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Updated: Jan 21, 2026

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
Published on: February 17, 2017
Cloning of a trehalose-6-phosphate synthase gene from Exopalaemon carinicauda and its expression response to bacteria
Jiquan Zhang1, Yujie Liu1, Yongzhao Zhou1
1Laboratory of Zoological Systematics and Application of Hebei Province, College of Life Sciences, Hebei University, Baoding, 071002, China.
Abstract:
Trehalose, a nonreducing disaccharide, is present in a wide variety of organisms and plays a key role in many organisms under different stress conditions. In the study, the full-length cDNA sequence encoding trehalose-6-phosphate synthase (EcTPS) was obtained from Exopalaemon carinicauda. The complete nucleotide sequence of EcTPS contained a 2532 bp open reading frame (ORF) encoding a putative protein of 843 amino acids. The domain architecture of the deduced EcTPS contained a glycol_transf_20 domain and a trehalose_PPase domain. EcTPS mRNA was predominantly expressed in the hepatopancreas. The expression of EcTPS in the prawns challenged with Vibrio parahaemolyticus and Aeromonas hydrophila changed in a time-dependent manner. The function of EcTPS was also studied by double-strand RNA interference. The results showed that the knock-down of EcTPS increased the mortality of the Vibrio-challenged group and Aeromonas-challenged group compared with the control group. The present study provides some new insight into the immune function of the trehalose-6-phosphate synthase in prawns.
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