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The norovirus capsid protein, also known as VP1, is the major structural protein forming the outer shell of noroviruses. It plays a central role in viral assembly, host cell recognition, and immune response evasion. The capsid is composed of 180 copies of VP1 arranged in a T=3 icosahedral symmetry. Each VP1 monomer (~58–60 kDa) consists of three main regions: N-terminal arm (N), Shell domain (S) and Protruding domain (P). The S domain mediates formation of the interior shell; both S and P domains are essential for proper capsid assembly. The P2 subdomain binds to histo-blood group antigens (HBGAs), which serve as attachment factors or receptors on host cells.
Attachment inhibition (potential)
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