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Rift Valley fever virus glycoproteins consist of two major envelope proteins, **Gn (glycoprotein N)** and **Gc (glycoprotein C)**, both encoded by the M segment of the viral genome[1][2][3]. These glycoproteins are expressed as a polyprotein precursor and processed by host cell proteases[3]. Gn and Gc assemble as heterodimers on the virion surface, forming the outer viral envelope and mediating critical steps in the virus life cycle, including attachment to host cell receptors and fusion of the viral and cellular membranes necessary for entry[2][6][8]. Gc is identified as the membrane fusion effector and exhibits a class II fusion protein architecture similar to proteins found in flaviviruses and alphaviruses[6]. Neutralizing antibodies primarily recognize epitopes on Gn and Gc, making them the main targets for vaccine and therapeutic antibody development[1][2][5]. Recombinant versions of these glycoproteins are also valuable for diagnostic assays and studies investigating viral pathogenesis and immune response[3]. Therapies targeting RVFV glycoproteins are under development, with small molecule inhibitors and monoclonal antibodies representing leading strategies[1].
Inhibition of glycoprotein-mediated cell entry (block receptor attachment or membrane fusion)[1] Neutralization by monoclonal or polyclonal antibodies targeting surface glycoproteins[1][2].
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