Recombinant porcine alpha and gamma interferon

Through the insect-baculovirus expression system and synonymous preference modification codons, combined with the use of phomin signal peptides, the defects of the pig α and γ interferon expression systems in the prior art were solved, efficient and stable co-expression and purification were achieved, and biological activity and production efficiency were improved.

CN119709765APending Publication Date: 2025-03-28INST OF ANIMAL SCI & VETERINARY MEDICINE SHANDONG ACADEMY OF AGRI SCI
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Patent Information

Application Number
CN202510092737.9
Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
Filing Date
2025-01-21
Publication Date
2025-03-28

AI Technical Summary

Technical Problem

The existing expression systems have problems such as protein modification, inclusion body existence, and hybrid protein production when expressing pig α and γ interferon, which leads to increased purification difficulty and cost and affects activity.

Method used

The insect-baculovirus expression system was adopted to modify the codons through synonymous preferences, add phomin signal peptides to achieve extracellular expression, and recombinant vector construction and viral infection were carried out using pFastBacTMDual vector and DH10Bac cells to achieve efficient co-expression of pig α and gamma interferon.

Benefits of technology

The efficient expression of pig α and γ interferon is achieved, the protein structure is close to the natural state, the biological activity is high, the purification is easy to carry out, which reduces production costs and improves the quality and stability of the recombinant protein.

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Abstract

The invention belongs to the technical field of veterinary medicine, and provides a co-expressed recombinant porcine alpha and gamma interferon. The I-type interferon alpha and the II-type interferon gamma not only exert the anti-virus, anti-cell division and immune regulation effects of the interferon, but also can activate T cells and natural killer cells, and fully exert the multiple activities of the interferon. The two interferons are co-expressed in insect cells, the expression protein can be folded and then processed and modified, the structure of the expression protein is closer to a natural structure, the biological activity is high, the recombinant protein is easy to purify, the production scale is easy to expand, and live viruses or potential dangerous pathogens do not need to be treated, so that the production cost is reduced; by optimizing the production process and fermentation conditions, the quality and stability of the recombinant protein can be further improved.
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