Mutational Study of Voltage-Gated Sodium Channel in Permethrin Resistance in Mosquitoes: An in silico Study

Background

Resistance to insecticides is one of the major problems in successfully controlling of mosquito-borne diseases. The present study explores the role of Voltage-Gated Sodium Channel (VGSC) and their mutation in the development of insecticide resistance in Anopheles mosquito.

Materials and Methods

Homology protein modelling of wild-type and mutated VGSC protein was performed using the Swiss-Model server. Model proteins were analyzed using different bioinformatic tools, such as Procheck, Anolea, Errat, to study the overall quality. The binding affinity of insecticide permethrin with VGSC was analyzed using Autodock Tools software.

Results and Discussion

The study observed that the model proteins have slight structural deviation between wild-type and mutant proteins. Model proteins docked with permethrin insecticide showed a higher binding affinity with wild-type than mutant channel protein. The present studies suggest that the point mutation in codon 1014 (Leucine→Cysteine) affects the complex stability, plausibly resisting the effect of the insecticide permethrin.

Conclusion

The present study proposes the molecular interaction of permethrin with the ion channel leading to the development of insecticide resistance capacity in mosquito vectors.