Dengue virus serotype 2 pre-membrane protein (prM)

The Dengue virus serotype 2 pre-membrane protein (prM) is a critical structural component of the DENV-2 virion, playing a dual role in viral assembly and maturation. During the viral life cycle, prM forms a stable heterodimer with the envelope (E) protein within the endoplasmic reticulum, acting as a chaperone to ensure proper E protein folding (UniProt, 2024). It also serves to protect the E protein from undergoing premature, low-pH-triggered fusion while the virus is transported through the acidic environment of the secretory pathway (PubMed, 2021). As the immature virus moves through the trans-Golgi network, the host protease furin cleaves prM into the pr peptide and the mature M protein, a step essential for the virus to become infectious (NIH, 2023). In the context of disease, prM is a primary target for the host immune response, though antibodies directed against it are often non-neutralizing (Nature, 2022). These non-neutralizing antibodies are strongly associated with antibody-dependent enhancement (ADE), a phenomenon where they facilitate viral entry into Fc-receptor-bearing cells, potentially leading to severe dengue hemorrhagic fever (PubMed, 2020). Consequently, prM is a focal point in vaccine design, such as in the tetravalent Dengvaxia and Qdenga vaccines, where it is used to elicit protective immunity against multiple serotypes (StatPearls, 2023). Therapeutic strategies targeting prM aim to either block the maturation process or neutralize the virus before it can infect host cells.

Other names

prM proteinPre-membrane proteinDENV-2 prMMembrane glycoprotein precursorprM/M protein

Induction of neutralizing antibodies and inhibition of viral maturation