Zaire ebolavirus glycoprotein (EBOV GP) glycan cap (EBOV GP glycan cap)

The Zaire ebolavirus glycoprotein (GP) is the primary protein on the viral envelope, mediating host cell attachment, endosomal fusion, and entry (UniProt P87666). The glycan cap is a specific domain within the GP1 subunit that covers the conserved receptor-binding site (RBS), acting as a shield against the host immune system (PubMed 25470055). During the viral entry process, the glycan cap and the mucin-like domain must be proteolytically removed by host endosomal proteases, such as cathepsins B and L, to expose the binding site for the Niemann-Pick C1 (NPC1) receptor (PubMed 18617644). Monoclonal antibodies targeting the glycan cap epitope, such as odesivimab (a component of Inmazeb) and 13C6 (a component of ZMapp), interfere with this process by blocking enzymatic cleavage or by facilitating the clearance of viral particles through Fc-mediated effector functions like antibody-dependent cellular cytotoxicity (PubMed 33091368). While the glycan cap is a major target for the humoral immune response, its high degree of glycosylation and potential for mutational drift present challenges for long-term therapeutic efficacy and vaccine development (PubMed 27185960).

Other names

EBOV GP1 glycan capEbola virus glycoprotein glycan capGP glycan cap epitopeZaire ebolavirus GP1 glycan cap

Inhibition of endosomal proteolytic cleavage of GP1 by cathepsins, neutralization of viral entry, and induction of Fc-mediated effector functions such as antibody-dependent cellular phagocytosis (ADCP) and antibody-dependent cellular cytotoxicity (ADCC).