Marburg virus glycoprotein (Angola strain) (MARV GP)

The Marburg virus glycoprotein (GP) is the sole surface-exposed protein of the Marburg virus, a member of the Filoviridae family (UniProt: P35253). It is a Class I viral fusion protein that mediates host cell attachment, endocytosis, and subsequent membrane fusion within the endolysosomal compartment by interacting with the host receptor Niemann-Pick C1 (NPC1) (Kuhn et al., 2006). The Angola strain is particularly notorious for its high case-fatality rate, reaching up to 90% in documented outbreaks (WHO, 2023). GP is synthesized as a precursor that is cleaved by host furin into GP1 (attachment) and GP2 (fusion) subunits, which remain linked by a disulfide bond. As the primary target for the host's neutralizing antibody response, GP is the central focus of vaccine development and therapeutic monoclonal antibody research, such as the development of MR191 (Flyak et al., 2015). Therapeutic strategies targeting this protein aim to prevent the virus from entering host cells, thereby neutralizing the infection and reducing viral load.

Other names

GPSpike proteinMarburg virus surface glycoproteinMARV-Angola GPGP1,2

Monoclonal antibodies target the glycoprotein to neutralize the virus by blocking attachment to the host cell receptor Niemann-Pick C1 (NPC1) or preventing the conformational changes required for membrane fusion.