Norwalk virus capsid protein (VP1) (VP1)

The Norwalk virus capsid protein, specifically the major structural protein VP1, is the primary component of the Norwalk virus shell, which is the prototype strain of the Norovirus genus (UniProt P21942). VP1 self-assembles into virus-like particles (VLPs) and consists of two distinct domains: the Shell (S) domain, which forms the internal scaffold, and the Protruding (P) domain, which extends outward from the surface (PubMed: 12551977). The P domain, particularly the P2 subdomain, contains the binding sites for histo-blood group antigens (HBGAs), which serve as essential co-receptors for viral attachment to human intestinal cells (PubMed: 24957083). As the most immunodominant protein on the viral surface, VP1 is the principal target for the development of vaccines and neutralizing antibodies. Therapeutic strategies focusing on VP1, such as those employed by Vaxart's VXA-NVV-104, aim to block viral docking and entry, providing protection against acute gastroenteritis, a leading cause of non-bacterial diarrhea worldwide (ClinicalTrials.gov NCT03897309).

Other names

Major capsid proteinNV VP1Capsid protein VP1Norwalk virus VP1 protein

Vaccines and experimental inhibitors target the VP1 protein to induce neutralizing antibodies or physically block the interaction between the viral P2 subdomain and host histo-blood group antigens (HBGAs), preventing viral attachment and entry (PubMed: 24957083).