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Induced expression of three heat shock proteins mediated by thermal stress in Heortia vitessoides (Lepidoptera: Crambidae)

To gain an insight into the function of heat shock proteins (HSPs) in insects during thermal stress, three HSP cDNAs were identified in the transcriptome of adult Heortia vitessoides, one of the most destructive defoliating pests in Aquilaria sinensis (Loureiro) Sprenger forests. The open reading frames of HvHsp60, HvHsp70, and HvHsp90 were 1,719, 2,070, and 2,151 bp in length, respectively, and encoded proteins with molecular weights of 61.05, 75.02, and 82.23 kDa, respectively. Sequence analysis revealed that all three HSPs were highly conserved in structure. Regarding the stage‐specific expression profiles, HvHsp60, HvHsp70, and HvHsp90 mRNAs were detected in all developmental stages. Regarding the tissue‐specific expression profiles, the expression levels of the three HSP genes were different in various larval and adult tissues. Moreover, the expression patterns of heat‐stressed larvae, pupae, and adults indicated that HvHsp60, HvHsp70, and HvHsp90 were heat‐inducible. In particular, HvHsp60 transcripts increased dramatically in larvae and pupae that were heat‐stressed at 40°C and were upregulated in adults that were heat‐stressed at 35°C and 40°C. The expression of HvHsp70 significantly increased in all of the three different developmental stages at 35°C, 40°C, and 45°C. The expression of HvHsp90 obviously increased at 30°C, 35°C, and 40°C in larvae and could be induced at 35°C in pupae and adults. The results suggest that HSP60, HSP70, and HSP90 play a major role in protecting H. vitessoides against high‐temperature stress.