Zika virus structural proteins (ZIKV structural proteins)

The Zika virus structural proteins comprise the Capsid (C), Pre-membrane/Membrane (prM/M), and Envelope (E) proteins, which are translated as part of a single polyprotein and subsequently cleaved by viral and host proteases (UniProt: Q32ZE1). The Envelope protein is the most critical for therapeutic development as it mediates viral attachment to host receptors, such as AXL, and facilitates membrane fusion within endosomes (PubMed: 27074518). The prM protein serves as a chaperone to prevent the E protein from undergoing premature conformational changes during assembly, while the C protein dimerizes to package the viral RNA into the nucleocapsid (PubMed: 28288131). These proteins are the primary drivers of Zika virus infection, which can lead to Congenital Zika Syndrome and neurological disorders like Guillain-Barré syndrome (CDC). Current drug development efforts focus on vaccines, such as mRNA-1893 and TAK-426, and neutralizing monoclonal antibodies like ZIKV-117, which aim to block the E protein's function (NIH; Nature: 10.1038/nature20149). However, a significant hurdle in targeting these proteins is the potential for antibody-dependent enhancement (ADE), where cross-reactive antibodies from previous flavivirus infections, like Dengue, may exacerbate the disease (PubMed: 27302225).

Other names

ZIKV C-prM-EZika virus envelope, membrane, and capsid proteinsZika virus polyprotein (structural region)Zika virus structural polyprotein

Neutralization of viral particles by binding to the Envelope (E) protein to block receptor attachment and membrane fusion; induction of protective T-cell and B-cell responses via vaccination.