The glutathione S-transferases (GSTs)
are important
detoxifying enzymes in insects. Our previous studies found that the
susceptibility of Chilo suppressalis to abamectin was significantly increased when the CsGST activity
was inhibited by glutathione (GSH) depletory. In this study, the potential
detoxification mechanisms of CsGSTs to abamectin were explored. Six
CsGSTs of C. suppressalis were expressed in vitro. Enzymatic kinetic parameters including K
m and V
max of recombinant
CsGSTs were determined, and results showed that all of the six CsGSTs
were catalytically active and displaying glutathione transferase activity.
Insecticide inhibitions revealed that a low concentration of abamectin
could effectively inhibit the activities of CsGSTs including CsGSTd1,
CsGSTe4, CsGSTo2, CsGSTs3, and CsGSTu1. However, the in vitro metabolism assay found that the six CsGSTs could not metabolize
abamectin directly. Additionally, the glutathione transferase activity
of CsGSTs in C. suppressalis was significantly
increased post-treatment with abamectin. Comprehensive analysis of
the results in present and our previous studies demonstrated that
CsGSTs play an important role in detoxification of abamectin by catalyzing
the conjugation of GSH to abamectin in C. suppressalis, and the high binding affinities of CsGSTd1, CsGSTe4, CsGSTo2, CsGSTs3,
and CsGSTu1 with abamectin might also suggest the involvement of CsGSTs
in detoxification of abamectin via the noncatalytic
passive binding and sequestration instead of direct metabolism. These
studies are helpful to better understand the detoxification mechanisms
of GSTs in insects.