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Absence of protein polymorphism attributable to insecticide-insensitivity of acetylcholinesterase in the green rice leafhopper, Nephotettix cincticeps.

Abstract
The cDNA sequence of acetylcholinesterase (AChE) from the green rice leafhopper, Nephotettix cincticeps, was amplified, based on conserved peptide sequences of AChEs. A 2.3 kb contiguous sequence, containing an ORF encoding an AChE precursor with 677 amino acid residues was obtained. The deduced protein sequence showed the most similarity to that of AChE in the Colorado potato beetle, having common features in the primary AChE structure. cDNA sequences of individual leafhoppers from an insecticide susceptible strain and the resistant strain Nakagawara, whose methylcarbamate-insensitive AChEs show 10(2) or more I(50) ratio for propoxur, were compared. No fixed inter-strain difference was identified in the protein sequence, though amino acid substitution polymorphism was found at one position in the susceptible strain. Insecticide-insensitivity of leafhopper AChE does not result from changes in the protein primary structure that is encoded by the AChE gene sequence isolated in this study.
AuthorsT Tomita, O Hidoh, Y Kono
JournalInsect biochemistry and molecular biology (Insect Biochem Mol Biol) Vol. 30 Issue 4 Pg. 325-33 (Apr 2000) ISSN: 0965-1748 [Print] England
PMID10727899 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • DNA, Complementary
  • Insecticides
  • Propoxur
  • Acetylcholinesterase
Topics
  • Acetylcholinesterase (genetics)
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • DNA, Complementary
  • Insecta (enzymology, genetics)
  • Insecticide Resistance (genetics)
  • Insecticides
  • Molecular Sequence Data
  • Polymorphism, Genetic
  • Propoxur
  • Sequence Homology, Amino Acid

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