Mutations in DIIS5 and the DIIS4-S5 linker of Drosophila melanogaster sodium channel define binding domains for pyrethroids and DDT

A - Papers appearing in refereed journals

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. and Williamson, M. S. 2007. Mutations in DIIS5 and the DIIS4-S5 linker of Drosophila melanogaster sodium channel define binding domains for pyrethroids and DDT. FEBS Letters. 581 (28), pp. 5485-5492.

AuthorsUsherwood, 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. and Williamson, M. S.
Abstract

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. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

KeywordsBiochemistry & Molecular Biology; Biophysics; Cell Biology
Year of Publication2007
JournalFEBS Letters
Journal citation581 (28), pp. 5485-5492
Digital Object Identifier (DOI)doi:10.1016/j.febslet.2007.10.057
PubMed ID17991435
Open accessPublished as non-open access
Funder project or codeCentre for Sustainable Pest and Disease Management (PDM)
ISSN00145793
PublisherWiley

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