

FOLLOWUS
1. MOE Key Laboratory of Marine Genetics and Breeding (Qingdao 266003), and Key Laboratory of Tropical Aquatic Germplasm of Hainan Province of Sanya Oceanographic Institution (Sanya 572024), Ocean University of China, Qingdao 266071, China
2. Laboratory for Marine Fisheries Science and Food Production Processes, and Center for Marine Molecular Biotechnology, Pilot National Laboratory for Marine Science and Technology (Qingdao), Qingdao 266237, China
3. Hainan Yazhou Bay Seed Laboratory, Sanya 572024, China
wangmengqiang@ouc.edu.cn
Received:08 July 2022,
Accepted:07 August 2022,
Online First:17 August 2022,
Published:01 September 2023
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LI Jiaobing,WANG Yan,HU Jingjie,et al.Molecular identification and biochemical characteristics of a delta class glutathione S-transferase gene (FcδGST) from Chinese shrimp Fenneropenaeus, chinensis[J].Journal of Oceanology and Limnology,2023,41(05):1940-1953.
Glutathione S-transferases (GSTs) are a superfamily of multifun
ction enzymes involved in the regulation of redox homeostasis and innate immune responses against various pathogenic infections in marine invertebrates. In the present study
a delta class GST gene (designated as FcδGST) was cloned from
Fenneropenaeus
chinensis
using rapid amplification of cDNA ends (RACE) technology. The complete cDNA sequence of FcδGST was 780 bp in length
which includes a 27-bp 5′ non-coding region (UTR)
a 117-bp 3′ UTR
a 636-bp open reading frame (ORF)
and a polyadenylate signal site (AATAAA) presented at the upstream of poly A tail. The FcδGST gene encoded 211 amino acids peptide
including a GST_N domain and a GST_C domain
and exhibited high similarity with previously reported delta GSTs. The predicted molecular mass of FcδGST protein was 23.39 kDa
and its theoretical isoelectric point (pI) was 5.34. The FcδGST mRNA transcripts were ubiquitously expressed in all the tested tissues
with the highest expression level in hemocytes and hepatopancreas. During the stimulation of
Vibrio
anguillarum
or white spot syndrome virus (WSSV)
the mRNA expression of FcδGST in hemocytes and hepatopancreas revealed significant up-regulation. The purified recombinant FcδGST protein (designated as rFcδGST) exhibited specific catalytic activity against 1-chloro-2
4-dinitrobenzene (CDNB) substrate with relatively low stable enzymatic activities. These results indicated that FcδGST was a fragile but typical novel delta class GST member and potentially involved in the innate immune responses of
F
.
chinensis
.
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