Andes virus envelope glycoprotein Gc (Gc (Andes virus))

The **Andes virus envelope glycoprotein Gc** is one of two major surface glycoproteins (Gn and Gc) present on the surface of Andes virus, a highly pathogenic hantavirus. Gc and Gn form heterodimers that further organize into tetrameric spikes, composing the viral envelope lattice. Gc is a class II fusion protein: upon uptake of the virus by endocytosis, acidic pH in the endosome induces a conformational change in Gc, exposing a fusion loop that inserts into the endosomal membrane, thereby driving membrane fusion and the delivery of the viral genome into the host cell[1][2][3][5][7][8]. Gc’s structure and function make it the key molecular actor in viral entry, and it is the principal target of neutralizing antibodies, which block virus-cell fusion and are critical for host defense[1][2][7][8]. Mutational analysis and high-resolution structural studies have elucidated unique hantavirus-specific features, such as an extended N-terminal segment involved in trimerization, differentiating it from other class II viral fusion proteins[5]. Gc’s sole known pharmacologic interactions are with neutralizing antibodies, but it remains under intense study for therapeutic and vaccine targeting due to its central role in infection[1][2][7][8].

Other names

Gc glycoproteinAndes virus GcANDV Gc

Targeted by virus-neutralizing antibodies; Mediates endosomal membrane fusion by pH-dependent conformational change