Dengue virus type 1 structural proteins (DENV-1 structural proteins)

Dengue virus type 1 (DENV-1) structural proteins comprise the Capsid (C), precursor Membrane (prM), and Envelope (E) proteins, which are translated as part of a single polyprotein and subsequently cleaved by host and viral proteases [4, 15]. The C protein is a highly basic protein that binds and condenses the viral RNA genome to form the nucleocapsid [13, 17]. The prM protein acts as a molecular chaperone for the E protein, shielding its fusion loop to prevent premature fusion during transport through the acidic trans-Golgi network [3, 5]. The E protein is the major surface glycoprotein that mediates host cell receptor binding and pH-dependent membrane fusion within endosomes [3, 10]. These proteins are primary targets for the host immune response and are central to the development of vaccines and direct-acting antivirals [2, 6]. However, therapeutic intervention is complicated by the risk of antibody-dependent enhancement (ADE), where sub-neutralizing antibodies facilitate viral entry into Fc-receptor-bearing cells, potentially leading to severe disease [1, 14]. The structural proteins also undergo significant conformational changes during the maturation process from immature spiky particles to mature smooth virions [3, 4]. Understanding these structural transitions is crucial for designing inhibitors that can stabilize specific states or disrupt the assembly process [2, 10].

Other names

DENV-1 C-prM-EDengue virus serotype 1 structural proteinsDENV1 structural polyprotein

Direct-acting antivirals target the structural proteins to inhibit various stages of the viral life cycle: E protein inhibitors block viral attachment and membrane fusion; Capsid inhibitors interfere with nucleocapsid assembly and genome packaging; and prM inhibitors prevent proper viral maturation and egress [2, 5, 6, 10].