Molecular cloning and expression analysis of cathepsin D from kuruma shrimp (<i>Marsupenaeus japonicus</i>)

Zhang Man; Cheng Guangping; Su Yongquan; Xu Yihua; Feng Wenrong; Wang Jun; Song Xiaohong; Mao Yong

doi:10.3969/j.issn.0253-4193.2016.08.006

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Zhang Man, Cheng Guangping, Su Yongquan, Xu Yihua, Feng Wenrong, Wang Jun, Song Xiaohong, Mao Yong. Molecular cloning and expression analysis of cathepsin D from kuruma shrimp (Marsupenaeus japonicus)[J]. Haiyang Xuebao, 2016, 38(8): 52-61. doi: 10.3969/j.issn.0253-4193.2016.08.006

Citation:

Zhang Man, Cheng Guangping, Su Yongquan, Xu Yihua, Feng Wenrong, Wang Jun, Song Xiaohong, Mao Yong. Molecular cloning and expression analysis of cathepsin D from kuruma shrimp (Marsupenaeus japonicus)[J]. Haiyang Xuebao, 2016, 38(8): 52-61. doi: 10.3969/j.issn.0253-4193.2016.08.006

Citation:

Zhang Man, Cheng Guangping, Su Yongquan, Xu Yihua, Feng Wenrong, Wang Jun, Song Xiaohong, Mao Yong. Molecular cloning and expression analysis of cathepsin D from kuruma shrimp (Marsupenaeus japonicus)[J]. Haiyang Xuebao, 2016, 38(8): 52-61. doi: 10.3969/j.issn.0253-4193.2016.08.006

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Molecular cloning and expression analysis of cathepsin D from kuruma shrimp (Marsupenaeus japonicus)

doi: 10.3969/j.issn.0253-4193.2016.08.006

1.
Guangxi Colleges and Universities Key Laboratory of Aquatic Healthy Breeding and Nutrition Regulation, College of Animal Science and Technology, Guangxi University, Nanning 530005, China;College of Ocean and Earth Sciences, Xiamen University, Xiamen 361102, China
2.
Guangxi Colleges and Universities Key Laboratory of Aquatic Healthy Breeding and Nutrition Regulation, College of Animal Science and Technology, Guangxi University, Nanning 530005, China
3.
College of Ocean and Earth Sciences, Xiamen University, Xiamen 361102, China

Received Date: 2015-12-15
Rev Recd Date: 2016-03-31

Abstract

Abstract

Cathepsin D is the principal member of lysosomal aspartic proteinase family which participates in various degradations of intracellular protein and plays important roles in normal metabolism for the maintenance of cellular homeostasis. In this current study, the cDNA sequence of kuruma shrimp (Marsupenaeus japonicus) cathepsin D (MjCatD) was cloned for the first time through RACE technology, including a 1 161 bp open reading frame encoding 386 amino acids. Both sequence analysis and homology modeling revealed that the deduced protein of MjCatD contained well conserved N-glycosylation site, aspartic proteinase signature sequence, active site and the characteristic sequence of non-digestive cathepsin D, as well as presented a conserved bilobal structure. MjCatD shared high similarity with those from Penaeus monodon, Homarus americanus, Palaemon carinicauda, and clustered together with above three cathepsin Ds. Real-time quantitative PCR demonstrated that MjCatD was ubiquitously expressed in all the examined tissues, predominantly in hepatopancreas. After challenging with white spot syndrome virus (WSSV), the expression level of MjCatD in the hepatopancreas was gradually down regulated during 3 h to 24 h, then very significantly increased (P<0.01) and peaked at 48 h compared to the control. MjCatD also showed obvious changes during different larval stages. These findings indicated that MjCatD may play key roles in the innate immune response and larval development of kuruma shrimp.
- Marsupenaeus japonicus,
- cathepsin D,
- gene cloning,
- gene expression

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References(28)

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