St. Louis encephalitis virus pre-membrane protein (prM) (prM)

The St. Louis encephalitis virus pre-membrane protein (prM) is a structural glycoprotein essential for the assembly and maturation of the St. Louis encephalitis virus (SLEV), a mosquito-borne flavivirus (UniProt, 2024). Its primary function is to serve as a chaperone for the envelope (E) protein, shielding the E protein's fusion loop to prevent premature membrane fusion within the acidic environment of the host cell's secretory pathway (PubMed, 2021). As the immature virion moves toward the cell surface, prM is cleaved by the host protease furin into the 'pr' peptide and the mature membrane (M) protein, which triggers a conformational change that renders the virus infectious (NCBI, 2023). In clinical terms, SLEV is a pathogen responsible for outbreaks of febrile illness and encephalitis, particularly in North and South America (CDC, 2023). Because prM is vital for the production of infectious particles, it is a significant target for the development of vaccines and therapeutic antibodies aimed at neutralizing the virus (NIH, 2022). Although no specific small-molecule drugs are currently approved to target SLEV prM, research into flavivirus inhibitors often focuses on blocking the prM-to-M cleavage or disrupting the prM-E heterodimer interface to prevent viral spread.

Other names

prM proteinPre-M proteinSt. Louis encephalitis virus prM proteinSmall envelope protein MGenome polyprotein prM

Inhibition of viral maturation by preventing the cleavage of prM to M or blocking the prM-E complex formation.