Dengue virus type 3 pre-membrane protein (prM)

The Dengue virus type 3 pre-membrane protein (prM) is a structural protein that plays a vital role in the life cycle of the Dengue virus serotype 3. It acts as a molecular chaperone for the Envelope (E) protein, preventing it from undergoing premature conformational changes and fusion while passing through the acidic secretory pathway of the host cell (Pierson & Kielian, 2013). During the maturation process in the trans-Golgi network, prM is cleaved by the host protease furin into a 'pr' peptide and a mature membrane (M) protein, which is a prerequisite for the virus to become fully infectious (UniProt Consortium, 2024). As a surface-exposed protein, prM is a significant target for the development of vaccines, such as the chimeric Dengvaxia and the live-attenuated Qdenga, which include prM sequences to induce protective immunity (WHO, 2024). However, prM is also associated with the production of non-neutralizing antibodies that can lead to antibody-dependent enhancement (ADE). ADE is a condition where the virus more easily infects Fc-receptor-bearing cells, increasing the risk of severe disease (Katzelnick et al., 2017). Consequently, the prM protein is a central focus in both the design of dengue therapeutics and the evaluation of their safety profiles. Its role in viral assembly and its interaction with host proteases make it a potential target for novel antiviral strategies.

Other names

Pre-membrane proteinprM proteinMembrane protein precursorpM

Vaccine-mediated induction of neutralizing antibodies and cellular immune responses against the viral structural proteins to prevent infection and viral replication.