Abstract

The development of insects is critically affected by temperature, which therefore plays an important role in the control of stored grain pests. Extreme temperature stress conditions lead to biological responses in mites, such as the synthesis of heat shock proteins. Tyrophagus putrescentiae (Tp) is a pest mite in stored grain that has negative effects on both economy and health. Since T. putrescentiae population dynamics are strongly influenced by temperature, in the present study we have cloned the cDNA of HSP70 and HSP90 (referred to as TpHSP70-1, TpHSP70-2 and TpHSP90) and determined their expression by fluorescence real time quantitative PCR. TpHSP70 and TpHSP90 showed high homology with similar genes in other species and the open reading frames of TpHSP70-1, TpHSP70-2 and TpHSP90 encoded proteins of 665, 661 and 718 amino acid residues, respectively. Under thermal stress, expression of TpHsp70-1 and TpHsp90 was up-regulated at higher temperatures, suggesting their role in the defense against thermal stress.

Highlights

  • The development of insects is critically affected by temperature, which plays an important role in the control of stored grain pests

  • We found that TpHSP70-1 and TpHSP70-2 failed to express, consistent with Heat shock proteins (Hsps)[70] expression results in T. cinnabarinus[24,28], P. citri[24] and D. melanogaster[19]

  • The expression of T. putrescentiae TpHSP70-1 and TpHSP90 genes was up-regulated at higher temperatures and improved heat resistance

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Summary

Introduction

The development of insects is critically affected by temperature, which plays an important role in the control of stored grain pests. Heat shock proteins (Hsps) are molecular chaperones with crucial roles in protein folding and unfolding, aggregation, degradation and ­transport[18]. They are important for the insect survival under thermal ­stress[17,19]. In Panonychus citri, the three Hsp[70] proteins were expressed under cold shock, only Hsp[70-2] was up-regulated under heat shock, whereas Hsp[90] gene was expressed under high temperature stress, suggesting that both Hsp[90] and Hsp[70-2] proteins play an important role in the adaptation to high ­temperatures[22,23]. These results suggest that Hsps play an important role in improving heat resistance of mites

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