Marburg virus glycoprotein (GP) (MARV GP)

The Marburg virus glycoprotein (GP) is the sole surface-exposed protein of the Marburg virus (MARV), making it the primary target for the host immune system and therapeutic interventions (UniProt: P0C6X7). It is synthesized as a precursor (GP0) that is proteolytically cleaved by host furin into GP1 and GP2 subunits, which remain linked by a disulfide bond to form a trimeric spike on the viral envelope (Nature, 2011, 477(7364)). GP1 is responsible for attachment to host cell surface factors and subsequent binding to the essential endosomal receptor Niemann-Pick C1 (NPC1), while GP2 contains the fusion machinery required for releasing the viral genome into the cytoplasm (Science, 2015, 348(6235)). Because of its essential role in the viral life cycle, MARV GP is the principal antigen used in vaccine development, including the rVSV-MARV and ChAd3-MARV platforms currently in clinical trials (The Lancet, 2023). Additionally, monoclonal antibodies such as MR191-N target conserved epitopes on the GP to neutralize the virus, providing a potential post-exposure treatment for Marburg virus disease (Cell Host & Microbe, 2017).

Other names

Marburg virus surface glycoproteinGP1,2MARV GPMarburgvirus glycoprotein

Vaccine antigens induce the production of neutralizing antibodies and T-cell responses that target the glycoprotein to prevent viral entry and clear infected cells. Monoclonal antibodies bind to specific epitopes on the GP1 or GP2 subunits to neutralize the virus by blocking receptor binding or membrane fusion (Flyak et al., 2015, Cell).