Manas Sarkar^1,2 , Aparajita Borkotoki¹

1. Department of Zoology, Gauhati University, Guwahati, Assam-781014, India
2. Research & Development (Advance Technology and Innovation), Godrej Consumer Products Ltd., Pirojshanagar, Mumbai-400079, India
Author    Correspondence author
Journal of Mosquito Research, 2015, Vol. 5, No. 23   doi: 10.5376/jmr.2015.05.0023
Received: 16 Sep., 2015    Accepted: 04 Nov., 2015    Published: 24 Nov., 2015

This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

 Sarkar M., and Borkotoki A., 2015, In Silico modeling of voltage-gated sodium channel alpha subunit to understand insecticide binding simulation in mosquitoes, Journal of Mosquito Research, 5(23): 1-8 (doi: 10.5376/jmr.2015.05.0023)

The Voltage Gated Sodium Channel (VGSC) is critical for binding of different insecticides and play key role in insecticide resistance. An important mechanism of resistance to DDT and pyrethroids is termed knockdown resistance (kdr), caused by mutations in IIS6 domain of sodium channels. To attain a better management strategy for insecticide resistance and screening of new insecticide molecules, it is important to understand the three-dimensional structure of insecticide-binding domain of VGSC and its molecular interaction with insecticides. We constructed a theoretical model of ion transport domain–II of VGSC from mosquitoes, Culex quinquefasciatus. The stereochemistry of the model shows 91.1% residues are in the most favored region. Docking studies with DDT and deltamethrin indicated that deltamethrin showed interaction with Thr⁹²⁹, Met⁹¹⁸, Ile⁹³⁶, Cys⁹³³, Leu⁹²⁵, Glu⁸⁸¹, Met⁸⁵⁷ and Gly⁸⁶⁶ and DDT showed interaction with Ile⁹³⁶, Thr⁹²⁹, Ser⁸⁷⁸, Phe⁸⁶³, Gln⁸⁶⁴, Trp⁸⁶¹ and Met⁸⁵⁷. We also predicted that mutation of Thr⁹²⁹ should confer resistance to both DDT and deltamethrin. 

Insecticide resistance; in silico modeling; Knockdown resistance; Docking; Kdr mutation