Molecular characterization and transcriptional analysis of a crustacean heat shock protein 10 gene in shrimp Litopenaeus vannamei

Authors

  • M Q Wang Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China
  • B J Wang Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China
  • Ke Y Jiang Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China
  • M Liu Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China
  • Si Y Han Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China; University of Chinese Academy of Sciences, Beijing 100049, China
  • L Wang Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China; Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao 266237, China

DOI:

https://doi.org/10.25431/1824-307X/isj.v14i1.404-413

Keywords:

heat shock protein 10, hepatopancreas, Litopenaeus vannamei

Abstract

Heat shock proteins (HSPs) are the most abundant and ubiquitous soluble intracellular proteins which conserved phylogenetically in all living organisms from archaebacteria to humans. Recent research achievements indicated that HSP10s might not only be involved in the responses to environmental stresses, but also play a pivotal role in the host defenses mechanism. In the present study, a cDNA of 715 bp for the Pacific white shrimp Litopenaeus vannamei HSP10 (designated as LvHSP10) was cloned via rapid amplification of cDNA ends (RACE) technique. The complete cDNA sequence of LvHSP10 contained an open reading frame (ORF) of 309 bp, which encoded a protein of 102 amino acids. The protein sequence of LvHSP10 shared over 80 % similarity with previously identified HSP10s. There were a CPN10 domain and a chaperonins HSP10/CPN10 signature in the protein sequence of LvHSP10. The mRNA transcripts of LvHSP10 were constitutively expressed in all the tested tissues, including eyestalk, gill, gonad, heart, hemocytes, hepatopancreas, intestine, muscle, nerve and stomach, with the highest expression level in hepatopancreas. The mRNA expression profiles of LvHSP10 in hepatopancreas could be significantly induced by the stimulation of Vibrio parahaemolyticus, white spot syndrome virus (WSSV), and low and high pH challenge. These results provided useful information of the potential roles of LvHSP10 in the defense mechanism of shrimp against various biological stimulations and multiple environmental stresses. 

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Published

2017-10-20

Issue

Section

Research Reports