Ebola virus Glycoprotein/GP RBD His Tag Protein, Ebola virus-AHX24649

The Ebola virus glycoprotein (GP) is a key protein responsible for its pathogenicity. As a class I fusion protein, it forms a trimeric structure on the viral surface composed of GP1 and GP2 subunits linked by disulfide bonds. During viral entry, the receptor-binding domain of GP1 interacts with various host cell receptors (such as TIM-1 and NPC1), while GP2 mediates the fusion between the viral and host cell membranes, facilitating the release of the viral genome into the cytoplasm.Beyond mediating viral entry, GP exerts multiple complex pathogenic effects during later stages of infection. It downregulates the expression of host cell surface adhesion molecules, such as integrins, disrupting intercellular connections and compromising vascular integrity, which may contribute to the hemorrhagic symptoms characteristic of Ebola virus disease. In terms of immune regulation, GP interacts with host TLR4, activating immune cells and triggering a severe cytokine storm, while simultaneously inducing bystander death of T lymphocytes, thereby impairing adaptive immune responses. Additionally, GP counteracts host antiviral factors like BST2/tetherin and acts as a "molecular decoy" to neutralize antibodies, enabling effective immune evasion. These multifunctional properties collectively establish GP as a central target for studying Ebola virus pathogenesis and designing vaccines.