Human CLDN1 Virus-Like Particles

Claudin-1 (CLDN1) is a key tight junction protein that plays a crucial role in maintaining the integrity of epithelial and endothelial barriers. As a member of the tight junction protein family, CLDN1 regulates paracellular permeability by forming selective pores that control the passage of ions and small molecules. CLDN1 is widely expressed in various tissues, including the liver, skin, and gastrointestinal tract, and is involved in cell adhesion and signal transduction. Importantly, CLDN1 has been implicated in numerous pathological conditions, such as hepatitis C virus (HCV) infection, where it serves as a coreceptor for viral entry. Furthermore, CLDN1 dysregulation has been linked to cancer progression, inflammatory diseases, and impaired barrier function, making it a promising target for therapeutic and diagnostic applications.

Human CLDN1 virus-like particles (VLPs) are innovative nanoscale constructs designed to mimic the native conformation of CLDN1 within the envelope of non-infectious viruses. These VLPs are produced by expressing CLDN1 and viral structural proteins, which self-assemble into particles that resemble the native virus but lack viral genetic material, ensuring safety for biomedical applications. CLDN1 VLPs are a powerful tool for vaccine development, particularly for hepatitis C (HCV) vaccines, as they present CLDN1 in its native form, eliciting a potent immune response. Beyond vaccines, these VLPs can also be used in targeted drug delivery systems, leveraging their ability to bind to specific cell receptors for precision medicine. Furthermore, CLDN1 VLPs facilitate the study of virus-host interactions, enabling investigation of CLDN1-mediated viral entry mechanisms without the risks associated with live pathogens.