Hantaan virus Gc glycoprotein (Gc)

The Hantaan virus Gc glycoprotein is a key envelope protein derived from cleavage of the glycoprotein precursor (GPC) encoded by the viral M segment, forming heterodimers with Gn to create surface spikes on the pleomorphic virion envelope. It functions primarily as a class II viral fusion protein, undergoing low pH-triggered conformational changes in endosomes to insert fusion loops into the host membrane, drive trimerization, and mediate viral ribonucleocapsid release into the cytosol during cell entry. Gc also contributes to virus assembly and budding at the Golgi apparatus by self-assembling into virus-like particles and interacting via its cytoplasmic tail with viral ribonucleocapsids. These roles enable Hantaan virus, a hantavirus pathogen, to infect endothelial cells and cause hemorrhagic fever with renal syndrome. While Gn likely aids receptor binding, Gc's fusion activity is conserved across hantaviruses, with structural features like beta-strand domains and N-linked glycosylation essential for stability and function. The glycoprotein spikes exhibit four-fold symmetry, protruding 10-12 nm from the membrane. Neutralizing antibodies target Gc conformational changes, suggesting potential for fusion inhibitor development, though no approved drugs exist.

Other names

Glycoprotein 2G2