Inhibition of the recombinant cattle tick Rhipicephalus (Boophilus) annulatus glutathione S-transferase

Guneidy, Rasha A.; Shahein, Yasser E.; Abouelella, Amira M.; Zaki, Eman R.; Hamed, Ragaa R.

doi:10.1016/j.ttbdis.2014.03.009

Cited by 15 publications

(7 citation statements)

References 38 publications

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“…Ticks are obligate hematophagous parasites prevalent worldwide. They serve as several disease vectors in humans and other animals [ 1 ]. Haemaphysalis longicornis is a tick with a distribution in Australia, New Zealand and eastern Asia [ 2 ].…”

Section: Introductionmentioning

confidence: 99%

Characterization and expression analysis of a newly identified glutathione S-transferase of the hard tick Haemaphysalis longicornis during blood-feeding

et al. 2018

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BackgroundTicks are obligate hematophagous parasites important economically and to health. Ticks consume large amounts of blood for their survival and reproduction; however, large amounts of iron in blood could lead to oxidative stress. Ticks use several molecules such as glutathione S-transferases (GSTs), ferritins, and peroxiredoxins to cope with oxidative stress. This study aimed to identify and characterize the GSTs of the hard tick Haemaphysalis longicornis in order to determine if they have a role in coping with oxidative stress.MethodsGenes encoding GSTs of H. longicornis were isolated from the midgut CDNA library. Genes have been cloned and recombinant GSTs have been expressed. The enzymatic activities, enzyme kinetic constants, and optimal pH of the recombinant GSTs toward 1-chloro-2,4-dinitrobenzene (CDNB) were determined. The gene transcription and protein expression profiles were determined in the whole ticks and internal organs, and developmental stages using real time RT-PCR and Western blotting during blood feeding. The localization of GST proteins in organs was also observed using immunofluorescent antibody test (IFAT).ResultsWe have isolated two genes encoding GSTs (HlGST and HlGST2). The enzymatic activity toward CDNB is 9.75 ± 3.04 units/mg protein for recombinant HlGST and 11.63 ± 4.08 units/mg protein for recombinant HlGST2. Kinetic analysis of recombinant HlGST showed Km values of 0.82 ± 0.14 mM and 0.64 ± 0.32 mM for the function of CDNB and GSH, respectively. Meanwhile, recombinant HlGST2 has Km values of 0.61 ± 0.20 mM and 0.53 ± 0.02 mM for the function of CDNB and GSH, respectively. The optimum pH of recombinant HlGST and recombinant HlGST2 activity was 7.5–8.0. Transcription of both GSTs increases in different developmental stages and organs during blood-feeding. GST proteins are upregulated during blood-feeding but decreased upon engorgement in whole ticks and in some organs, such as the midgut and hemocytes. Interestingly, salivary glands, ovaries, and fat bodies showed decreasing protein expression during blood-feeding to engorgement. Varying localization of GSTs in the midgut, salivary glands, fat bodies, ovaries, and hemocytes was observed depending on the feeding state, especially in the midgut and salivary glands.ConclusionsIn summary, a novel GST of H. longicornis has been identified. Characterization of the GSTs showed that GSTs have positive correlation with the degree and localization of oxidative stress during blood-feeding. This could indicate their protective role during oxidative stress.Electronic supplementary materialThe online version of this article (10.1186/s13071-018-2667-1) contains supplementary material, which is available to authorized users.

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Section: Introductionmentioning

confidence: 99%

Characterization and expression analysis of a newly identified glutathione S-transferase of the hard tick Haemaphysalis longicornis during blood-feeding

et al. 2018

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“…annulatus resisted the effect of IVM on GST levels with time. Thus, the suppression of tick GST action to interrupt their detoxification system and heme metabolism has potential as a tick control strategy [40,41].…”

Section: Discussionmentioning

confidence: 99%

In vitro study of ivermectin efficiency against the cattle tick, Rhipicephalus (Boophilus) annulatus, among cattle herds in El-Beheira, Egypt

et al. 2019

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Background and Aim: Ivermectin (IVM) has been used in veterinary practice to control different parasitic infestations over the past two decades. This study aimed to re-assess the acaricidal effects of IVM, as well as to evaluate its efficacy against Rhipicephalus (Boophilus) annulatus by determining the mortality rate, γ-aminobutyric acid (GABA) level, and oxidative/ antioxidative homeostasis (malondialdehyde [MDA] levels and glutathione S-transferase [GST] activities). Materials and Methods: Adult females of Rhipicephalus (Boophilus) annulatus were picked from cattle farms in El-Beheira Governorate, Egypt. Ticks were equally allocated to seven experimental groups to assess the acaricidal potential of IVM chemotherapeutics in controlling R. (B.) annulatus. IVM was prepared at three concentrations (11.43, 17.14, and 34.28 μM of IVM). Results: Mortality rate was calculated among the treated ticks. In addition, GABA, GST, and MDA biomarker levels were monitored. The data revealed a noticeable change in GST activity, a detoxification enzyme found in R. (B.) annulatus, through a critical elevation in mortality percentage. Conclusion: IVM-induced potent acaricidal effects against R. (B.) annulatus by repressing GST activity for the initial 24 h after treatment. Collectively, this paper reports the efficacy of IVM in a field population of R. (B.) annulatus in Egypt. Keywords: acaricidal, glutathione S-transferase, ivermectin, malondialdehyde, Rhipicephalus (Boophilus) annulatus, γ-aminobutyric acid.

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“…annulatus and the active recombinant BaGST was expressed and purified as fusion protein His-tagged protein (Shahein et al, 2008). This GST was later shown to be effectively inhibited by phenolic compounds and flavonoids from plant extracts but also by a haematin (Guneidy et al, 2014). RNAi-mediated silencing of the GST from R. sanguineus revealed the role of this enzyme in permethrin detoxification as the GST-KD ticks were more susceptible to the acaricide exposure (Duscher et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

Inducible glutathione S-transferase (IrGST1) from the tick Ixodes ricinus is a haem-binding protein

Perner

Kotál

Hatalová

et al. 2018

Insect Biochemistry and Molecular Biology

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Blood-feeding parasites are inadvertently exposed to high doses of potentially cytotoxic haem liberated upon host blood digestion. Detoxification of free haem is a special challenge for ticks, which digest haemoglobin intracellularly. Ticks lack a haem catabolic mechanism, mediated by haem oxygenase, and need to dispose of vast majority of acquired haem via its accumulation in haemosomes. The knowledge of individual molecules involved in the maintenance of haem homeostasis in ticks is still rather limited. RNA-seq analyses of the Ixodes ricinus midguts from blood- and serum-fed females identified an abundant transcript of glutathione S-transferase (gst) to be substantially up-regulated in the presence of red blood cells in the diet. Here, we have determined the full sequence of this encoding gene, ir-gst1, and found that it is homologous to the delta-/epsilon-class of GSTs. Phylogenetic analyses across related chelicerates revealed that only one clear IrGST1 orthologue could be found in each available transcriptome from hard and soft ticks. These orthologues create a well-supported clade clearly separated from other ticks' or mites' delta-/epsilon-class GSTs and most likely evolved as an adaptation to tick blood-feeding life style. We have confirmed that IrGST1 expression is induced by dietary haem(oglobin), and not by iron or other components of host blood. Kinetic properties of recombinant IrGST1 were evaluated by model and natural GST substrates. The enzyme was also shown to bind haemin in vitro as evidenced by inhibition assay, VIS spectrophotometry, gel filtration, and affinity chromatography. In the native state, IrGST1 forms a dimer which further polymerises upon binding of excessive amount of haemin molecules. Due to susceptibility of ticks to haem as a signalling molecule, we speculate that the expression of IrGST1 in tick midgut functions as intracellular buffer of labile haem pool to ameliorate its cytotoxic effects upon haemoglobin intracellular hydrolysis.

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Inhibition of the recombinant cattle tick Rhipicephalus (Boophilus) annulatus glutathione S-transferase

Cited by 15 publications

References 38 publications

Characterization and expression analysis of a newly identified glutathione S-transferase of the hard tick Haemaphysalis longicornis during blood-feeding

Characterization and expression analysis of a newly identified glutathione S-transferase of the hard tick Haemaphysalis longicornis during blood-feeding

In vitro study of ivermectin efficiency against the cattle tick, Rhipicephalus (Boophilus) annulatus, among cattle herds in El-Beheira, Egypt

Inducible glutathione S-transferase (IrGST1) from the tick Ixodes ricinus is a haem-binding protein

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