Recombinant Human U51 protein

U51 recombinant protein is a genetically engineered protein derived from the U51 gene encoded by human herpesvirus 6 (HHV-6) or its homologs in related herpesviruses. As a member of the G protein-coupled receptor (GPCR) family, U51 plays a critical role in viral pathogenesis and immune modulation. It is implicated in immune evasion by interacting with host chemokines, disrupting normal chemotactic signaling, and promoting viral latency or reactivation. The recombinant form is typically expressed in heterologous systems like *E. coli* or mammalian cells, enabling structural and functional studies.

Research on U51 focuses on its dual role as a viral virulence factor and a potential therapeutic target. Structurally, it features seven transmembrane domains characteristic of GPCRs, with extracellular loops mediating ligand binding. Studies reveal its ability to bind chemokines such as CCL2 and CCL5. interfering with immune cell recruitment. This interaction may contribute to HHV-6-associated diseases, including encephalitis and chronic fatigue syndrome. Additionally, U51 modulates intracellular signaling pathways, including MAPK and NF-κB, influencing both viral replication and host inflammatory responses.

The development of U51 recombinant protein has facilitated drug discovery efforts, particularly in screening inhibitors that block its chemokine-binding sites. Its unique mechanism of immune interference also provides insights into broader GPCR biology and viral-host coevolution. However, challenges remain in fully elucidating its in vivo conformational dynamics and tissue-specific effects. Current applications extend to diagnostic tools for detecting HHV-6 antibodies and experimental models studying neurotropic viral infections. Ongoing research aims to clarify its role in viral latency cycles and explore its potential as a biomarker for herpesvirus-associated pathologies.