N-terminal truncation of the foot-and-mouth disease virus VP0 protein promotes soluble co-expression and particle assembly stability of viral capsid proteins in Escherichia coli
Collectively, our findings establish a robust platform for the efficient production of structurally stable FMDV VLPs in E. coli, providing a valuable framework for developing soluble expression systems for other FMDV serotypes.
Authors
- Yanxia Wang (ORCID: https://orcid.org/0000-0002-1318-9231)
- Xiaolin Geng
- S. S. Wu (ORCID: https://orcid.org/0009-0004-7113-8258)
- Yinghong Yue (ORCID: https://orcid.org/0000-0002-8000-1606)
- Suling Zhang
- Peng Wu (ORCID: https://orcid.org/0000-0003-4498-7663)
- Aihua Wang (ORCID: https://orcid.org/0000-0001-9693-7292)
- Yuxin Huang (ORCID: https://orcid.org/0000-0003-3056-4168)
- Kegong Tian (ORCID: https://orcid.org/0000-0002-1420-6347)
- Wenqiang Pang
Institutions
- Center for Veterinary Medicine (US)
- North West Agriculture and Forestry University (CN)
- China National Biotechnology (China) (CN)
- Luoyang Institute of Science and Technology (CN)
- Northwest A&F University (CN)
Publication Details
- Journal
- BMC Biotechnology
- Published
- 2025-10-10
- DOI
- https://doi.org/10.1186/s12896-025-01049-2
- Primary Topic
- Animal Disease Management and Epidemiology
- Type
- article
- Field-Weighted Citation Impact
- 0.00