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Mutations in DIIS5 and the DIIS4–S5 linker of Drosophila melanogaster sodium channel define binding domains for pyrethroids and DDT
Author(s) -
Usherwood P.N.R.,
Davies T.G.E.,
Mellor I.R.,
O'Reilly A.O.,
Peng F.,
Vais H.,
Khambay B.P.S.,
Field L.M.,
Williamson M.S.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.10.057
Subject(s) - pyrethroid , potency , sodium channel , deltamethrin , xenopus , drosophila melanogaster , linker , mutant , chemistry , permethrin , voltage clamp , biology , sodium , stereochemistry , biochemistry , in vitro , pesticide , membrane potential , organic chemistry , gene , computer science , agronomy , operating system
Mutations in the DIIS4–S5 linker and DIIS5 have identified hotspots of pyrethroid and DDT interaction with the Drosophila para sodium channel. Wild‐type and mutant channels were expressed in Xenopus oocytes and subjected to voltage‐clamp analysis. Substitutions L914I, M918T, L925I, T929I and C933A decreased deltamethrin potency, M918T, L925I and T929I decreased permethrin potency and T929I, L925I and I936V decreased fenfluthrin potency. DDT potency was unaffected by M918T, but abolished by T929I and reduced by L925I, L932F and I936V, suggesting that DIIS5 contains at least part of the DDT binding domain. The data support a computer model of pyrethroid and DDT binding.