Zika virus precursor membrane protein and envelope protein (ZIKV prM and E proteins)

The Zika virus precursor membrane protein (prM) and envelope protein (E) are two essential structural components of the Zika virus particle. The E protein is a surface glycoprotein that mediates viral attachment to host cell receptors and fusion of the viral membrane with host cell membranes, enabling viral entry and infection[1][3][6][7]. The E protein has three main domains (DI, DII—including a fusion loop, and DIII—containing the receptor binding site) and forms a dimeric structure on mature virions[1][7]. The prM protein functions as a chaperone during virion assembly; it protects the E protein from premature fusion during transport through the Golgi and is cleaved to the mature M protein during virus maturation, which allows conformational rearrangement of E proteins into the infectious virus structure[3][6]. Both prM and E proteins are targets for neutralizing antibodies and form the basis for most Zika vaccine candidates[3][5]. As viral envelope proteins, prM and E are not typically "receptors" in the classical pharmacological sense, but they are considered therapeutic targets for antivirals and vaccines, and are involved in critical steps of the viral life cycle[1][3][5].

Other names

prM and E proteinsZIKV structural proteinsZika virus prM-E complex

Inhibition of viral entry/fusion (monoclonal antibodies bind E protein and prevent receptor binding or membrane fusion)[1][5]; Inhibition of prM cleavage or function (prevents maturation and infectious virion production; mainly vaccine and experimental strategies)[3][6]