Chimeric Investigations into the Diamide Binding Site on the Lepidopteran Ryanodine Receptor.

ABSTRACT: Alterations to amino acid residues G4946 and I4790, associated with resistance to diamide insecticides, suggests a location of diamide interaction within the pVSD voltage sensor-like domain of the insect ryanodine receptor (RyR). To further delineate the interaction site(s), targeted alterations were made within the same pVSD region on the diamondback moth (Plutella xylostella) RyR channel. The editing of five amino acid positions to match those found in the diamide insensitive skeletal RyR1 of humans (hRyR1) in order to generate a human-Plutella chimeric construct showed that these alterations strongly reduce diamide efficacy when introduced in combination but cause only minor reductions when introduced individually. It is concluded that the sites of diamide interaction on insect RyRs lie

SUBMITTER: Richardson E 

PROVIDER: S-EPMC8657592 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature