ZEBOV

Zaire ebolavirus (ZEBOV) is a highly pathogenic filovirus whose envelope glycoprotein (GP) mediates host-cell attachment, endosomal entry, and membrane fusion, making GP the central determinant of viral infectivity and a primary target for mechanistic and translational research^[1][2]. After cellular uptake through endocytic pathways, proteolytic processing of GP exposes a receptor-binding site that engages the host cholesterol transporter Niemann-Pick C1 (NPC1), a critical intracellular receptor required for productive viral entry^[3][4][5]. Mechanistically, structural studies demonstrated direct interaction between cleaved GP and NPC1, linking receptor recognition to conformational changes that promote membrane fusion and cytoplasmic release of the viral genome^[4][5]. In disease models, genetic or pharmacological disruption of NPC1 markedly reduces susceptibility to Ebola virus infection, establishing the GP-NPC1 axis as a key pathway in ZEBOV pathogenesis and a valuable experimental system for studying filovirus host dependence^[3][6]. Compared with other viral proteins, GP is uniquely exposed on the virion surface and therefore serves as the principal antigen in vaccine development, including recombinant vesicular stomatitis virus-based platforms that express ZEBOV GP and induce protective immune responses^[7][8]. For experimental applications, inhibitors that block GP-NPC1 engagement or interfere with GP-mediated entry are widely used to investigate viral entry mechanisms and evaluate candidate antiviral strategies targeting early stages of infection^[3][6].