Cloning, expression and characterization of protein disulfide isomerase of Schistosoma japonicum

被引：9

作者：

Cao, Xiaodan ^{[1
]}

Hong, Yang ^{[1
]}

Zhang, Min ^{[1
,3
]}

Han, Yanhui ^{[1
,4
]}

Wu, Miaoli ^{[1
]}

Wang, Xinzhuo ^{[1
]}

Guo, Xiaoyong ^{[1
]}

Li, Changjian ^{[1
]}

Lu, Ke ^{[1
]}

Li, Hao ^{[1
]}

Fu, Zhiqiang ^{[1
]}

Lin, Jiaojiao ^{[1
,2
]}

机构：

[1] Chinese Acad Agr Sci, Minist Agr China, Shanghai Vet Res Inst, Key Lab Anim Parasitol, Shanghai, Peoples R China

[2] Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou, Peoples R China

[3] Henan Univ Sci & Technol, Coll Anim Sci & Technol, Luoyang, Peoples R China

[4] Henan Inst Sci & Technol, Coll Anim Sci, Xinxiang, Peoples R China

来源：

EXPERIMENTAL PARASITOLOGY | 2014年 / 146卷

基金：

中国博士后科学基金; 中国国家自然科学基金;

关键词：

Schistosoma japonicum; Protein disulfide isomerase; Cloning; Characterization; Vaccine candidate; EXCRETORY-SECRETORY PRODUCTS; FASCIOLA-HEPATICA; MAMMALIAN PEROXIREDOXIN; THIOREDOXIN PEROXIDASE; PROTEOMIC ANALYSIS; REDUCE PEROXIDES; NEOSPORA-CANINUM; IDENTIFICATION; GENE; SEQUENCE;

D O I：

10.1016/j.exppara.2014.09.004

中图分类号：

R38 [医学寄生虫学]; Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ; 100103 ;

摘要：

The excretory/secretory (ES) proteins of schistosomes play important roles in modulating host immune systems and are regarded as potential vaccine candidates and drug targets. Protein disulfide isomerase (PDI) is an essential enzyme that is involved in disulfide bond formation and rearrangement. In the present study, SjPDI, a 52.8 kDa protein previously identified in a proteomics analysis as one of the ES proteins of Schistosoma japonicum, was cloned and characterized. Western blot analysis showed that recombinant SjPDI (rSjPDI) was recognized by serum from rabbits vaccinated with schistosome worm antigen. Worm protein extracts and ES protein extracts from S.japonicum could react with anti-rSjPDI mouse serum. Real-time PCR analysis indicated that SjPDI was expressed at all developmental stages tested, and a high expression level was detected in 42-day-old male worms. Immunofluorescence analysis revealed that SjPDI was mainly distributed on the tegument and parenchyma of S. japonicum worms. An enzyme-linked immunosorbent assay (ELISA) demonstrated that rSjPDI could induce a high level of rSjPDI-specific IgG antibodies. The biological activity of purified rSjPDI was confirmed by isomerization and antioxidative activity assays. The 35.32%, 26.19% reduction in the worm burden and 33.17%, 31.7% lower liver egg count were obtained in mice vaccinated with rSjPDI compared with the blank control group in two independent trials. Our preliminary results suggest that rSjPDI plays an important role in the development of the schistosome and is a potential vaccine candidate for schistosomiasis. (C) 2014 Elsevier Inc. All rights reserved.

引用

页码：43 / 51

页数：9

共 43 条

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