Dengue virus serotype 4 pre-membrane protein (prM) (prM)

The Dengue virus serotype 4 pre-membrane protein (prM) is a critical structural glycoprotein of the DENV-4 virion (UniProt: P09866). Its primary biological role is to act as a chaperone for the Envelope (E) protein during the assembly and transport of immature virus particles through the host cell's secretory pathway. By forming a heterodimer with the E protein, prM prevents the E protein from undergoing premature, low-pH-triggered conformational changes in the trans-Golgi network (PMID: 11448161). During the final stages of viral maturation, prM is cleaved by the host protease furin into the 'pr' peptide and the mature 'M' protein, rendering the virus infectious (PMID: 23824813). In the context of therapeutics, prM is a major component of recombinant and live-attenuated dengue vaccines, such as Dengvaxia and Qdenga, where it is used to elicit a protective immune response. However, antibodies against prM are often non-neutralizing and have been implicated in antibody-dependent enhancement (ADE), a phenomenon where sub-neutralizing antibodies facilitate viral entry into Fc-receptor-bearing cells, potentially increasing the severity of the disease (PMID: 20448183).

Other names

prM proteinPre-membrane proteinDENV4 prMMembrane glycoprotein precursorpM

Vaccines containing the prM protein sequence induce the production of neutralizing antibodies that target the virus and prevent infection. The prM protein itself functions as a chaperone for the Envelope protein during viral assembly, and its cleavage into the M protein is essential for viral infectivity (PMID: 23824813).