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Hantavirus glycoprotein Gc is a viral envelope protein essential for virus entry into host cells and a major target for the immune response. It is encoded by the M segment of the hantavirus genome and forms a heterodimer with glycoprotein Gn, assembling into tetrameric spikes that create a surface lattice on the virus[1][5][9]. Gc is classified as a **class II fusion protein**, structurally and functionally analogous to fusion proteins found in other enveloped viruses. During infection, Gn/Gc spikes engage host cell receptors, and upon endocytosis and acidification of the endosome, Gc undergoes an irreversible conformational change to mediate fusion between the viral envelope and the endosomal membrane, allowing viral genome release into the cytoplasm[3][6][8]. Gc is the **membrane fusion effector** and the principal target of neutralizing antibodies, making it a candidate for vaccines and antiviral drug development[1][3][8]. The structure of Gc has been resolved in its post-fusion trimer conformation, and its functional regions offer potential targets for membrane fusion inhibitors and antibody therapies[8]. There are currently no approved drugs that specifically target Gc, but research efforts are exploring antivirals that disrupt its conformational changes and monoclonal antibodies designed to neutralize its activity[8][9].
Inhibition of the class II membrane fusion activity, preventing viral envelope fusion with host endosomal membrane Neutralization via binding and blocking conformational changes essential for fusion
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