The HSP/co-chaperone network in environmental cold adaptation of Chilo suppressalis

Winter cold is one of the major environmental stresses for ectotherm species. Chilo suppressalis, a notorious lepidopteran pest of rice, has a wide geographic region that includes temperate zones with severe environmental conditions. Although C. suppressalis exhibits remarkable cold tolerance, its cold-adaptation mechanisms remain unclear. Here, we used bioinformatics approaches to evaluate transcript levels of genes comprising the C. suppressalis heat shock protein (HSP)/co-chaperone network in response to cold-induced stress. Using all such genes identified in the C. suppressalis genome, we experimentally examined the corresponding transcript levels under cold-acclimation or intermittent cold-shock stresses in diapause and non-diapausing larvae. In total, we identified 19 HSPs and 8 HSP co-chaperones in the C. suppressalis genome. Nine (hsp90, hsp75, hsp70, hsp40, small hsp, activator of 90 kDa heat shock protein ATPase-like, heat shock factor, heat shock factor binding protein 1-like and HSPB1-associated protein 1) were highly cold-inducible and likely comprise the principal cold-response HSP/co-chaperone network in C. suppressalis. We also found that transcriptional regulation of the HSP/co-chaperone networks response differs between cold-acclimation and short-term cold-shock. Moreover, activation of the HSP/co-chaperone network depends on the diapause state of overwintering larvae and cold acclimation may further increase larval cold tolerance. These results provide key new insights in the cold-adaptation mechanisms in C. suppressalis.