Major capsid protein VP1 (Norovirus GII.3) (VP1)

Major capsid protein VP1 (Norovirus GII.3) is the primary structural protein of the GII.3 genotype of human norovirus, which is a leading cause of acute gastroenteritis, particularly in infants and young children (NIH, PMC7484443). The protein self-assembles into icosahedral virus-like particles (VLPs) consisting of 180 VP1 monomers, organized into a conserved shell (S) domain and a variable protruding (P) domain (UniProt G0WK46). The P domain contains the P2 subdomain, which is responsible for binding to host histo-blood group antigens (HBGAs) that serve as essential attachment factors for viral entry (NIH, PMC7484443). As the primary target for neutralizing antibodies, VP1 is the central component of most norovirus vaccine candidates, including VLP-based and viral vector-based vaccines like VXA-NVV-104 (JCI, PMC6039665). However, the rapid evolution and antigenic drift of the VP1 protein, especially within the P2 domain, present significant challenges for developing vaccines that provide broad and durable protection (ResearchGate, Hong et al., 2024). Therapeutic research also explores small molecules and monoclonal antibodies, such as 8C7 and 8D1, designed to block the VP1-HBGA interaction to prevent infection (NIH, PMC9784634).

Other names

Major capsid proteinORF2 proteinCapsid protein VP1GII.3 VP1Norovirus GII.3 major capsid protein

Blocking binding to host histo-blood group antigens (HBGAs), neutralization of viral particles, inhibition of viral attachment and entry, and induction of mucosal and systemic immunity including VP1-specific IgA and IgG antibodies.