Guoxing Quan
Great Lakes Forestry Centre, Canada
Title: Molecular cloning and characterization of the small heat shock protein family in the spruce budworm, Choristoneura fumiferana
Biography
Biography: Guoxing Quan
Abstract
Small heat shock proteins are a superfamily of molecular chaperones and are characterized by the presence of a conserved α-crystallin domain. They exhibit ATP-independent chaperone-like activity by assisting in the correct folding of nascent and stress-accumulated misfolded protein to prevent irreversible protein aggregation. Unlike HSPs of large molecular weight, the sHSPs display structural and functional diversity among different insect species. Some sHSPs may contribute to stress tolerance, enhancing insect survival in severe environmental conditions. As such, studying SHSPs may lead to a better understanding of how pest insect survives in unfavorable environments and how the changing climate affects their distribution and outbreaks. The spruce budworm, C. fumiferana is a destructive native forest defoliator in North America. In the past few hundred years, periodic outbreaks are known to have occurred across tens of millions of square kilometers of forest. Here, we report the identification of 15 sHSP genes from the spruce budworm transcriptome. Examination of the mRNA expression profiles of the sHSPs revealed that the levels varied according to the developmental stage and tissue as well as whether the insects were reared under normal and stress conditions. Nine sHSP genes were sensitive to heat shock stress. Some, but not all, sHSPs may play a vital role during diapause.