Sustaining induced heat shock protein 70 confers biological thermotolerance in a high-temperature adapted predatory mite Neoseiulus barkeri (Hughes).

Abstract

In fluctuating climatic environments, heat acclimation in predatory mites is a superior adaptation strategy for effective agricultural pest management and can be used to enhance the abilities critical in biological control efficiency. We investigated the regulatory mechanism governing the remarkable plastic response of thermotolerance in a high-temperature adapted strain (HTAS) and discerned the differences in the defensive reactions between the HTAS and the conventional strain (CS) in the predatory mite Neoseiulus barkeri. At 42 °C, the relative expression levels of four identified HSP70 genes increased rapidly in both N. barkeri strains; meanwhile the expression of NbHSP70-1 and NbHSP70-2 in CS sharply decreased after 4 h, displaying a distinct contrast with the remaining elevated expression in HTAS. Western blot analysis showed that the protein level of NbHSP70-1 in CS was dramatically elevated at 0.5 h and decreased at 6 h at 42 °C. Conversely, in HTAS, NbHSP70-1 was constantly induced and peaked at 6 h at 42 °C. Furthermore, HSP70 suppression by RNAi knockdown had a greater influence on the survival of HTAS, causing a higher mortality under high temperature than CS. Finally, the recombinant exogenous NbHSP70-1 protein enhanced the viability of E. coli BL21 under a lethal temperature of 50 °C. Sustained accumulation of HSP70 proteins results in predatory phytoseiid mites with the thermotolerance advantage that could promote their biological control function to pests. The divergent constitutive regulation of HSP70 to a thermal environment is conducive to the flexible adaptability of predators in the higher trophic level to trade off under extremely adversity stress.