Arenavirus envelope glycoprotein complex (GP-C)

The Arenavirus envelope glycoprotein complex, commonly known as GP-C, is a viral surface protein essential for virus attachment and membrane fusion during host cell entry. It comprises three noncovalently associated subunits: GP1 (receptor binding), GP2 (membrane fusion), and a unique stable signal peptide (SSP; ~58 amino acids, myristoylated). Upon synthesis, the precursor GP-C is cleaved by cellular enzymes into its subunits, followed by glycosylation critical for folding and transport. Structural studies show that GP2 adopts a typical class I fusion protein architecture after pH-induced conformational change in the endosome, driving fusion of the viral and host membranes. GP1 binds host receptors (e.g., α-dystroglycan for Old World arenaviruses), but New World arenaviruses use different—and sometimes poorly characterized—receptors. The GP complex is the primary target of the neutralizing antibody response and the main component of experimental vaccines directed against arenavirus infections. The diversity and metastability of the GP1-GP2 interface pose challenges for the development of broadly protective immunogens and therapeutics.

Other names

Arenavirus GP complexArenavirus glycoprotein precursor (GPC)GP1-GP2-SSP complexEnvelope GP complex

Inhibition of viral entry (antibodies or entry inhibitors bind GP1/GP2 and prevent host cell attachment/fusion); Neutralization (antibodies bind exposed epitopes, block receptor engagement/fusion)