Hantaan virus envelope glycoprotein Gn-Gc complex (GnGc)

The Hantaan virus envelope glycoprotein Gn-Gc complex is a multimeric spike composed of two glycoproteins, Gn and Gc, anchored in the viral envelope. These proteins are translated as a polyprotein precursor and cleaved during viral maturation. The spikes form a lattice-like array on the virus surface, mediating host cell recognition and entry. Gn and Gc function cooperatively: Gn is implicated in initial attachment and shielding fusion epitopes, while Gc is a class II fusion protein that facilitates membrane fusion between viral and host endosomal membranes at low pH. The Gn-Gc complex is a major target for neutralizing antibodies and vaccine development due to its surface exposure and essential role in infection. Structural studies have revealed dynamic rearrangements of these proteins during virus entry and exit, with conformational changes pivotal for fusion and immune evasion. Their interactions, molecular architecture, and disease relevance make Gn-Gc a prototypical viral therapeutic target crucial to hantavirus infection and pathogenesis.

Other names

HTNV GnGcHantavirus surface glycoprotein Gn-GcGlycoprotein G1-G2 complex (historical, now standardized as Gn-Gc)

- Neutralization of viral entry (by blocking Gn/Gc-mediated attachment or fusion) - Inhibition of membrane fusion (blocking conformational changes of Gc required for fusion at acidic pH) - Disruption of spike assembly (possible via interfering with Gn-Gc oligomerization)