Rift Valley fever virus glycoprotein Gn–Gc complex interface (RVFV Gn–Gc interface)

The **Rift Valley fever virus glycoprotein Gn–Gc complex interface** forms the critical structural and functional unit responsible for viral entry into host cells. The complex consists of two glycoproteins, **Gn (envelope glycoprotein N)** and **Gc (envelope glycoprotein C)**, which are embedded in the viral envelope and assemble into heterodimeric spikes. Gc is a class II fusion protein mediating membrane fusion, while Gn appears to shield the fusion loop of Gc and plays a major role in receptor binding and immune recognition. The **interface** between Gn and Gc is essential for the viral fusion mechanism: Gn shields the hydrophobic fusion loops of Gc in the pre-fusion state, and conformational changes expose Gc for fusion during host cell entry[1][2][3][4][5]. The interface is also a major target for neutralizing antibodies and potentially for antiviral small molecules. Disrupting this interface inhibits viral entry, making it a strategic therapeutic target for managing Rift Valley fever virus infections[6]. **Note:** The entity described is a molecular interface and not a single protein or receptor, but literature and drug design efforts commonly regard the Gn–Gc interface as a therapeutically actionable viral target[6].

Other names

RVFV envelope glycoprotein interfaceRVFV Gn–Gc heterodimerRift Valley fever virus envelope spike complex

Small-molecule or antibody inhibitors block viral entry by: - Inhibiting receptor binding (Gn) - Inhibiting membrane fusion (Gc) - Sterically preventing conformational rearrangement or fusion loop exposure