Norovirus GI.1 major capsid protein (VP1)

Norovirus GI.1 major capsid protein (VP1) is the principal structural protein forming the icosahedral capsid of norovirus, which causes a significant proportion of human acute viral gastroenteritis cases worldwide[1][2][4][5][7]. VP1 is encoded by ORF2 and forms 90 stable dimers, totaling 180 monomers per virion, with each monomer comprising distinct domains: a conserved shell (S) domain and a highly variable protruding (P) domain, further divided into P1 and P2 subdomains[1][2][5][7]. The P domain mediates binding to host cellular receptors, namely histo-blood group antigens (HBGA), which are essential for virus entry and tropism[6][7]. VP1 presents key epitopes for neutralizing antibodies, making it a focus of vaccine and antiviral therapeutic development[5][6]. High conformational flexibility of the P domain contributes to immune evasion and adaptability, presenting challenges for vaccine efficacy but also opportunities for inhibition by nanobodies and small molecule HBGA mimics[3][5][6].

Other names

Norwalk virus capsid proteinViral protein 1VP1HuNoV VP1Norovirus major capsid protein

Blockade of virus binding to histo-blood group antigens (HBGA)[6] Capsid destabilization or aggregation via antibody binding[6]