Purification of Classical Swine Fever Virus E2 Subunit Vaccines Based on High Affinity Peptide Ligand

文献类型： 外文期刊

第一作者： Wang, Fangyu

作者： Wang, Fangyu;Hu, Man;Xing, Guangxu;Zhao, Dong;Zhang, Gaiping;Yu, Qiuying;Zhang, Gaiping

作者机构：

关键词： Classical swine fever virus; glycoprotein E2; computational design; affinity peptide ligand; purification; pro-tein-peptide screening

期刊名称：PROTEIN AND PEPTIDE LETTERS （ 影响因子：1.89； 五年影响因子：1.528 ）

ISSN： 0929-8665

年卷期： 2021 年 28 卷 5 期

页码：

收录情况： SCI

摘要： Background: The purification of expressed proteins is the most critical part of subunit -vaccine production. Protein-purification methods such as affinity chromatography and exchange still have the shortcomings of being time consuming and complicated. With the rapid development of computational molecular-simulation technology, structure-based peptide-ligand design has become feasible. Objection: We aimed to apply molecular docking for a peptide ligand designed for classical swine fever virus (CSFV) E2 purification. Methods: Computational-derived peptides were synthesized, and the in vitro binding interaction with E2 was investigated. The effects of purification on E2 were also evaluated. Results: The best peptide recognizing E2 was P-6, which had a sequence of KKFYWRYWEH. Based on kinetic surface plasmon resonance (SPR) analysis, the apparent affinity constant of P-6 was found to be 148 nM. Importantly, P-6 showed suitable binding affinity and specificity for E2 purification from transgenic rice seeds. Evaluation of immune antibodies in mice showed that the antibody-blocking rate on day 42 after inoculation reached 86.18% and 90.68%. Conclusion: The computational-designed peptide in this study has high sensitivity and selectivity and is thus useful for the purification of CSFV E2. The novel method of design provided a broad platform and powerful tool for protein-peptide screening, as well as new insights into CSFV vaccine design.

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