Norovirus genogroup II major capsid protein VP1 (VP1)

The Norovirus genogroup II VP1 capsid protein is the primary structural component of the norovirus virion, which is the leading cause of acute gastroenteritis worldwide [1, 8]. VP1 self-assembles into a T=3 icosahedral capsid consisting of 180 subunits (90 dimers) that protect the viral RNA genome [7, 10]. The protein is structurally divided into a conserved shell (S) domain and a variable protruding (P) domain; the P domain is further subdivided into P1 and P2 subdomains, with P2 being the most exposed and hypervariable region [1, 6]. This P2 subdomain contains the binding sites for histo-blood group antigens (HBGAs), which serve as essential attachment factors for viral entry into host cells [2, 14]. Genogroup II (GII) strains, particularly the GII.4 genotype, are responsible for the majority of human norovirus outbreaks and exhibit significant antigenic drift [12, 13]. As the major antigen, VP1 is the central target for vaccine development, primarily through the use of virus-like particles (VLPs) that mimic the viral structure without being infectious [2, 5]. Therapeutic strategies also include monoclonal antibodies and small-molecule glycomimetics designed to block the VP1-HBGA interaction and prevent infection [2, 16].

Other names

Major capsid protein VP1ORF2 proteinCoat proteinp59CPCapsid protein VP1

Vaccines (VLPs) induce the production of neutralizing antibodies that block the interaction between the VP1 P domain and host HBGA receptors [2, 5]. Monoclonal antibodies and glycomimetics act as attachment inhibitors by binding to the P2 subdomain, thereby preventing viral entry [2, 16].