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The **Norovirus genotype I.1 capsid protein VP1** is the principal structural protein forming the icosahedral capsid of Norwalk virus, the prototypical human norovirus (genogroup I, genotype 1). VP1, approximately 58 kDa, assembles into 180 copies per viral particle, creating a shell (S domain) and surface protrusions (P domain, further divided into P1 and P2 subdomains). The P2 subdomain contains binding sites necessary for attachment to host carbohydrates (histo-blood group antigens; HBGAs) and epitopes for neutralizing antibodies, making VP1 a crucial determinant of host range, immune response, and antigenic diversity[1][2][3][4][7]. VP1 forms virus-like particles in vitro, which serve as the basis for norovirus vaccine development. However, the capsid's flexibility and antigenic variability present challenges for lasting immunity and vaccine efficacy. This protein does not act as an enzyme or receptor itself but is a primary immune and vaccine target in norovirus infection and prevention[1][2][3][4][6][7].
Target for vaccine-induced neutralizing antibodies
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