Keywords

Selenium, Antiviral Peptides, Glutathione Peroxidase

Abstract

Objective: To express the soluble cysteine-deficient fusion protein of selenium-containing antiviral polypeptide in Escherichia coli, and to conduct preliminary identification of the biological activity of the purified protein. Methods: The se-containing antiviral peptide Se-GBVA10 gene was cloned into the GST fusion expression vector pGEX-2T, transformed into cysteine-deficient E. coli BL21 cysE51, and then expressed in cysteine-deficient form. Purify the target protein using Sepharose 4B affinity column, and conduct preliminary identification of its selenium content, antiviral activity and other properties. Results: The cysteine-deficient expression method was used to successfully express soluble sjGST-Se-GBVA10 and sjGST-GBVA10 fusion proteins, and the purified Se-GBVA10 and GBVA10 antiviral polypeptides were obtained after thrombin digestion. The selenium content of Se-GBVA10 was determined to be 0.974 mol/mol peptide, the GPX activity was 47.52 U/¦Ìmol, its EC50 was 21.73¦Ìmol/L, and its CC50 was 849.41¦Ìmol/L. Conclusion: Se-GBVA10 has the same antiviral activity as GBVA10 and has certain antioxidant activity

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Original research done by Lu Shaowu, Mou Ying, Wang Cheng, Yan Ganglin, Sui Chunhong

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