Characterisation of Dermanyssus gallinae glutathione S-transferases and their potential as acaricide detoxification proteins.
Characterisation of Dermanyssus gallinae glutathione S-transferases and their potential as acaricide detoxification proteins.
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DOI：
10.1186/s13071-015-0960-9
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发表时间：
2015-06-26
影响因子：
3.2
通讯作者：
Nisbet AJ
中科院分区：
文献类型：
--
作者：
Bartley K;Wright HW;Bull RS;Huntley JF;Nisbet AJ
谷胱甘肽S-转移酶（GST）通过催化还原型谷胱甘肽（GSH）与亲电性异生物质底物的结合促进药物的解毒，因此在多药耐药中具有功能。因此，GST的知识可以告知内寄生虫和外寄生虫物种的耐药性和新的干预措施。杀螨剂抗性和对新的控制方法的需求都是对鸡皮刺螨的迫切需求，鸡皮刺螨是一种经济上非常重要的家禽嗜血性体外寄生虫。建立了D.对鸡的11个重叠群序列进行了GSTBlastX鉴定。由3个重叠群代表的转录物，命名为Deg-GST-1，−2和−3，进行了完全测序，并通过系统发育分析进一步表征。Deg-GST-1、-2和-3（rDeg-GST）的重组版本具有酶活性，通过评估所选杀螨剂抑制rDeg-GST酶活性的能力，确定了rDeg-GST的杀螨剂结合特性。鉴定的GST中有6个属于mu类，其次是3个kappa、1个omega和1个delta类分子。Deg-GST-1和-3明确划分为orthophylmu类GST，Deg-GST-2划分为delta类GST。辛硫磷、氯菊酯和阿维菌素对rDeg-GST-1活性的抑制率分别为56%、35%和17%。辛硫磷对rDeg-2-GST（14.8%）和rDeg-GST-3（20.6%）活性也有抑制作用。Deg-GST在农药解毒中可能具有重要作用，并且随着世界范围内该物种杀螨剂抗性的增加，Deg-GST是新干预措施的有吸引力的目标。
Glutathione S-transferases (GSTs) facilitate detoxification of drugs by catalysing the conjugation of the reduced glutathione (GSH) to electrophilic xenobiotic substrates and therefore have a function in multi-drug resistance. As a result, knowledge of GSTs can inform both drug resistance in, and novel interventions for, the control of endo- and ectoparasite species. Acaricide resistance and the need for novel control methods are both pressing needs for Dermanyssus gallinae, a highly economically important haematophagous ectoparasite of poultry. A transcriptomic database representing D. gallinae was examined and 11 contig sequences were identified with GST BlastX identities. The transcripts represented by 3 contigs, designated Deg-GST-1, −2 and −3, were fully sequenced and further characterized by phylogenetic analysis. Recombinant versions of Deg-GST-1, −2 and −3 (rDeg-GST) were enzymically active and acaricide-binding properties of the rDeg-GSTs were established by evaluating the ability of selected acaricides to inhibit the enzymatic activity of rDeg-GSTs. 6 of the identified GSTs belonged to the mu class, followed by 3 kappa, 1 omega and 1 delta class molecules. Deg-GST-1 and −3 clearly partitioned with orthologous mu class GSTs and Deg-GST-2 partitioned with delta class GSTs. Phoxim, permethrin and abamectin significantly inhibited rDeg-GST-1 activity by 56, 35 and 17 % respectively. Phoxim also inhibited rDeg-2-GST (14.8 %) and rDeg-GST-3 (20.6 %) activities. Deg-GSTs may have important roles in the detoxification of pesticides and, with the increased occurrence of acaricide resistance in this species worldwide, Deg-GSTs are attractive targets for novel interventions.
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