mercuribenzoate (pHMB), and diisopropylphosphofluoridate (DFP). All of the esterases had a molecular mass of 64 Kd (PAGE), but were characterized based on the esterase inhibitor effects as a B-esterase with beta-naphthyl acetate affinity, a carboxylesterase with beta-naphthyl acetate and p-nitrophenyl acetate affinity, and one A-Esterase (nonspecific esterase) with p-nitrophenyl acetate affinity. The described esterases are an important detoxification mechanism in B. microplus ticks at the integument. We describe also a microplate biochemical assay for the detection of esterase activity in the tick integument, potentially a useful tool to detect esterase-mediated OP resistance in B. microplus ticks.
    Journal of Medical Entomology 02/2003; 40(1):52-7. DOI:10.1603/0022-2585-40.1.52 · 1.95 Impact Factor
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    ABSTRACT: The cattle tick Boophilus microplus causes significant economic losses in cattle in the tropical areas of Central and South America. Acaricides are widely used to control tick infestations, with the consequent selection of tolerant and resistant subpopulations. Detoxifying enzymes, and esterases in particular, have been associated with organophosphate resistance in Mexican isolates of B. microplus ticks. Here, we present results of the biochemical detection of esterases and oxidases in 20 isolates of larvae and adult ticks and the effect of esterase and oxidase inhibitors on larvae and adult stages of the tick. Our results indicate the presence of significant differences both in vivo and in vitro between esterase and oxidase activities of OP-susceptible and OP-resistant isolates, even when samples were collected in the same area. The importance of such differences in regionalized integrated pest management and in the US Tick Eradication Program is discussed.
    Enperimental and Applied Acarology 01/2002; 28(1-4):265-71. DOI:10.1023/A:1025371105437 · 1.62 Impact Factor
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    ABSTRACT: The levels of resistance to two organophosphate acaricides, coumaphos and diazinon, in several Mexican strains of Boophilus microplus (Canestrini) were evaluated using the FAO larval packet test. Regression analysis of LC50 data revealed a significant cross-resistance pattern between those two acaricides. Metabolic mechanisms of resistance were investigated with synergist bioassays. Piperonyl butoxide (PBO) reduced coumaphos toxicity in susceptible strains, but synergized coumaphos toxicity in resistant strains. There was a significant correlation between PBO synergism ratios and the coumaphos resistance ratios. The results suggest that an enhanced cytochrome P450 monooxygenase (cytP450)-mediated detoxification mechanism may exist in the resistant strains, in addition to the cytP450-mediated metabolic pathway that activates coumaphos. PBO failed to synergize diazinon toxicity in resistant strains, suggesting the cytP450 involved in detoxification were specific. Triphenylphosphate (TPP) synergized toxicity of both acaricides in both susceptible and resistant strains, and there was no correlation between TPP synergism ratios and the LC50 estimates for either acaricide. Esterases may not play a major role in resistance to coumaphos and diazinon in those strains. Bioassays with diethyl maleate (DEM) revealed a significant correlation between DEM synergism ratios and LC50 estimates for diazinon, suggesting a possible role for glutathione S-transferases in diazinon detoxification. Resistance to coumaphos in the Mexican strains of B. microplus was likely to be conferred by both a cytP450-mediated detoxification mechanism described here and the mechanism of insensitive acetylcholinesterases reported elsewhere. The results of this study also underscore the potential risk of coumaphos resistance in B. microplus from Mexico to the U.S. cattle fever tick eradication program.
    Journal of Medical Entomology 08/2003; 40(4):482-90. DOI:10.1603/0022-2585-40.4.482 · 1.95 Impact Factor
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