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.

ABSTRACT:

Background

Foot-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.

Results

A 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

SUBMITTER: Zhang S 

PROVIDER: S-EPMC12512805 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature