Rift Valley fever virus Gn glycoprotein (Gn)

The Rift Valley fever virus (RVFV) Gn glycoprotein is a primary structural component of the viral envelope, encoded by the M segment of the virus's tripartite RNA genome [1.2.1, 1.3.2]. It forms a heterodimeric complex with the Gc glycoprotein, which assembles into a T=12 icosahedral lattice on the surface of the virion [1.3.5]. Gn is essential for viral entry, as its head domain (GnH) mediates attachment to host cell receptors, most notably the low-density lipoprotein receptor-related protein 1 (LRP1) and DC-SIGN [1.3.1, 1.3.2, 1.3.4]. Beyond attachment, Gn contains a Golgi localization signal that directs the Gn/Gc complex to the Golgi apparatus, the site of viral budding, and its cytoplasmic tail is responsible for recruiting the viral nucleocapsid (N) and RNA-dependent RNA polymerase (RdRp) for assembly [1.2.2, 1.4.1]. Crucially, Gn acts as a shield for the Gc fusion protein, preventing the premature exposure of Gc's hydrophobic fusion loops until the virus reaches the acidic environment of the endosome [1.2.4, 1.3.1]. Because it is the most accessible protein on the viral surface and the primary target for neutralizing antibodies, Gn is the leading candidate for vaccine development and therapeutic monoclonal antibody targeting [1.2.5, 1.3.3]. While no vaccines or drugs are currently FDA-approved, several neutralizing antibodies such as RVFV-268, RVFV-379, and RVFV-140 are being investigated for their ability to block viral entry and prevent disease progression [1.3.2, 1.3.5].

Other names

G2 glycoproteinRVFV GnM-segment glycoproteinEnvelope glycoprotein Gn

Neutralization of viral infectivity by blocking receptor binding or preventing the prefusion-to-postfusion conformational change of the Gn/Gc complex.