Abstract Virus‐like particles (VLPs) are widely recognized as safe and versatile nanostructures with broad applications in vaccine development, gene delivery, and nanotechnology, but their production typically requires time‐consuming procedures, incurs high costs, and yields products of limited purity. This article outlines a rapid, scalable, and cost‐effective method for producing high‐quality VLPs using the VP1s capsid protein from murine polyomavirus. The procedure comprises four principal stages: expression of the capsid protein in Escherichia coli , extraction and stabilization of the protein, purification to yield high‐quality capsomeres, and controlled in vitro assembly of VLPs. Compared with conventional protocols that rely on in vivo assembly and labor‐intensive purification procedures, such as ultracentrifugation‐ or affinity tag‐based methods, the described approach provides a streamlined and rapid workflow that avoids affinity tags, achieves consistently high yields, and enables precise regulation of assembly conditions, resulting in a scalable and highly cost‐efficient strategy for VLP production within 5 days. © 2026 Wiley Periodicals LLC. Basic Protocol 1 : Expression and preparation of polyomavirus VP1 protein in E. coli Basic Protocol 2 : Polymomavirus VP1 purification Basic Protocol 3 : VP1 assembly Basic Protocol 4 : Quality control
Wang et al. (Thu,) studied this question.