Norovirus major capsid protein VP1 (Viral Protein 1) (VP1)

Norovirus VP1 is the major structural protein of human norovirus, a non-enveloped icosahedral virus approximately 27 nm in diameter that causes acute gastroenteritis. The protein comprises 180 copies arranged as 90 dimers with T=3 icosahedral symmetry, organized into shell (S) and protruding (P) domains that establish the capsid architecture. The P2 subdomain, located at the virion surface, contains the binding pocket for histo-blood group antigens (HBGAs), which serve as cellular attachment factors essential for infection.[3][5] Recent structural analyses reveal that VP1 exhibits significant conformational flexibility, particularly in the P domain, which enables both receptor binding and immune evasion through antibody escape mechanisms.[3] While VP1 itself is not a traditional therapeutic target for direct inhibition, it represents an important focus for vaccine development and the identification of vulnerable epitopes that could be exploited for therapeutic interventions targeting norovirus infection.

Other names

Major capsid proteinCapsid protein VP1Shell protein (S domain)Protruding domain protein (P domain)

Not applicable (structural protein, not a therapeutic target)