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Marburg and Ravn virus glycoprotein (GP) is a surface protein forming homotrimeric spikes on the viral envelope, comprised of GP1 and GP2 subunits. GP1 contains a receptor binding domain, glycan cap, and a heavily glycosylated mucin-like domain responsible for host receptor interactions. GP2 mediates fusion of the viral and host cellular membranes. During cell entry, the glycoprotein is cleaved and rearranged, enabling binding to the host NPC1 receptor and triggering membrane fusion. This molecule is a principal determinant of viral infectivity and tropism, overriding cell and tissue specificity and is responsible for immune evasion. The glycoprotein is at the center of ongoing research on vaccine candidates and neutralizing therapies for Marburg virus disease, but as of now, no approved therapies or vaccines exist.
Antibody binding blocks glycoprotein-mediated host cell attachment and fusion, neutralizing virus entry; Small molecule inhibitors block interaction with host entry factors (e.g., NPC1)
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