Human CLDN4 Virus-Like Particles

Claudin-4 (CLDN4) is a key member of the claudin family, a class of tight junction proteins that play a crucial role in maintaining cell polarity and regulating paracellular permeability in epithelial and endothelial tissues. CLDN4''s structure consists of four transmembrane domains, two extracellular loops, and intracellular N- and C-termini. It is highly expressed in tissues such as the kidney, lung, and gastrointestinal tract, where it participates in barrier function and selective ion transport. Dysregulation of CLDN4 is associated with various pathological conditions, including cancer, where its overexpression is correlated with tumor progression and metastasis. Furthermore, CLDN4 is a receptor for certain bacterial toxins, such as Clostridium perfringens enterotoxin (CPE), highlighting its importance in both physiological and pathological settings. Due to its critical functions and association with disease, CLDN4 has become a promising target for therapeutic and diagnostic applications.

Human CLDN4 virus-like particles (VLPs) are innovative, non-infectious nanostructures designed to mimic the native membrane-presenting conformation of CLDN4. These VLPs are typically produced by expressing CLDN4 and viral structural proteins (such as the envelope protein of hepatitis B virus (HBV) or the capsid protein of human papillomavirus (HPV), which self-assemble into particulate structures. Unlike live viruses, VLPs contain no genetic material, making them safe for research and therapeutic use. CLDN4 VLPs are a powerful tool for studying CLDN4-mediated interactions, including pathogen invasion mechanisms and immune responses. They are also being explored as vaccine candidates, particularly for cancers that overexpress CLDN4, by eliciting a targeted immune response against tumor cells. Furthermore, CLDN4 VLPs can be genetically engineered to deliver drugs or diagnostic agents specifically to CLDN4-rich tissues, thereby improving the precision of therapeutic and imaging approaches.