Norovirus genogroup I major capsid protein VP1 (VP1)

The Norovirus genogroup I major capsid protein VP1 is the primary structural component of the norovirus virion, responsible for forming the icosahedral shell that protects the viral RNA (UniProt: P03311). It is organized into two main domains: the conserved Shell (S) domain, which forms the inner core, and the variable Protruding (P) domain, which extends outward and mediates interaction with host cell receptors (PubMed: 10521341). Specifically, the P2 subdomain within the P domain contains the binding sites for histo-blood group antigens (HBGAs), which are essential for viral attachment and entry into human intestinal cells (PubMed: 12743361). As the most exposed part of the virus, VP1 is the principal target for the host immune response and the primary antigen used in the development of virus-like particle (VLP) vaccines, such as HIL-214 (PubMed: 22150035). Therapeutic strategies focusing on VP1 aim to elicit neutralizing antibodies that block the interaction between the P2 domain and HBGAs, thereby preventing infection (PubMed: 25135944). However, the high genetic diversity and rapid evolution of the VP1 protein across different norovirus strains present significant challenges for broad-spectrum vaccine efficacy (PubMed: 26184931). This protein's ability to self-assemble into non-infectious VLPs has made it a cornerstone of norovirus vaccine research and diagnostic assay development.

Other names

Major capsid proteinGI VP1Capsid protein VP1VP1 proteinNorwalk virus major capsid protein

Induction of neutralizing antibodies that block viral attachment to histo-blood group antigens (HBGAs) on host cells.