Characterization of a novel superoxide dismutase in Nilaparvata lugens.

The brown planthopper (Nilaparvata lugens) is a major agricultural pest of rice crops. Analysis of the enzymes produced by N. lugens is important to develop pest-control methods. Superoxide dismutase (SOD) is a detoxification enzyme that catalyzes the conversion of superoxide anions (reactive oxygen species) into oxygen and hydrogen peroxide. As there have been no reports on SOD in N. lugens, in this study, we characterized a new SOD in the brown planthopper, nlSOD1. Amino acid sequence and phylogenetic analyses revealed that nlSOD1 is a member of the Cu/Zn-SOD family. Recombinant nlSOD1, when overexpressed in Escherichia coli, catalyzes the dismutation of superoxide radicals into molecular O2 and H2 O2 . Exposure to various insecticides induced nlSOD1 messenger RNA expression. These results indicate that nlSOD1 may contribute to the insecticide resistance of N. lugens. The findings of this study may assist in the development of novel methods to control the population of N. lugens.

Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning.

Glutathione transferase (GST) is an important class of detoxification enzymes that are vital for defense against various xenobiotics and cellular oxidative stress. Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazinon. In this study, we aimed to identify the amino acid residues that constitute a hydrogen-bonding network important for GST activity. Site-directed mutagenesis of bmGSTu2 suggested that residues Asn102, Pro162, and Ser166 contribute to its catalytic activity.