Norovirus GII.17 capsid protein VP1 (VP1)

Norovirus GII.17 capsid protein VP1 is the primary structural component of the GII.17 genotype of human norovirus, a major cause of epidemic acute gastroenteritis [1, 8]. Encoded by the ORF2 gene, 180 copies of VP1 self-assemble to form the viral capsid, which protects the RNA genome [4, 11]. The protein is organized into a conserved Shell (S) domain and a Protruding (P) domain, with the P2 subdomain being the most surface-exposed and variable region [2, 9]. This P2 subdomain mediates binding to host histo-blood group antigens (HBGAs), which are essential attachment factors for viral entry [5, 14]. The emergence of the GII.17 Kawasaki 308 variant in 2014 highlighted the protein's capacity for rapid antigenic evolution and altered receptor binding, leading to widespread outbreaks [12, 15]. As a therapeutic target, VP1 is the focus of vaccine development, including virus-like particle (VLP) and viral-vectored candidates like HIL-216, which aim to elicit HBGA-blocking antibodies [10, 13, 17]. Additionally, monoclonal antibodies and small-molecule inhibitors are being explored to disrupt the VP1-HBGA interface and prevent infection [14, 16].

Other names

Major capsid proteinViral protein 1ORF2 proteinCapsid protein VP1GII.17 VP1

Induction of neutralizing antibodies or direct binding of inhibitors to the P2 subdomain of VP1 to block the interaction with host histo-blood group antigens (HBGAs), thereby preventing viral attachment and entry into host enterocytes.