Abstract <p>Heat shock proteins (HSPs) is a protective protein that is highly conserved in molecular evolution, distributed in almost all organisms and abundant in insects. In this study, the small heat shock protein HSP27.4 gene was cloned from <i>Bombyx mandarina</i> (<i>Bmm</i>). Small molecule heat shock protein BmmHSP27.4 was obtained by cloning, which has an ORF length of 741 bp, encodes 246 amino acids, has a molecular mass of 27 387.34 Da, an isoelectric point of 5.86, and a coefficient of instability of 43.29; there exists signal peptide of the type SP (Sec/SPI), and the presence of a transmembrane region. The phylogenetic tree showed that <i>Bombyx mandarina</i> HSP27.4 had the highest sequence identity with <i>Bombyx mori</i> HSP27.4 and clustered into a single unit. The expression of HSP27.4 gene in different tissues of <i>Bombyx mandarina</i> larvae differed significantly, with the highest expression in the canaliculus of <i>Bombyx mandarina</i>, a higher expression in the head, and a relatively low expression in other tissues. <i>Bombyx mandarina</i> HSP27.4 responded most positively in the midgut under high and low temperature stress. mNPV induced the expression of the BmmHSP27.4 gene in the haemolymph and midgut. The transcriptional level of the BmmHSP27.4 gene was elevated in the midgut of <i>Bombyx andarina</i> eared on deltamethrin-contaminated mulberry leaves. The results suggest that BmmHSP27.4 may play an important role in the molecular mechanisms of external stress and development of <i>Bombyx mandarina</i>.</p>

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Identification and Expression Analysis of the Small Molecule Heat Shock Protein 27.4 Gene in Bombyx mandarina

  • E. Chen,
  • J. Ding,
  • Yu. Zhang,
  • Y. Qian,
  • G. Zhao,
  • H. Qian

摘要

Abstract

Heat shock proteins (HSPs) is a protective protein that is highly conserved in molecular evolution, distributed in almost all organisms and abundant in insects. In this study, the small heat shock protein HSP27.4 gene was cloned from Bombyx mandarina (Bmm). Small molecule heat shock protein BmmHSP27.4 was obtained by cloning, which has an ORF length of 741 bp, encodes 246 amino acids, has a molecular mass of 27 387.34 Da, an isoelectric point of 5.86, and a coefficient of instability of 43.29; there exists signal peptide of the type SP (Sec/SPI), and the presence of a transmembrane region. The phylogenetic tree showed that Bombyx mandarina HSP27.4 had the highest sequence identity with Bombyx mori HSP27.4 and clustered into a single unit. The expression of HSP27.4 gene in different tissues of Bombyx mandarina larvae differed significantly, with the highest expression in the canaliculus of Bombyx mandarina, a higher expression in the head, and a relatively low expression in other tissues. Bombyx mandarina HSP27.4 responded most positively in the midgut under high and low temperature stress. mNPV induced the expression of the BmmHSP27.4 gene in the haemolymph and midgut. The transcriptional level of the BmmHSP27.4 gene was elevated in the midgut of Bombyx andarina eared on deltamethrin-contaminated mulberry leaves. The results suggest that BmmHSP27.4 may play an important role in the molecular mechanisms of external stress and development of Bombyx mandarina.