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Esterases of Varroa destructor (Acari: Varroidae), parasitic mite of the honeybee

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Abstract

Varroa destructor is an ectoparasite that causes serious damage to the population of the honeybee. Increasing resistance of the parasite to acaricides is related, among others, to metabolic adaptations of its esterases to facilitate decomposition of the chemicals used. Esterases are a large heterogeneous group of enzymes that metabolize a number of endogenous and exogenous substrates with ester binding. The aim of the present study was to determine the activity of esterases in the body extracts (BE) and excretion/secretion products (E/SP) of the mite. The enzymes contained in the E/SP should originate mainly from the salivary glands and the alimentary system and they may play a particularly important role in the first line of defence of the mite against acaricides. Activity of cholinesterases (ChEs) [acetylcholinesterase (AChE) and butyrylcholinesterase], carboxylesterases (CEs) and phosphatases [alkaline phosphatase (AP) and acid phosphatase (AcP)] was investigated. The activity of all the enzymes except AChE was higher in the E/SP than in the BE. ChEs from the BE and from the E/SP reacted differently on eserine, a ChE inhibitor. Eserine inhibited both enzymes from the BE, increased decomposition of acetylcholine, but did not influence hydrolysis of butyrylcholine by the E/SP. Activity of the CEs from the BE in relation to the esters of carboxylic acids can be presented in the following series: C10 > C12 > C14 > C8 > C2 > C4 = C16, while activity of the CEs from the E/SP was: C4 > C8 > C2 > C14 > C10 > C12 > C16. The inhibitor of CEs, triphenyl phosphate, reduced the activity of esterases C2–C8 and C14–C16; however, it acted in the opposite way to CEs C10 and C12. The activity of both phosphatases was higher in the E/SP than in the BE (AcP about twofold and AP about 2.6-fold); the activities of AP and AcP in the same material were similar. Given the role of esterases in resistance to pesticides, further studies are necessary to obtain complete biochemical characteristics of the enzymes currently present in V. destructor.

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Acknowledgments

This study was supported by Grant Number N N308 169338 from the Ministry of Science and Higher Education, Poland.

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Authors and Affiliations

  1. Biochemistry Department, Faculty of Biology and Biotechnology, University of Warmia and Mazury, Oczapowskiego 1A Str., 10-719, Olsztyn, Poland

    Małgorzata Dmitryjuk, Krystyna Żółtowska & Regina Frączek

  2. Division of Reproductive Biology, Institute of Animal Reproduction and Food Research of Polish Academy of Sciences, Tuwima Str. 10, 10-748, Olsztyn, Poland

    Zbigniew Lipiński

Authors
  1. Małgorzata Dmitryjuk
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  2. Krystyna Żółtowska
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  3. Regina Frączek
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  4. Zbigniew Lipiński
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Correspondence to Małgorzata Dmitryjuk.

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Dmitryjuk, M., Żółtowska, K., Frączek, R. et al. Esterases of Varroa destructor (Acari: Varroidae), parasitic mite of the honeybee. Exp Appl Acarol 62, 499–510 (2014). https://doi.org/10.1007/s10493-013-9754-y

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