Characterization of glutathione S-transferase of the rice leaffolder moth, Cnaphalocrocis medinalis (Lepidoptera: Pyralidae): Comparison of its properties of glutathione S-transferases from other lepidopteran insects

Yamamoto, Kohji; Teshiba, Satoshi; Aso, Yoichi

doi:10.1016/j.pestbp.2008.07.005

Cited by 5 publications

(4 citation statements)

References 30 publications

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“…The activities of GSTs from each population were highest at 371C, which is congruent with reports for Cnaphalocrocis medinalis (Yamamoto et al, 2008) and S. invicta (Valles et al, 2003). Each population tested was characterized by a pH optimum of 7.5, similar to that quantified for H. cunea (Yamamoto et al, 2007) and various field populations of L. paeta ).…”

Section: Discussionsupporting

confidence: 84%

“…The GST kinetic constants for the four field populations of B. dorsalis toward CDNB and GSH were comparable to values reported from several insect species (Valles et al, 2003;Yamamoto et al, 2008;Dou et al, 2009;Wu et al, 2009). With CDNB as the substrate, the K m values of the purified GSTs in the DG and HN populations are significantly higher than those for the GZ and YN populations, suggesting a lower affinity of GSTs toward the substrates in the DG and HN populations of B. dorsalis.…”

Section: Discussionsupporting

confidence: 76%

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Purification and biochemical characterization of glutathione S‐transferases from four field populations of Bactrocera dorsalis (Hendel) (Diptera: Tephritidae)

Dou

Wang

et al. 2011

Arch Insect Biochem Physiol

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Glutathione S-transferases (GSTs) are a group of detoxification enzymes that catalyze the nucleophilic addition of glutathione to a wide variety of endogenous and xenobiotic compounds. In this study, GSTs were purified from four field populations of Bactrocera dorsalis with different insecticide susceptibilities by glutathione-agarose affinity chromatography. The populations were collected from Dongguan (DG) and Guangzhou (GZ) of the Guangdong Province, Haikou of the Hainan province (HN), and Kunming of the Yunnan province (YN), China. Differences in GST characteristics among the four populations were studied using purified enzyme samples through comparative SDS-PAGE, kinetic, and inhibition experiments. The specific activities of the purified enzymes were similar, but the purification yield of the GZ population (31.54%) was the lowest. SDS-PAGE analysis showed only one band at approximately 23 kDa for these four populations. Kinetic analyses showed that the affinities of the purified GSTs from the GZ and YN populations for 1-chloro-2.4-dinitrobenzene (CDNB) were much higher than those of GSTs from the other two populations, whereas the HN population had the highest catalytic capability in terms of V(max) value. The optimum temperature for CDNB conjugation was 37 °C and the optimum pH was 7.5 in all four populations. Inhibition kinetics showed that ethacrynic acid, diethyl maleate, tetraethylthiuram disulfide, curcumin, bromosulfalein, and β-cypermethrin had excellent inhibitory effects on GSTs in the four populations of B. dorsalis, but the low inhibitory effects of malathion and avermectin did not differ between populations. These results suggest that GSTs may have a role in detoxification of β-cypermethrin in B. dorsalis.

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Section: Discussionsupporting

confidence: 84%

Section: Discussionsupporting

confidence: 76%

Purification and biochemical characterization of glutathione S‐transferases from four field populations of Bactrocera dorsalis (Hendel) (Diptera: Tephritidae)

Dou

Wang

et al. 2011

Arch Insect Biochem Physiol

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“…Each stage was characterized by a temperature optimum of 37 °C. Similar phenomena were also recorded for B. dorsalis (Hu et al 2011), the red imported fire ant, Solenopsis invicta Buren (Hymenoptera: Formicidae) (Valles et al 2003) and the rice leaf roller Cnaphalocrocis medinalis Guenée (Lepidoptera: Crambidae) (Yamamoto et al 2008); and the GST activities varied slightly at lower temperatures in the larvae and adults but varied more in the pupae. This may be because fruit fly pupae live in the soil, where the environmental temperature was relatively stable, and, therefore, the pupae are more sensitive to temperature changes.…”

Section: Discussionsupporting

confidence: 70%

Purification and Biochemical Characterization of Glutathione S-Transferases inBactrocera minax(Diptera: Tephritidae)

Chen¹,

Dou²,

Hu³

et al. 2012

Florida Entomologist

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“…GSTs have been shown to involve in the detoxification of several chemical classes of insecticides, i.e., OPs (organophosphates; Alias and Clark 2010;Sonoda and Igaki 2010), pyrethroids (Yamamoto et al 2008(Yamamoto et al , 2009, organochlorines (Ranson et al 2001), and IGRs (insect growth regulators; Sonoda and Tsumuki 2005). Moreover, GSTs-based resistance to insecticides was observed to be facilitated with the increase in the level of GSTs activity, while the responsible molecular genetic mechanisms for this upregulation of activity were gene amplification or overexpression (Li et al 2007).…”

Section: Introductionmentioning

confidence: 99%

Purification and partial characterization of glutathione S-transferases from three field populations of Panonychus citri (Acari: Tetranychidae)

et al. 2011

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Glutathione S-transferases (GSTs) play central roles in phase II detoxification of both xenobiotics (drugs, insecticides, and herbicides) and endogenous compounds in almost all living organisms. In this study, we successfully purified the GSTs from the citrus red mite, Panonychus citri, by affinity chromatography on Glutathione Sepharose 4B and compared the biochemical characterizations of the purified GSTs from three field populations [beibei (BB), wanzhou (WZ), and zhongxian (ZX)]. SDS-PAGE revealed that the molecular weight of GSTs from three populations consisted of two subunits of 27.3 and 26.1 kDa. The specific activity of the purified GSTs from the WZ and ZX populations was increased 1.5- and 3.8-fold, respectively, compared with the BB population. Accordingly, the pyridaben susceptibility of WZ and ZX populations was less compared with BB population. Kinetic analyses showed that the WZ and ZX populations had higher substrate specificity compared with the BB population based on the values of k (cat) and k (cat) /K (m) to both reduced glutathione (GSH) and 1-chloro-2,4-dinitrobenzene (CDNB). The in vitro inhibition studies of GSTs indicated that the I (50) values of pyridaben from WZ and ZX populations of P. citri expressed 1.6- and 4.4-fold decreases, respectively, compared to the I (50) value of pyridaben from the BB population. In conclusion, all evidence suggested that the purified GSTs may partially contribute to the susceptibility of acaricide pyridaben in field populations of P. citri.

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Characterization of glutathione S-transferase of the rice leaffolder moth, Cnaphalocrocis medinalis (Lepidoptera: Pyralidae): Comparison of its properties of glutathione S-transferases from other lepidopteran insects

Cited by 5 publications

References 30 publications

Purification and biochemical characterization of glutathione S‐transferases from four field populations of Bactrocera dorsalis (Hendel) (Diptera: Tephritidae)

Purification and biochemical characterization of glutathione S‐transferases from four field populations of Bactrocera dorsalis (Hendel) (Diptera: Tephritidae)

Purification and Biochemical Characterization of Glutathione S-Transferases inBactrocera minax(Diptera: Tephritidae)

Purification and partial characterization of glutathione S-transferases from three field populations of Panonychus citri (Acari: Tetranychidae)

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