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The Sudan ebolavirus glycoprotein (GP) is the sole surface protein expressed on the virion and is essential for viral attachment to host cells and catalysis of membrane fusion, enabling entry into target cells. It forms trimeric spikes on the virus surface, with each spike composed of a GP1-GP2 heterodimer. GP1 serves as the receptor-binding subunit, while GP2 mediates membrane fusion. The primary known receptor facilitating entry is human Niemann-Pick C1 (NPC1), an endosomal/lysosomal cholesterol transporter. Antibodies targeting this protein can neutralize infection. The glycoprotein’s ability to mediate efficient cell entry underlies its role as a major determinant of pathogenicity, making it a prime target for vaccine design efforts as well as antiviral drug development aimed at blocking receptor engagement or membrane fusion steps.
Antibodies targeting the glycoprotein can neutralize infection by blocking receptor engagement or membrane fusion.
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