Dengue virus type 1 pre-membrane and envelope proteins (DEN-1 prM and E)

The **pre-membrane (prM) protein** is a glycoprotein present in immature dengue virus particles, where it forms heterodimers with the envelope (E) protein and shields the E protein fusion loop during transit, preventing premature membrane fusion. During viral maturation, prM is cleaved by furin in the trans-Golgi network, releasing the 'pr' peptide and allowing the mature M protein to remain as a transmembrane component underlying the E protein shell. The **envelope (E) protein** is a major surface glycoprotein responsible for host cell receptor binding and membrane fusion; it undergoes extensive conformational changes and is the main antigenic determinant recognized by neutralizing antibodies. Both prM and E proteins are essential for viral infectivity and are considered key drug and vaccine targets due to their roles in facilitating virus entry, fusion, and immune response modulation. They are not classical human "receptors" but are instead *viral* therapeutic targets.

Other names

Dengue prM proteinDengue envelope proteinDEN-1 pre-membrane (prM) and envelope (E) proteinsDengue E proteinDengue prM/E

Inhibition of envelope protein conformational changes required for membrane fusion and viral entry. Blockage of fusogenic rearrangement of E protein. Prevention of virion maturation (targeting prM cleavage and transition).