Point mutations in domain II of the voltage-gated sodium channel gene in deltamethrin-resistant Aedes aegypti (Diptera: Culicidae)

• Published in: Applied Entomology and Zoology Vol. 45; no. 2; pp. 275 - 282
• Main Authors: Srisawat, R., Mahidol Univ., Bangkok (Thailand), Komalamisra, N, Eshita, Y, Zheng, M, Ono, K, Itoh, T.Q, Matsumoto, A, Petmitr, S, Rongsriyam, Y
• Format: Journal Article
• Language: English
• Published: JAPANESE SOCIETY OF APPLIED ENTOMOLOGY AND ZOOLOGY 2010
• Subjects: AEDES AEGYPTI; BIOLOGIA MOLECULAR; BIOLOGIE MOLECULAIRE; DELTAMETHRIN; DELTAMETHRINE; DELTAMETRIN; http://www.fao.org/aos/agrovoc#c_25427; http://www.fao.org/aos/agrovoc#c_30482; http://www.fao.org/aos/agrovoc#c_33971; http://www.fao.org/aos/agrovoc#c_4891; http://www.fao.org/aos/agrovoc#c_5014; http://www.fao.org/aos/agrovoc#c_7575; knockdown resistance; MOLECULAR BIOLOGY; MUTACION; MUTATION; PESTICIDE RESISTANCE; PIRETRINAS SINTETICAS; point mutation; PYRETHRINE DE SYNTESE; RESISTANCE AUX PESTICIDES; RESISTENCIA A LOS PLAGUICIDAS; SYNTHETIC PYRETHRINS; voltage-gated sodium channel
• ISSN: 0003-6862; 1347-605X
• DOI: 10.1303/aez.2010.275

The continuous usage of pyrethroids against insects has provoked the emergence of insecticide resistance that has become a major obstacle to disease vector control. The knockdown resistance (kdr) voltage-gated sodium channel gene is regarded as a key to understanding the mechanism of resistance to pyrethroids. The main purpose of this study is to identify point mutations in the sodium channel gene associated with deltamethrin resistance in Aedes aegypti. Two mutations in the IIS6 domain of the channel, S989P and V1016G, were identified as possible candidates responsible for the emergence of deltamethrin resistance in Ae. aegypti Khu Bua strain. As S989P and V1016G mutations are located within the IIS5–S6 loop and IIS6 near the ion filter and binding site, these mutations might enhance pyrethroid resistance. Allelic variation in the sodium channel gene is thought to be one of the principal molecular mechanisms regulating pyrethroid resistance in mosquitoes.