Zika virus envelope glycoprotein quaternary dimer-dimer interface epitope (ZIKV E dimer-dimer epitope)

The Zika virus envelope (E) glycoprotein is the primary protein on the viral surface, organized into 90 homodimers that form a herringbone pattern (Sankhala et al., 2023). The quaternary epitope at the dimer-dimer interface is a complex antigenic site formed by the juxtaposition of two adjacent E protein dimers on the mature virion (Sapparapu et al., 2016). This epitope is a critical target for potently neutralizing human monoclonal antibodies, such as ZIKV-117, which bind across the interface to lock the dimers in place (Zhang et al., 2016). By stabilizing the dimeric structure, these antibodies prevent the large-scale conformational changes—specifically the transition from dimers to fusogenic trimers—required for membrane fusion and viral entry into host cells (Long et al., 2020). Targeting this specific quaternary structure is a key strategy in developing ZIKV-specific therapeutics and vaccines that aim to provide high potency while minimizing the risk of antibody-dependent enhancement (ADE) associated with cross-reactive antibodies to other flaviviruses like Dengue (Sankhala et al., 2023).

Other names

Zika virus envelope protein inter-dimer epitopeZIKV E quaternary epitopeZIKV E-raft epitopeZika virus envelope glycoprotein dimer-dimer interface

Neutralization of viral infection by binding across adjacent envelope protein dimers to stabilize the mature virion structure and inhibit the dimer-to-trimer transition required for membrane fusion.