Surface display of classical swine fever virus E2 glycoprotein on gram-positive enhancer matrix (GEM) particles via the SpyTag/SpyCatcher system

文献类型： 外文期刊

第一作者： Li, Ding

作者： Li, Ding;Zhang, Haoming;Yang, Li;Chen, Jin;Zhang, Yuanpeng;Yu, Xiaoming;Zheng, Qisheng;Hou, Jibo;Li, Ding;Zhang, Haoming;Yang, Li;Chen, Jin;Zhang, Yuanpeng;Yu, Xiaoming;Zheng, Qisheng;Hou, Jibo;Li, Ding;Zhang, Haoming;Yang, Li;Chen, Jin;Zhang, Yuanpeng;Yu, Xiaoming;Zheng, Qisheng;Hou, Jibo

作者机构：

关键词： Classical swine fever virus E2 protein; Glycosylation; SpyTag/SpyCatcher system; Conjugation; Surface display

期刊名称：PROTEIN EXPRESSION AND PURIFICATION （ 影响因子：1.65； 五年影响因子：1.548 ）

ISSN： 1046-5928

年卷期： 2020 年 167 卷

页码：

收录情况： SCI

摘要： The E2 envelope protein is the main protective antigen of classical swine fever virus (CSFV). Importantly, gram-positive enhancer matrix (GEM) particles can work as an immunostimulant and/or carrier system to improve the immune effect of antigens. In this study, the artificially designed E2-Spy was expressed and glycosylated in Pichia pastoris, and subsequently conjugated with SpyCatcher-PA which was expressed in Escherichia coli. The conjugated E2-Spy-PA was displayed on the surface of GEM particles, generating the E2-Spy-PA-GEM complex. Blocking ELISA analysis and neutralization assays showed that both E2-Spy and E2-Spy-PA-GEM complexes induced high levels of anti-CSFV antibodies in mice. Furthermore, statistical analyses indicated that the E2-Spy-PA-GEM complex exhibited enhanced immunogenicity compared with E2-Spy alone.

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