A unique mechanism of transfluthrin action revealed by mapping its binding sites in the mosquito sodium channel.

Pyrethroid insecticides exert their toxic action by prolonging the opening of insect voltage-gated sodium channels, resulting in the characteristic tail current during membrane repolarization in voltage clamp experiments. Permethrin (PMT) and deltamethrin (DMT), representative type I and type II pyrethroids, respectively, are predicted to bind to two lipid-exposed pyrethroid receptor sites, PyR1 and PyR2, at the lipid-exposed interfaces of repeats II/III and I/II, respectively. Transfluthrin (TF), a volatile type I pyrethroid and mosquito repellent, has received increased attention in the global combat of vector-borne human diseases.