Hantavirus envelope glycoprotein Gn and Gc (Gn and Gc)

Hantavirus envelope glycoproteins Gn and Gc are membrane-anchored proteins expressed from the viral M segment as a GPC precursor that is cleaved into mature forms[4][5]. Gn and Gc assemble as heterodimers, which further organize into tetrameric spike complexes on the viral envelope, creating a lattice structure that decorates the virion surface[1][2][5]. These glycoproteins are essential for viral entry—Gn/Gc mediates host cell recognition, endocytosis, and Gc specifically mediates the fusion of the viral and endosomal membranes at acidic pH during cell entry[2][3][5]. Gc is classified as a class II fusion protein, undergoing substantial conformational changes to expose fusion peptides and enable membrane fusion[2][3][5]. The spike complexes formed by Gn/Gc are major targets of neutralizing antibodies, which can prevent infection by blocking glycoprotein function[1][5]. Beyond entry, the cytoplasmic tails of Gn and Gc play a critical role in virion assembly and budding by interacting with the viral nucleoprotein and other assembly components[3][4]. There are currently no clinically approved drugs specifically targeting Gn or Gc, but multiple investigational monoclonal antibodies and viral entry inhibitors are being explored as potential therapeutics.

Other names

GnGcGlycoprotein NGlycoprotein CG1 (Gn)G2 (Gc)

Neutralizing antibodies block glycoprotein function to prevent virus entry; Fusion inhibitors stabilize prefusion state or block conformational change of Gc; Small molecules or peptides may disrupt glycoprotein assembly, fusion, or receptor binding (experimental)