Hantavirus glycoprotein Gn (Gn)

Hantavirus glycoprotein Gn is a major viral surface protein encoded by the M segment of the hantavirus genome, expressed as part of a precursor polypeptide GPC that is processed to yield the mature Gn and its partner Gc[1][3]. Gn and Gc form stable heterodimers, which then assemble into tetrameric spikes that create a square-shaped lattice on the viral surface, essential for virus particle architecture and infectivity[1][4][5]. Gn serves a dual role in mediating interactions with host cell receptors (such as β3-integrins) and maintaining the stability of the viral fusion protein (Gc) prior to entry, where it undergoes pH-dependent conformational changes to facilitate membrane fusion and entry into host cells[2][4][6][8]. The Gn-Gc complex is the principal target of neutralizing antibodies and is a key focus of therapeutic and vaccine strategies, though there are no FDA-approved drugs directly targeting Gn at this time[5][7]. Structural analysis reveals the Gn ectodomain has a conserved α/β fold across hantavirus species, acting as the membrane-distal component of the viral spike[2][8]. Gn is critical for infection and pathogenesis of diseases such as hemorrhagic fever with renal syndrome and hantavirus pulmonary syndrome[2][4].

Other names

GnG1 glycoprotein (historical context, sometimes denoted as G1 instead of Gn)Envelope glycoprotein Gn

For neutralizing antibodies: Block interaction of Gn-Gc spikes with host cell receptors, prevent entry by sterically hindering or destabilizing fusion complex formation\n- For experimental antivirals: Mechanisms would involve interfering with Gn-mediated assembly, receptor binding, or stability of the fusion complex