Evolutionary and functional characterization of oxidative stress proteins in dendroctonus ponderosae hopkins (curculionidae: scolytinae)

Understanding the mountain pine beetle detoxification systems is vital for predicting its continued spread into the novel jack pine host. Phylogenetic analyses were conducted for mountain pine beetle catalase, glutathione peroxidase, superoxide dismutase, and peroxiredoxin. These proteins were generally conserved, but there were differences in some key functional motifs. Specifically, a peroxiredoxin (DPPrx1) contained a unique combination of hyperoxidation motifs. DPPrx1 and a superoxide dismutase (DPSOD1) were selected for further functional analyses and demonstrated higher reactivity when compared to other SOD and Prx proteins. Also, DPPrx1 experiences hyperoxidation at a lower H2O2 concentration (~0.06 mM) than human peroxiredoxin (~0.12 mM). In other systems, hyperoxidized peroxiredoxin does act as a signal molecule for the expression of other oxidative stress proteins. Therefore, due to its relatively high reactivity and potential role as a cellular signal, DPPrx1 could serve as a future pest management target.