Norovirus GII.3 capsid protein VP1 (VP1)

Norovirus GII.3 capsid protein VP1 is the primary structural component of the GII.3 genotype of human norovirus, which is a leading cause of acute gastroenteritis, particularly in infants and young children [2, 3]. The protein is organized into a shell (S) domain that forms the icosahedral core and a protruding (P) domain, where the P2 subdomain contains the critical binding sites for human histo-blood group antigens (HBGAs) that serve as attachment receptors for viral entry [2, 4, 12]. As the dominant surface antigen, VP1 is the central target for vaccine development, including virus-like particle (VLP) and mRNA-based platforms designed to elicit blockade antibodies that disrupt viral attachment [1, 6, 10]. Therapeutic research also focuses on small-molecule carbohydrate mimics, such as fucosyllactose, which competitively bind the P2 domain to prevent infection [5, 11]. However, the rapid evolution of the VP1 region and the emergence of new antigenic variants present significant challenges for maintaining long-term vaccine efficacy and achieving broad-spectrum protection [3, 7, 8].

Other names

Major capsid protein VP1Coat proteinp59ORF2 proteinCapsid protein VP1

Induction of blockade antibodies that prevent viral attachment to histo-blood group antigens (HBGAs); competitive inhibition of the HBGA-binding pocket on the P2 domain; neutralization of viral entry into intestinal epithelial cells.