Chikungunya virus E1–E2 glycoprotein interface (CHIKV E1–E2 interface)

The Chikungunya virus E1–E2 glycoprotein interface is a critical structural component of the CHIKV virion, composed of the E1 fusion protein and the E2 attachment protein (Voss et al., 2010, DOI: 10.1038/nature09387). These proteins form heterodimers that further assemble into icosahedral spikes on the viral surface, mediating the essential steps of host cell recognition and entry. E2 facilitates binding to cellular receptors such as Mxra8, while E1 contains the fusion loop required for merging the viral envelope with the host endosomal membrane (Song et al., 2019, DOI: 10.1016/j.cell.2019.04.008). During the entry process, the acidic environment of the endosome triggers a conformational change at the E1–E2 interface, leading to E2 dissociation and E1 trimerization. This interface is a primary target for potent neutralizing antibodies, such as Bolandimab (CHKV-24), and experimental small-molecule inhibitors designed to lock the complex in a pre-fusion state or sterically hinder receptor interactions (Long et al., 2015, DOI: 10.1128/JVI.03449-14). Targeting this interface is a key strategy for developing therapeutics and vaccines to treat or prevent Chikungunya fever, a disease characterized by debilitating joint pain and fever.

Other names

CHIKV E1-E2 heterodimerChikungunya virus envelope protein complexCHIKV E1/E2 spikeCHIKV E1-E2 glycoprotein complex

Inhibition of viral entry by stabilizing the E1-E2 heterodimer, blocking receptor binding sites, or preventing pH-induced membrane fusion.