Enzymatic characterization of insecticide resistance mechanisms in field populations of Malaysian Culex quinquefasciatus say (Diptera: Culicidae)

PLoS One. 2013 Nov 21;8(11):e79928. doi: 10.1371/journal.pone.0079928. eCollection 2013.

Abstract

Background: There has been no comprehensive study on biochemical characterization of insecticide resistance mechanisms in field populations of Malaysian Culex quinquefasciatus. To fill this void in the literature, a nationwide investigation was performed to quantify the enzyme activities, thereby attempting to characterize the potential resistance mechanisms in Cx. quinquefasciatus in residential areas in Malaysia.

Methodology/principal findings: Culex quinquefasciatus from 14 residential areas across 13 states and one federal territory were subjected to esterases, mixed function oxidases, glutathione-S-transferase and insensitive acetylcholinesterase assays. Enzyme assays revealed that α-esterases and β-esterases were elevated in 13 populations and 12 populations, respectively. Nine populations demonstrated elevated levels of mixed function oxidases and glutathione-S-transferase. Acetylcholinesterase was insensitive to propoxur in all 14 populations. Activity of α-esterases associated with malathion resistance was found in the present study. In addition, an association between the activity of α-esterases and β-esterases was also demonstrated.

Conclusions/significance: The present study has characterized the potential biochemical mechanisms in contributing towards insecticide resistance in Cx. quinquefasciatus field populations in Malaysia. Identification of mechanisms underlying the insecticide resistance will be beneficial in developing effective mosquito control programs in Malaysia.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / metabolism*
  • Animals
  • Culex / enzymology*
  • Esterases / metabolism*
  • Glutathione Transferase / metabolism*
  • Insecticide Resistance*
  • Mixed Function Oxygenases / metabolism*

Substances

  • Mixed Function Oxygenases
  • Glutathione Transferase
  • Esterases
  • Acetylcholinesterase

Grants and funding

This study was supported by the University of Malaya Research Grant (RG164/12SUS). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.