Zaire ebolavirus glycoprotein, Sudan ebolavirus glycoprotein, and Marburg marburgvirus glycoprotein (EBOV GP, SUDV GP, MARV GP)

The envelope glycoprotein of Zaire ebolavirus, Sudan ebolavirus, and Marburg marburgvirus is the primary surface protein responsible for virus attachment to host cells and catalysis of membrane fusion, enabling viral entry[1][2][3][6]. It is expressed as a single precursor and cleaved into GP1 and GP2 subunits, assembling as a trimeric complex that interacts with host cell surface receptors (including lectins and possibly others)[1][4][6]. The glycoprotein is heavily glycosylated, contributing to immune evasion and posing challenges for vaccine and therapeutic antibody development[3][4]. Neutralizing antibodies and vaccines that target the glycoprotein have demonstrated protective efficacy, and its central role in viral entry makes it a key focus for drug development[1][2][3]. The current entry combines three related but genetically and antigenically distinct glycoproteins; each mediates similar biological functions in its respective virus but therapeutic agents may differ in efficacy across the viruses[2][6].

Other names

Ebola virus glycoproteinEBOV GPEbolavirus envelope glycoproteinSudan virus glycoproteinSUDV GPMarburg virus glycoproteinMARV GP

Neutralizing antibody binding blocks receptor attachment and/or fusion (sterically or allosterically inhibits functional domains of glycoprotein); Small molecule inhibitors block glycoprotein processing (e.g., inhibiting host endosomal cathepsin proteases); Vaccines induce an immune response against the glycoprotein, producing neutralizing antibodies