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Rift Valley Fever Virus (RVFV) surface glycoproteins, Gn and Gc, are the primary structural components of the viral envelope and play a critical role in the virus's life cycle [1, 6]. Encoded by the M segment of the viral genome, these proteins form heterodimeric complexes that assemble into an icosahedral lattice on the virion surface [1, 15]. Gn is primarily responsible for host cell attachment, interacting with receptors such as LRP1 and DC-SIGN, while Gc acts as a class II fusion protein that mediates the merger of the viral and endosomal membranes under acidic conditions [5, 14, 15]. Because they are the most exposed viral antigens, Gn and Gc are the principal targets for the host's neutralizing antibody response and are the focus of vaccine and therapeutic antibody development [8, 10]. Experimental treatments include monoclonal antibodies like RVFV-379 and RVFV-268, as well as vaccine candidates such as ChAdOx1 RVFV, which aim to prevent infection by blocking viral entry [7, 11]. Understanding the structural arrangement and function of these glycoproteins is essential for developing effective countermeasures against Rift Valley Fever, a significant zoonotic disease [1, 10].
Neutralization of viral entry by blocking host cell attachment or membrane fusion.
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