Hantaan virus envelope glycoprotein (None commonly used (Gn and Gc subunits may be abbreviated individually))

The Hantaan virus envelope glycoprotein is a heterodimeric viral surface complex composed of two membrane-anchored subunits: Gn and Gc. Both are encoded by the viral M genomic segment and generated via cleavage from a single polyprotein precursor. These glycoproteins assemble into tetrameric spike lattices decorating the viral lipid envelope, mediating essential roles in host cell entry by interacting with cellular receptors (notably β3-integrins for pathogenic hantaviruses), facilitating receptor-mediated endocytosis, and catalyzing endosomal membrane fusion through conformational change, primarily attributed to the Gc subunit[1][2][3][5][6]. The glycoproteins are the exclusive viral targets of neutralizing antibodies and are central to vaccine and antiviral therapeutic designs[3][6][7]. They additionally engage host immune evasion mechanisms and direct the assembly and budding of new virions[5][8]. The Gn and Gc envelope glycoproteins are highly conserved among hantaviruses, with variations influencing pathogenic potential and immune recognition[2][3][5][6]. Their dysfunction or structural alteration can prevent viral infection, establishing them as key therapeutic targets for Hantaan virus and related hantavirus diseases.

Other names

Hantaan virus glycoproteinHantaan virus surface glycoproteinHantaan virus GnHantaan virus GcHTNV envelope glycoprotein

Neutralizing antibodies block glycoprotein-mediated cell entry and membrane fusion[3][6]. Fusion inhibitors would prevent the conformational change required for membrane fusion. Vaccine-induced antibodies prevent infection by binding to functional glycoprotein epitopes.