Bundibugyo virus glycoprotein (BDBV GP)

The Bundibugyo virus glycoprotein (BDBV GP) is the primary surface protein of the Bundibugyo ebolavirus, responsible for mediating host cell attachment, endocytosis, and membrane fusion [1]. It is expressed as a trimeric spike consisting of GP1 and GP2 subunits, which are produced through the proteolytic cleavage of a precursor protein by host furin [1, 2]. GP1 facilitates binding to host cell surface lectins and the intracellular receptor Niemann-Pick C1 (NPC1), while GP2 contains the machinery necessary for the fusion of the viral envelope with the host endosomal membrane [2, 3]. As the sole protein exposed on the virion surface, BDBV GP is the critical target for the host immune response and the primary focus for the development of vaccines and therapeutic monoclonal antibodies [3, 4]. Drugs targeting this protein, such as the MBP134 antibody cocktail, aim to neutralize the virus by sterically hindering receptor binding or preventing the structural transitions required for fusion [2]. Understanding the specific structure of the BDBV GP is essential for developing pan-ebolavirus therapeutics, as it shares structural similarities but also distinct antigenic differences with the more common Zaire ebolavirus glycoprotein [2, 3].

Other names

Bundibugyo ebolavirus glycoproteinBDBV GPGPEnvelope glycoproteinGP1/GP2

Monoclonal antibodies bind to specific epitopes on the GP1 or GP2 subunits, neutralizing the virus by blocking attachment to host receptors like NPC1 or preventing the conformational changes required for membrane fusion [2, 3].