RRC ID 57004
Author Yamamoto K, Higashiura A, Hirowatari A, Yamada N, Tsubota T, Sezutsu H, Nakagawa A.
Title Characterisation of a diazinon-metabolising glutathione S-transferase in the silkworm Bombyx mori by X-ray crystallography and genome editing analysis.
Journal Sci Rep
Abstract Previously, we found an unclassified glutathione S-transferase 2 (bmGSTu2) in the silkworm Bombyx mori that conjugates glutathione to 1-chloro-2,4-dinitrobenzene and also metabolises diazinon, an organophosphate insecticide. Here, we provide a structural and genome-editing characterisation of the diazinon-metabolising glutathione S-transferase in B. mori. The structure of bmGSTu2 was determined at 1.68 Å by X-ray crystallography. Mutation of putative amino acid residues in the substrate-binding site showed that Pro13, Tyr107, Ile118, Phe119, and Phe211 are crucial for enzymatic function. bmGSTu2 gene disruption resulted in a decrease in median lethal dose values to an organophosphate insecticide and a decrease in acetylcholine levels in silkworms. Taken together, these results indicate that bmGSTu2 could metabolise an organophosphate insecticide. Thus, this study provides insights into the physiological role of bmGSTu2 in silkworms, detoxification of organophosphate insecticides, and drug targets for the development of a novel insecticide.
Volume 8(1)
Pages 16835
Published 2018-11-15
DOI 10.1038/s41598-018-35207-8
PII 10.1038/s41598-018-35207-8
PMID 30443011
PMC PMC6237972
MeSH Acetylcholine / metabolism Alleles Amino Acid Sequence Animals Base Sequence Bombyx / enzymology* Bombyx / genetics* Crystallography, X-Ray Diazinon / metabolism* Electrons Gene Editing* Genome, Insect* Glutathione Transferase / chemistry* Glutathione Transferase / genetics* Mutation / genetics
IF 4.011
Times Cited 0
Silkworms w1-pnd