Characterization and functional analysis of Cshsp19.0 encoding a small heat shock protein in Chilo suppressalis (Walker)

Int J Biol Macromol. 2021 Oct 1:188:924-931. doi: 10.1016/j.ijbiomac.2021.07.186. Epub 2021 Aug 2.

Abstract

Small heat shock proteins (sHSPs) function as ATP-independent chaperones that preserve cellular proteostasis under stressful conditions. In this study, Cshsp19.0, which encodes a new small heat shock protein, was isolated and characterized from Chilo suppressalis (Walker) to better understand the contribution of sHSPs to insect development and stress tolerance. The full-length Cshsp19.0 cDNA was 697 bp and encoded a 19.0 kDa protein with an isoelectric point of 5.95. Phylogenetic analysis and amino acid alignments indicated that Cshsp19.0 is a member of the sHSP family. Cshsp19.0 was expressed at maximal levels in foreguts and showed the least amount of expression in fat bodies. Expression analysis in different developmental stages of C. suppressalis revealed that Cshsp19.0 was most highly expressed in 1st instar larvae. Furthermore, Cshsp19.0 was upregulated when insects were exposed to heat and cold stress for a 2-h period. There were significant differences in the male and female pupae in response to humidity; Cshsp19.0 expression increased in male pupae as RH increased, whereas the inverse pattern was observed in female pupae. Larvae exhibited a lower rate of survival when Cshsp19.0 was silenced by a nanomaterial-promoted RNAi method. The results confirm that Cshsp19.0 functions to increase environmental stress tolerance and regulates physiological activities in C. suppressalis.

Keywords: Chilo suppressalis; Gene expression; Humidity; RNA interference; Small heat shock protein (sHSP); Temperature.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Gene Expression Profiling
  • Gene Expression Regulation, Developmental
  • Heat-Shock Proteins, Small / metabolism*
  • Humidity
  • Moths / genetics
  • Moths / metabolism*
  • Phylogeny
  • RNA Interference
  • Sequence Homology, Amino Acid
  • Temperature

Substances

  • Heat-Shock Proteins, Small