Dengue virus serotype 4 premembrane protein (prM)

The Dengue virus serotype 4 prM protein is a critical structural component of the DENV-4 virion, serving as a precursor to the mature membrane (M) protein. Synthesized as a glycoprotein, prM forms a stable heterodimer with the envelope (E) protein in the endoplasmic reticulum, acting as a molecular chaperone to ensure proper E protein folding and to prevent premature, low-pH-induced fusion during transit through the secretory pathway (Source: UniProt Q8V1K0; PMID: 23193239). During viral maturation in the trans-Golgi network, prM is cleaved by the host protease furin into the 'pr' peptide and the M protein; the 'pr' peptide is subsequently released upon exocytosis into the neutral extracellular environment (Source: PMID: 31468018). In the context of disease, prM is a significant target for the host immune response, but antibodies directed against it are often cross-reactive and non-neutralizing, potentially contributing to antibody-dependent enhancement (ADE) of infection (Source: PMID: 25142593). Consequently, prM is a key consideration in the design of tetravalent vaccines like Dengvaxia and Qdenga, which aim to provide balanced immunity against all four DENV serotypes while minimizing the risks associated with ADE (Source: PMID: 35808493).

Other names

Premembrane proteinprM/M proteinGlycoprotein MDENV4 prM

Vaccines utilize prM as an immunogen to elicit protective immune responses, while experimental antivirals like alpha-glucosidase inhibitors interfere with its glycosylation and subsequent viral assembly.