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Biochemical basis of insecticide resistance in the white backed plant hopper, sogatella furcifera (horvath) infesting rice

Author: 
Suri, K. S., Khetrapal, V. and Sangha, M. K.
Subject Area: 
Life Sciences
Abstract: 

The whitebacked planthopper, (Sogatella furcifera (Horvath) is a major threat to rice crops throughout Asia, damaging plants both through its feeding behavior and by acting as a vector. Due to high insecticide pressure, it is becoming resistant to many insecticides. Many enzymes are known to be involved in providing resistance to these planthoppers against insecticides. Fewer research investigations have been conducted on insecticide resistance in relation to WBPH The objective of this paper was to evaluate the biochemical basis of resistance probably by evolving new isoforms of insecticide detoxifying enzymes. Biochemical profile of esterase, acetylcholinesterase and glutathione S-transferase (GST) was assessed. No difference in the glutathione-S-transferase activity was seen in buprofezin and quinalphos, however significant increase in GST activity was seen in chlorntraniliprole resistant insects. Buprofezin was highly toxic as compared to quinalphos and chlorntraniliprole. Esterase (30.82 µg of napthol formed/min/mg of insect) and acetylcholinesterase (17.23 µg of glutathione formed/min/mg of insect activity) was higher in quinalphos. The results indicate the potential development of esterases as detoxification mechanisms responsible for resistance to buprofezin and quinalphos. Esterase isozyme profiling using native PAGE shows dark bands in Buprofezin and quinalphos however diffused light bands were observed in case of chlorntraniliprole, indicate GST as the principal enzyme for detoxification of chlorntraniliprole.

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