Effect of acaricides on the activity of a Boophilus microplus glutathione S-transferase

Vaz, Itabajara da Silva; Lermen, Tiago Torino; Michelon, André; Ferreira, Carlos Alexandre Sanchez; Freitas, Daniela Reis Joaquim de; Termignoni, Carlos; Masuda, Aoi

doi:10.1016/j.vetpar.2003.11.004

Cited by 39 publications

(23 citation statements)

References 23 publications

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“…We hypothesize that the SlituGSTs could play a role in insecticide resistance in the tobacco cutworm. This result is consistent with those found in the mosquito, Anopheles dirus , and ticks, Haemaphysalis longicornis , and Rhipicephalus appendiculatus (da Silva Vaz et al., ; Prapanthadara, Ranson, Somboon, & Hemingway, ).…”

Section: Discussionsupporting

confidence: 90%

Enzymatic characterization of two epsilon‐class glutathione S‐transferases of Spodoptera litura

Hirowatari

Chen

Mita

et al. 2017

Arch Insect Biochem Physiol

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Two cDNAs encoding glutathione S-transferase (GST) of the tobacco cutworm, Spodoptera litura, were cloned by reverse transcriptase-polymerase chain reaction. The deduced amino acid sequences of the resulting clones revealed 32-51% identities to the epsilon-class GSTs from other organisms. The recombinant proteins were functionally overexpressed in Escherichia coli cells in soluble form and were purified to homogeneity. The enzymes were capable of catalyzing the bioconjugation of glutathione with 1-chloro-2,4-dinitrobenzene, 1,2-epoxy-3-(4-nitrophenoxy)-propane, and ethacrynic acid. A competition assay revealed that the GST activity was inhibited by insecticides, suggesting that it could be conducive to insecticide tolerance in the tobacco cutworm.

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Section: Discussionsupporting

confidence: 90%

Enzymatic characterization of two epsilon‐class glutathione S‐transferases of Spodoptera litura

Hirowatari

Chen

Mita

et al. 2017

Arch Insect Biochem Physiol

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show abstract

“…This result is consistent with those found in the mosquito, Anopheles dirus, and ticks, Haemaphysalis longicornis and Rhipicephalus appendiculatus. 25,26) The activity levels of GSTs in these species were reduced to ∼85% and ∼60%, respectively, by 0.1 mM of deltamethrin, 27) while bmGSTO exhibited ∼20% of its maximum activity under the same conditions.…”

Section: Discussionmentioning

confidence: 90%

Biochemical characterization of an unclassified glutathione <i>S</i>-transferase of <i>Plutella xylostella</i>

et al. 2016

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cDNA encoding an unclassified glutathione S-transferase (GST) of the diamondback moth, Plutella xylostella, was cloned by reverse transcriptase-polymerase chain reaction. The resulting clone was sequenced and the amino acid sequence deduced, revealing 67%-73% identities with unclassified GSTs from other organisms. A recombinant protein was functionally overexpressed in Escherichia coli cells in a soluble form and purified to homogeneity. The enzyme was capable to catalyze the transformation of 1-chloro-2,4-dinitrobenzene and ethacrynic acid with glutathione. A competition assay revealed that GST activity was inhibited by insecticides, suggesting that the enzyme could contribute to insecticide metabolism in the diamondback moth.

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“…Glutathione S-transferase (GST) is a protein that catalyzes the conjugation of glutathione with several xenobiotic and endogenous substances [164]. In this sense, GST seems to be closely associated with detoxification and acaricide resistance [165]. Additionally, it has been proposed that GST secreted by parasite salivary glands has immunomodulatory activity due to the alteration of cytokine gene expression profile, modulation of immune cell proliferation and decrease in oxidative ability of phagocytes [166].…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Cattle Tick Rhipicephalus (Boophilus) microplus Saliva: A Comparison between Partially and Fully Engorged Females

et al. 2014

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The cattle tick Rhipicephalus (Boophilus) microplus is one of the most harmful parasites affecting bovines. Similarly to other hematophagous ectoparasites, R. microplus saliva contains a collection of bioactive compounds that inhibit host defenses against tick feeding activity. Thus, the study of tick salivary components offers opportunities for the development of immunological based tick control methods and medicinal applications. So far, only a few proteins have been identified in cattle tick saliva. The aim of this work was to identify proteins present in R. microplus female tick saliva at different feeding stages. Proteomic analysis of R. microplus saliva allowed identifying peptides corresponding to 187 and 68 tick and bovine proteins, respectively. Our data confirm that (i) R. microplus saliva is complex, and (ii) that there are remarkable differences in saliva composition between partially engorged and fully engorged female ticks. R. microplus saliva is rich mainly in (i) hemelipoproteins and other transporter proteins, (ii) secreted cross-tick species conserved proteins, (iii) lipocalins, (iv) peptidase inhibitors, (v) antimicrobial peptides, (vii) glycine-rich proteins, (viii) housekeeping proteins and (ix) host proteins. This investigation represents the first proteomic study about R. microplus saliva, and reports the most comprehensive Ixodidae tick saliva proteome published to date. Our results improve the understanding of tick salivary modulators of host defense to tick feeding, and provide novel information on the tick-host relationship.

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Effect of acaricides on the activity of a Boophilus microplus glutathione S-transferase

Cited by 39 publications

References 23 publications

Enzymatic characterization of two epsilon‐class glutathione S‐transferases of Spodoptera litura

Enzymatic characterization of two epsilon‐class glutathione S‐transferases of Spodoptera litura

Biochemical characterization of an unclassified glutathione <i>S</i>-transferase of <i>Plutella xylostella</i>

Proteomic Analysis of Cattle Tick Rhipicephalus (Boophilus) microplus Saliva: A Comparison between Partially and Fully Engorged Females

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