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The Rift Valley fever virus (RVFV) Gc glycoprotein is a critical structural component of the viral envelope and a member of the class II fusion protein family [UniProt, PNAS]. It is synthesized as part of a polyprotein precursor from the viral M segment and is subsequently cleaved into the Gn and Gc subunits, which form heterodimers on the virion surface [UniProt, MDPI]. Gc is primarily responsible for mediating the fusion between the viral envelope and the host cell's endosomal membrane, a process activated by the low pH environment of the endosome [PNAS, ResearchGate]. Because it contains the fusion loop and major neutralizing epitopes, Gc is a primary target for the development of vaccines and antiviral strategies, including monoclonal antibodies like NA137 and fusion-inhibiting peptides such as RVFV-6 [NIH, MDPI]. Currently, there are no licensed therapeutics or vaccines for human use that specifically target the RVFV Gc glycoprotein, making it a high-priority target for emerging infectious disease research [NIH, MDPI].
Neutralization of viral entry and inhibition of pH-dependent membrane fusion
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