Norovirus GII.4 capsid protein VP1 (VP1 (GII.4))

Norovirus GII.4 capsid protein VP1 is the major structural protein forming the outer shell of human norovirus particles. It assembles into icosahedral capsids with T = 3 or T = 4 symmetry, encapsulating the viral RNA genome. The VP1 protein contains an internal N-terminal arm, a shell (S) domain, and a protruding (P) domain. The P domain includes the hypervariable P2 subdomain, which is critical for host cell attachment via glycan/histoblood group antigen binding and determines antigenicity. Sequence variation in the P2 domain drives immune escape and frequent emergence of epidemic variants. VP1 virus-like particles are used in norovirus vaccine development, making it a major therapeutic and diagnostic target[1][2][3][4].

Other names

Major capsid protein VP1 (GII.4)GII.4 VP1Norovirus GII.4 VP1 capsid protein

Drugs and antibodies under investigation bind the VP1 protein to block cell attachment or induce neutralizing immune responses (vaccine mechanism)[1][3]. Vaccine-induced antibodies recognize conformational epitopes on VP1, particularly the hypervariable P2 domain.