Characterization, and Functional Analysis of Hsp70 and Hsp90 Gene Families in Glyphodes pyloalis Walker (Lepidoptera: Pyralidae).

Jian-Hao Ding,Jun Wang,Lu-Xin Zheng,Sheng Sheng,Fu-An Wu,Xin-Hao Liang,Jie Chu,Xiao-Wen Gao

doi:10.3389/fphys.2021.753914

Abstract

Glyphodes pyloalis Walker (Lepidoptera: Pyralidae) is a destructive mulberry pest, causing great damage to mulberry in China. Heat shock proteins (Hsps) are involved in various signal pathways and regulate lots of physiological processes in insects. The function of Hsps in G. pyloalis, however, has still received less attention. Here, we identified five Hsp genes from G. pyloalis transcriptome dataset including two Hsp70 family genes (GpHsp71.3 and GpHsp74.9) and three Hsp90 family genes (GpHsp82.4, GpHsp89, and GpHsp93.4). Quantitative Real-time PCR validation revealed that all Hsps of G. pyloalis have significant expression in pupal and diapause stage, at which the larvae arrest the development. Expressions of GpHsp71.3 and GpHsp82.4 were increased significantly after thermal treatment at 40°C, and this upregulation depended on heat treatment duration. Furthermore, silencing GpHsp82.4 by RNA interference led to a significant increase in mortality of G. pyloalis larvae under the heat stress compared to the control group. After starvation stress, the expression levels of GpHsp82.4 and GpHsp93.4 were significantly increased. At last, after being parasitized by the parasitoid wasp Aulacocentrum confusum, Hsp70 and Hsp90 genes of G. pyloalis were decreased significantly in the early stage of parasitization and this moderation was affected by time post-parasitization. This study highlights the function of G. pyloalis Hsps in response to environmental stress and provides a perspective for the control of this pest.

Highlights

Heat shock protein (Hsp) is a highly conservative protein induced by extreme temperature, heavy metals, hunger, and other stresses in organisms, which can help the protein fold correctly, degrade the denatured protein, and exercise the function of molecular chaperone in the biological resistance to adverse environments (Tammariello et al, 1999)
The results showed that the parasitization by A. confusum and significantly regulated the expression levels of all candidate Hsps in G. pyloalis larvae and this moderation were affected by durations post-parasitization
The expression level of Hsps can be expressed at various developmental stages

Summary

Introduction

Heat shock protein (Hsp) is a highly conservative protein induced by extreme temperature, heavy metals, hunger, and other stresses in organisms, which can help the protein fold correctly, degrade the denatured protein, and exercise the function of molecular chaperone in the biological resistance to adverse environments (Tammariello et al, 1999). Four major families of Hsps, along with several co-chaperones, are recognised, including the small heat shock proteins (sHsps), Hsp, Hsps in Glyphodes pyloalis. Hsp and Hsp function as molecular chaperones in response to a variety of stress factors, promote proper protein folding, and prevent the aggregation of denatured protein (Feder and Hofmann, 1999). Hsps have been found to be involved in many developmental processes, including insect diapause, metamorphosis, embryogenesis, apoptosis, and autophagy (Chu et al, 2020). In Omphisa fuscidentalis, OfHsp expression increased transiently during the termination of diapause (Tungjitwitayakul et al, 2008)

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