Human PROM1 Virus-Like Particles

PROM1, also known as prominin-1 or CD133, is a transmembrane glycoprotein that plays a key role in cellular processes such as proliferation, differentiation, and maintenance of stem cell identity. It is widely recognized as a marker of stem cells, particularly in neural, hematopoietic, and epithelial tissues. PROM1''s structure, consisting of five transmembrane domains and two large extracellular loops, underlies its diverse functions. The protein is involved in organizing plasma membrane protrusions and regulating signaling pathways that influence cell fate. Due to its association with stem cell identity and tumorigenesis, PROM1 overexpression has been extensively studied in cancer research. Beyond oncology, PROM1 has also been implicated in retinal degeneration and other genetic diseases, making it an important target for biomedical research and therapeutic development.

PROM1 virus-like particles (VLPs) are non-infectious nanostructures designed to mimic the structure and immunological properties of native viruses but without the presence of viral genetic material. These VLPs are produced by expressing PROM1 in recombinant systems (such as bacteria, yeast, or mammalian cells), where the protein self-assembles into stable, highly ordered particles. Due to the unique extracellular domain of PROM1, these VLPs exhibit excellent antigenicity, making them ideal candidates for vaccine development and targeted drug delivery. In cancer immunotherapy, PROM1 VLPs can be designed to present tumor-associated antigens, thereby stimulating a potent immune response against PROM1-positive cancer cells. Furthermore, their biocompatibility and customizable surface properties make them useful in diagnostic imaging and gene therapy. Compared to traditional viral vectors, PROM1 VLPs offer enhanced safety and a lower risk of insertional mutagenesis.