Marburg virus glycoprotein (MARV GP) (MARV GP)

The Marburg virus glycoprotein (MARV GP) is the sole surface-exposed protein of the Marburg virus and is essential for viral attachment, fusion, and entry into host cells [1, 12]. It is synthesized as a precursor (GP0) that is cleaved by host furin into two subunits, GP1 and GP2, which remain linked by a disulfide bond to form a trimeric spike [2, 11]. The wing domain is a unique structural feature of the Marburgvirus genus, comprising residues at the N-terminus of the GP2 subunit (approximately residues 436–501) that wrap around the GP1 core at the GP1–GP2 interface [5, 7]. This domain is characterized by significant conformational flexibility and plays a dual role in shielding the conserved fusion machinery and serving as a target for protective antibodies [1, 5]. Therapeutic interventions, such as the monoclonal antibodies MR228 and MR235, specifically target the wing domain, while others like MARV16 target the broader GP1–GP2 interface to neutralize the virus by preventing the structural transitions required for membrane fusion [2, 5, 7]. Because GP is the primary target of the host immune response, it is the central component of vaccine candidates like cAd3-Marburg [1, 2]. However, the high flexibility and mutational potential of the wing domain present challenges for the development of broadly effective and escape-resistant therapeutics [1, 6].

Other names

Marburg virus GPMARV glycoproteinGP1/GP2 complexWing domain of MARV GP2Marburg virus spike proteinGP1-GP2 interface

Neutralization of viral entry by blocking the receptor-binding site (RBS) or stabilizing the prefusion GP1-GP2 interface to prevent membrane fusion; induction of Fc-mediated effector functions.