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NADPH cytochrome P450 reductase (CPR) is essential for cytochrome P450 catalysis, which is important in the detoxification and activation of xenobiotics. In this study, two transcripts of  Bactrocera dorsalis CPR  ( BdCPR ) were cloned, and the deduced amino-acid sequence had an N-terminus membrane anchor for BdCPR-X1 and three conserved binding domains (FMN, FAD, and NADP), as well as an FAD binding motif and catalytic residues for both BdCPR-X1 and BdCPR-X2.  BdCPR-X1  was detected to have the high expression levels in adults and in Malpighian tubules, fat bodies, and midguts of adults, but  BdCPR-X2  expressed lowly in  B. dorsalis . The levels of  BdCPRs  were similar in malathion-resistant strain compared to susceptible strain. However, injecting adults with double-stranded RNA against  BdCPR  significantly reduced the transcript levels of the mRNA, and knockdown of  BdCPR  increased adult susceptibility to malathion. Expressing complete  BdCPR-X1  cDNA in Sf9 cells resulted in high activity determined by cytochrome  c  reduction and these cells had higher viability after exposure to malathion than control. The results suggest that  BdCPR  could affect the susceptibility of  B. dorsalis  to malathion and eukaryotic expression of  BdCPR  would lay a solid foundation for further investigation of P450 in  B. dorsalis .

Functional characterization of NADPH-cytochrome P450 reductase from Bactrocera dorsalis: Possible involvement in susceptibility to malathion