Cloning and Expression Analysis of Four Heat Shock Protein Genes in Ericerus pela (Homoptera: Coccidae)

Abstract

To explore the function of small heat shock protein genes ( shsp s) and hsp70 in Ericerus pela , we cloned the full-length cDNA sequences of hsp21.5 , hsp21.7 , hsp70 , and hsc70 and the genomic sequence of hsc70 . Open reading frames of the four hsp s were 570, 564, 1,908, and 1,962 base pairs (bp), respectively, which encode proteins with calculated molecular mass of 21.5, 21.7, 69.8, and 71.6 kDa. Amino acid sequence analysis revealed the presence of the conserved Hsp motifs in all four proteins. The genomic DNA of hsc70 had four introns. ep-hsp21.5 was orthologous and ep-hsp21.7 was species specific. Expression of all four transcripts during heat or cold stress and development was examined by quantitative real-time polymerase chain reaction. All four hsp s were upregulated during heat or cold stress in female adults, indicating a correlation between the four hsp s and heat or cold-stress tolerance in female adults. ep-hsp21.7 and ep-hsp70 were upregulated during heat stress in male larvae, implying a correlation between the two hsp s and heat-stress tolerance in male larvae. The four ep-hsp s were also upregulated during the developmental process in males, and ep-hsp21.5 , ep-hsp70 , and ep-hsc70 were upregulated in females, which indicates their possible role in the developmental regulation of E. pela .

Comparative proteome analysis and thermal stress induced changes in the embryo of poly- and bi-voltine strains of Bombyx mori

“…In addition, genome-wide analysis while explicit the presence of 16 HSPs in the embryo of B. mori [23], the mRNA level as a fact of gene expression measured quantitatively was not correlated with the amount of HSPs synthesized [24] where they facilitate embryo development and metabolism by ensuing proteins properly folded and protecting against their denaturation [15] as reported in the present study. Augmenting, the expression of HSPs measured in larval and adult stages was also found higher than the egg stage of Ericerus pela [22] and HS in Drosophila eggs did not induce HSPs in early developmental stages [19]. The molecular mechanism in differential expression of HSPs in different developmental stages in the life cycle of any insects still remains obscure but shall be correlated with sensitivity of the embryo to a HS that lead to low hatchability as recorded in the present study.…”

“…Interestingly, the expression of HSPs was not so obvious at the embryonic stage unlike larval stage of B. mori [14,21], while presence of nine HSPs was identified thorough shotgun proteomic analysis [15] which are known to involve in the basic metabolic process, but are not inducible in due to environmental stresses [22]. In addition, genome-wide analysis while explicit the presence of 16 HSPs in the embryo of B. mori [23], the mRNA level as a fact of gene expression measured quantitatively was not correlated with the amount of HSPs synthesized [24] where they facilitate embryo development and metabolism by ensuing proteins properly folded and protecting against their denaturation [15] as reported in the present study.…”

Characterization and functional analysis of hsp21.8b: An orthologous small heat shock protein gene in Tribolium castaneum

“…However, recent studies revealed that the expression patterns of the orthologous shsps among different organisms are not exactly the same, which is probably related to their different physiological characteristics. In E. pela , a species highly sexually dimorphic with holometamorphic males and hemimetabolic females, the mRNA levels of Ephsp21.5 showed the lowest expression in eggs, and in males it was maximal in adults stage and in females it reached a maximum in second‐stage larvae (Liu et al., ). This phenomenon is due to that the female insects enter the adult stage in August (hot weather), whereas the male larvae continuously keep in the second‐instar stage.…”

Transcriptomic and proteomic analyses on the supercooling ability and mining of antifreeze proteins of the Chinese white wax scale insect

“…These insects have been bred in China for over a thousand years. E. pela is widely distributed in China, the Korean Peninsula and Japan (Yang et al ., , , ; Liu et al ., ). E. pela can even survive and produce offspring in the Jilin and Xizang Provinces in China, where the lowest temperature is below ‐30°C.…”