The heat shock proteins (Hsp) play an important role in protein folding and protection of cells from stress. To investigate the role of Hsp90 in silk-producing insect Antheraea pernyi (Lepidoptera: Saturniidae), a full-length cDNA encoding Hsp90 from A. pernyi was cloned, sequenced and characterized. The complete cDNA (2,482 bp) contained a 2,154 bp open reading frame encoding 717 amino acid residues and had 94.5% identity with Antheraea yamamai Hsp90. The relative expression levels of Hsp90 in five different tissues at normal and high temperatures were evaluated with real-time fluorescence quantitative RT-PCR. The expression of Hsp90 was obviously changed in the examined tissues except for fat bodies after induced by high temperature. SDS-PAGE of purified protein demonstrated that an 86 KD recombinant protein was successfully expressed in transformed Escherichia coli cells. These results shed light on studying the mechanism of tolerance in A. pernyi.Key words: Antheraea pernyi, HSP90, sequence analysis, expression
