Preparation of poliovirus type 3 thermostable virus-like particles and immunogenicity research of poliovirus type 3 thermostable virus-like particles
By performing amino acid mutation and sequence optimization on the poliovirus type 3 structural protein, an sVLP series with better thermal stability and immunogenicity was prepared, which solved the problem of insufficient thermal stability and immunogenicity of virus-like particles and achieved a better vaccine candidate strategy.
CN120383662APending Publication Date: 2025-07-29HUA SONG (SHANGHAI) BIOMEDICAL TECH CO LTD +1
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Patent Information
- Application Number
- CN202410109647.1
- Authority / Receiving Office
- CN · China
- Patent Type
- Applications(China)
- Current Assignee / Owner
- Filing Date
- 2024-01-26
- Publication Date
- 2025-07-29
AI Technical Summary
Technical Problem
The existing poliovirus type 3 virus-like particles have poor thermal stability and immunogenicity, making it difficult to meet the needs of vaccines.
Method used
By performing amino acid mutation and sequence optimization on the poliovirus type 3 structural protein, the mutant capsid protein fragments sVP2, sVP3, and sVP1 are expressed in Pichia cerevisia, and sVLP series with better thermal stability and immunogenicity are prepared by connecting the operable elements in tandem.
Benefits of technology
The thermal stability of the sVLP series is significantly improved, can tolerate higher temperatures, and has better immunogenicity. The immune serum neutralization titer is much higher than that of wild-type, making it a good candidate strategy for PV3 vaccine.
✦ Generated by Eureka AI based on patent content.
Abstract
The invention relates to the field of medicine, in particular to preparation of poliovirus type 3 thermostable virus-like particles and immunogenicity research of the poliovirus type 3 thermostable virus-like particles. The invention provides a poliovirus type 3 virus-like particle. The poliovirus type 3 virus-like particle is selected from any one of the following: a, a capsid protein of the virus-like particle comprises a mutant capsid protein fragment sVP2, a mutant capsid protein fragment sVP3 and a mutant capsid protein fragment sVP1; and b, the capsid protein of the virus-like particle comprises a mutant capsid protein fragment sVP0 or a variant thereof, a mutant capsid protein fragment sVP3 and a mutant capsid protein fragment sVP1 or a variant thereof. According to the application, capsid proteins are connected in series at intervals through an operable element, the VLP is successfully prepared in pichia pastoris through sequence optimization, and the purified VLP is named as an sVLP series. The thermal stability result shows that the thermal stability of the sVLP series is far better than that of the wild type VLP (wtVLP), and the sVLP series can tolerate higher temperature; in addition, animal immune tests show that the immunogenicity of the sVLP series is better, and the neutralizing titer of immune serum of the sVLP series is far higher than that of wtVLP immune serum. In conclusion, the sVLP series is a good candidate strategy for PV3 vaccines.
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