ArticleBMC biotechnology2025
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.
Article in BMC biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundFoot-and-mouth disease (FMD), caused by foot-and-mouth disease virus (FMDV), is an acute, highly contagious, and economically devastating disease affecting cloven-hoofed animals worldwide. Vaccination remains the cornerstone of FMD control strategies. To increase the production yield and structural stability of virus-like particles (VLPs), we investigated the effects of the N-terminal truncation of VP0 on the soluble co-expression of three capsid proteins, and the stability of the assembled particles.
resultsA series of VP0 variants with progressive N-terminal truncations (5-20 amino acids) were co-expressed with VP3 and VP1 via a single plasmid in the Escherichia coli (E. coli) expression system by fusing these proteins with a small ubiquitin-like modifier (SUMO) tag. The assembly characteristics of the co-expressed fusion proteins were systematically characterized. Our findings show that all engineered fusion proteins were successfully co-expressed, and truncations between residues 10 and 20 yielded significantly higher expression levels and purification efficiencies than those of full-length VP0. The 031-VP0 dN10, 031-VP0 dN15, and 031-VP0 dN20 exhibited increased stability of the assembly and retained the native morphology. An in vitro binding assay for neutralizing antibodies against FMDV indicated that all VLPs maintained wild-type-like antigenic properties, demonstrating preserved conformational epitopes. Pigs immunized with VLPs-based vaccines exhibited humoral and cellular immune responses, with the 031-VP0 dN20 variant eliciting significantly stronger cellular immunity.
conclusionsCollectively, 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.
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