Molecular characterization and expression analysis of heat shock protein 70 and 90 from Hermetia illucens reared in a food waste bioconversion pilot plant.

Two full-length cDNAs of heat shock protein (HSP) genes (Hihsp70 and Hihsp90) were cloned from the black soldier fly (BSF) Hermetia illucens larvae reared in a food waste bioconversion pilot plant. The Hihsp70 and Hihsp90 transcripts were 2243 and 2507bp long, contained 1923 and 2166bp open reading frames encoding proteins of 640 and 721 amino acids with a molecular mass of 69.8 and 83kDa, respectively. Comparative analysis of protein sequences revealed the presence of the conserved HSP motifs in both proteins, showing high homology to their counterparts in other insect species from six different orders. Hihsp70 and Hihsp90 transcriptional expression profiles during two key developmental stages in the bioconversion process were evaluated by quantitative real time PCR showing that both genes were modulated during larval development. HiHsp70 mRNA expression levels during the II instar larvae was higher in respect to the V instar larvae. A similar difference in mRNA expression levels, but in a less extent, was found for the Hihsp90. Moreover, a diverse transcript level between the two genes at the V larval stage was observed where Hihsp90 was up-regulated compared to Hihsp70. These results suggested the involvement of Hsp70 and Hsp90 in H. illucens development and provide further evidences on the ecological and evolutionary importance of HSPs in the insect developmental processes together with valuable information on molecular features of adaptability to peculiar rearing conditions during food waste bioconversion.
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