当前位置: X-MOL 学术Acta Parasitol. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Prediction and Identification of Epitopes in the Emy162 Antigen of Echinococcus multilocularis.
Acta Parasitologica ( IF 1.5 ) Pub Date : 2020-06-15 , DOI: 10.2478/s11686-020-00231-0
Ming-Quan Pang 1, 2 , Feng Tang 2, 3 , Hai-Jiu Wang 1, 2 , Ying Zhou 1, 2 , Li Ren 1, 2 , Run-Le Li 2, 3 , Hu Zhou 1, 2 , Chen-Fei Wan 1, 2 , Chuan-Chuan Liu 2, 3 , Cai-Rang Yangdan 1, 2 , Hai-Ning Fan 1, 2
Affiliation  

Introduction

Alveolar echinococcosis (AE) is a zoonotic disease caused by the parasitism of Echinococcus multilocularis larvae in the intermediate host or the final host. This study aims to identify and analyze the B-cell and T-cell (Th1, Th2 and Th17) epitopes of E. multilocularis antigen Emy162.

Methods

(1) The secondary structural characteristics of the Emy162 protein were predicted by bioinformatics software to further predict the potential T- and B-cell epitopes. (2) The dominant antigen epitopes were detected by ELISA through the reaction of patient serum with small B-cell antigen peptide and assessing the proliferation of splenic lymphocytes of mice immunized with Emy162. (3) The expression of cytokines in splenic lymphocytes of mice stimulated by small T-cell antigen peptides was detected by ELISA, ELISpot and flow cytometry to enable the identification of the T-cell epitopes.

Results

(1) The high-scored T-cell epitopes were located at positions E7-13, E36-41, E80-89, E87-96, E97-106 and E129-139, while B-cell epitopes were located at positions E7-13, E19-27, E28-36, E37-48, E78-83, E101-109, E112-121 and E129-139. (2) The three advanced antigen epitopes of Emy162 were E19-27, E112-121 and E129-139. (3) The four Th1 advanced antigen epitopes of Emy162 were E7-13, E36-41, E80-89 and E129-139. The three Th2 advanced antigen epitopes were E36-41, E87-96 and E97-106. The three Th17 advanced antigen epitopes were E36-41, E87-96 and E97-106.

Conclusion

(1) The Emy162 protein has advanced antigenicity and numerous potential epitopes. Six T-cell and eight B-cell dominant epitopes were revealed using bioinformatics methods. (2) There are three dominant B-cell epitopes, four dominant Th1 epitopes, three dominant Th2 epitopes, and three dominant Th17 epitopes in the Emy162 antigen.



中文翻译:

多房棘球蚴Emy162抗原表位的预测与鉴定。

简介

肺泡棘球蚴病(AE)是由多房棘球蚴幼虫寄生于中间宿主或终宿主引起的一种人畜共患疾病。本研究旨在鉴定和分析多房大肠杆菌抗原 Emy162的 B 细胞和 T 细胞(Th1、Th2 和 Th17)表位。

方法

(1)通过生物信息学软件预测Emy162蛋白的二级结构特征,进一步预测潜在的T细胞和B细胞表位。(2)通过ELISA检测患者血清与小B细胞抗原肽反应,评估Emy162免疫小鼠脾淋巴细胞增殖情况,检测显性抗原表位。(3)ELISA、ELISpot和流式细胞术检测小T细胞抗原肽刺激小鼠脾淋巴细胞中细胞因子的表达,从而鉴定T细胞表位。

结果

(1) 高分 T 细胞表位位于 E7-13、E36-41、E80-89、E87-96、E97-106 和 E129-139,而 B 细胞表位位于 E7- 13、E19-27、E28-36、E37-48、E78-83、E101-109、E112-121 和 E129-139。(2)Emy162的三个高级抗原表位为E19-27、E112-121和E129-139。(3)Emy162的4个Th1晚期抗原表位为E7-13、E36-41、E80-89和E129-139。三个 Th2 晚期抗原表位是 E36-41、E87-96 和 E97-106。三个 Th17 高级抗原表位是 E36-41、E87-96 和 E97-106。

结论

(1) Emy162 蛋白具有高级抗原性和众多潜在表位。使用生物信息学方法揭示了六个 T 细胞和八个 B 细胞优势表位。(2)Emy162抗原中有3个B细胞优势表位、4个Th1优势表位、3个Th2优势表位和3个Th17优势表位。

更新日期:2020-06-15
down
wechat
bug