Norovirus major capsid protein VP1 (VP1) (VP1)

The Norovirus major capsid protein VP1 is the primary structural component of the norovirus virion, an icosahedral, non-enveloped virus responsible for the majority of global epidemic gastroenteritis cases (UniProt P03313). The protein is organized into 180 subunits that form two distinct domains: the conserved Shell (S) domain, which protects the viral RNA, and the Protruding (P) domain, which is further divided into P1 and P2 subdomains. The P2 subdomain is the most surface-exposed region and contains the binding sites for host histo-blood group antigens (HBGAs), which are critical for viral attachment and entry into host cells (Prasad et al., 2014, PMID: 25214518). Because it is the primary target for neutralizing antibodies, VP1 is the central focus of norovirus vaccine development, including virus-like particle (VLP) and mRNA-based platforms. Therapeutic candidates like HIL-214 and mRNA-1403 aim to elicit antibodies that block the P domain's interaction with host receptors. However, the significant antigenic diversity among norovirus strains, particularly within the GII.4 lineage, necessitates the development of multivalent vaccines and poses a challenge for long-term efficacy due to frequent antigenic drift.

Other names

Major capsid proteinVP1 proteinNorovirus VLPCapsid protein VP1Norovirus capsid antigenCapsid protein VP2 (minor component)

Induction of neutralizing antibodies that specifically target the P2 subdomain of the VP1 protein to block the interaction between the viral capsid and host histo-blood group antigens (HBGAs), thereby preventing viral attachment and subsequent entry into enterocytes (Tan & Jiang, 2014, PMID: 24957088).