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The rotavirus VP8 protein, often referred to as VP8*, is the distal (N-terminal) domain of the viral spike protein VP4. Upon proteolytic cleavage of VP4, two subunits are generated: the N-terminal VP8* and the C-terminal VP5*. The primary function of VP8* is to mediate initial attachment of rotavirus particles to host cell surface receptors, a critical step for viral entry and infection. It exhibits a galectin-like fold and binds to sialic acids (in animal RVs) or histo-blood group antigens (HBGAs) in human RVs, thus initiating the infection cycle.
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