Norovirus major capsid protein VP1 (GI.1 and GII.4) (VP1)

Norovirus major capsid protein VP1 (GI.1 and GII.4) is the primary structural component of the norovirus virion, which is the leading cause of acute gastroenteritis worldwide [1, 16]. The VP1 protein self-assembles into icosahedral virus-like particles (VLPs) and is divided into a conserved shell (S) domain and a variable protruding (P) domain [1, 3]. The P domain, specifically the P2 subdomain, contains the binding sites for host histo-blood group antigens (HBGAs), which serve as essential attachment factors for viral entry [5, 13]. As the main target for neutralizing antibodies, VP1 is the central focus of vaccine development, with bivalent formulations targeting the GI.1 and GII.4 genotypes to provide broad protection against common epidemic strains [14, 15]. Therapeutic strategies include the induction of HBGA-blocking antibodies through vaccination or the use of small-molecule inhibitors to prevent viral attachment [12, 14]. However, the rapid antigenic evolution of GII.4 variants, characterized by frequent mutations in the P2 domain, presents a significant challenge for maintaining long-term immunity and vaccine efficacy [7, 11].

Other names

Major capsid protein VP1Norovirus GI.1 VP1Norovirus GII.4 VP1ORF2 proteinNorwalk virus capsid proteinNoV VP1

Induction of neutralizing antibodies that block viral attachment to host histo-blood group antigens (HBGAs) or competitive inhibition of the HBGA binding site on the VP1 P2 domain.