Transcript analysis and expression profiling of three heat shock protein 70 genes in the ectoparasitoid Habrobracon hebetor (Hymenoptera: Braconidae).

Heat shock proteins (HSPs) are known as chaperones that help with folding of other proteins when cells are under environmental stresses. The upregulation of HSPs is essential for cold survival during insect diapause. The ectoparasitoid Habrobracon hebetor, a potential biological control agent, can enter reproductive diapause when reared at low temperature and short photoperiod. However, the expression of HSPs during diapause of H. hebetor has not been studied. In this study, we sequenced and characterized the full-length complementary DNAs of three Hsp70 genes (HhHsp70I, HhHsp70II and HhHsp70III) from H. hebetor. Their deduced amino acid sequences showed more than 80% identities to their counterparts from other insect species. However, the multiple sequence alignment among the three deduced amino acid sequences of HhHsp70s showed only 46% identities. A phylogenetic analysis of the three HhHsp70s and all other known Hsp70 sequences from Hymenoptera clustered all the Hsp70s into four groups, and the three HhHsp70s were distributed into three different groups. Real-time quantitative polymerase chain reaction analysis showed that the expression of the three HhHsp70 genes in H. hebetor reared at different conditions was quite different. HhHsp70I showed higher relative expression when H. hebetor were reared at 27.5°C than at two lower temperatures (17.5°C and 20°C) regardless of the photoperiod, whereas HhHsp70II showed higher expression when H. hebetor were reared at 20°C and 10 : 14 L : D than when reared at 17.5°C and either 16 : 8 L : D or 10 : 14 L : D. In contrast, HhHSP70III was expressed at similar levels regardless of the rearing conditions. These results may suggest functional differences among the three HhHsp70 genes in H. hebetor.