Norovirus genogroup I genotype 1 capsid protein VP1 (VP1)

The Norovirus genogroup I genotype 1 capsid protein VP1 (VP1) is the primary structural protein that forms the icosahedral shell (capsid) of norovirus particles, specifically the Norwalk virus (GI.1)[1][2][4][5]. It is approximately 58 kDa and self-assembles into a shell with T=3 symmetry, composed of 180 copies arranged as 90 dimers[1][2][5]. VP1 is organized into two main domains: the conserved shell (S) domain and the protruding (P) domain, the latter involved in host cell receptor binding via histo-blood group antigens (HBGAs)[1][2]. The P domain is further divided into P1 and P2 subdomains, with P2 being surface-exposed and highly variable—serving as an important antigenic and receptor-binding region[1]. VP1’s sequence and structural features allow genotyping and epidemiological tracking, while its immunodominant surface makes it the main antigen targeted by protective immune responses, as well as a platform for norovirus vaccine development in the form of virus-like particles (VLPs)[2][5]. Antibodies targeting VP1, particularly those that block the HBGA-binding interface, can neutralize the virus, although rapid VP1 antigenic variation can undermine lasting immunity[1][2]. No approved antiviral drugs directly target VP1, but it is critical for both basic virology research and translational vaccine design.

Other names

Norwalk virus major capsid proteinmajor structural protein VP1NV VP1GI.1 VP1

Elicitation of neutralizing antibodies (for VLP-based vaccines), blockade of virus attachment to host cell receptors (targeting HBGA binding sites)