Major capsid protein VP1 (Norovirus Genogroup II genotype 4) (VP1)

The Major capsid protein VP1 (Norovirus Genogroup II genotype 4) is the primary structural protein forming the norovirus capsid, organized in a T=3 icosahedral lattice of 180 subunits. It is functionally divided into a conserved shell (S) domain that forms the interior scaffold and a highly variable protruding (P) domain that extends from the viral surface. The P domain, specifically the P2 sub-domain, is critical for viral pathogenesis as it contains the binding pockets for host Histo-Blood Group Antigens (HBGAs), which serve as primary attachment factors for entry into human cells. Norovirus GII.4 is the most prevalent genotype responsible for the majority of acute gastroenteritis outbreaks worldwide and is known for its rapid molecular evolution. This evolution leads to the emergence of new variants that can evade existing population immunity, making the VP1 protein a central target for vaccine design. Current therapeutic strategies include virus-like particle (VLP) vaccines, mRNA vaccines, and oral viral vector-based platforms that express VP1 to elicit robust neutralizing antibody responses. These antibodies aim to prevent infection by blocking the interaction between the VP1 P2 domain and host cell receptors. [1, 4, 11, 16]

Other names

Capsid protein VP1GII.4 VP1Major structural protein VP1HuNoV GII.4 VP1

Induction of neutralizing antibodies that competitively block the binding of the VP1 P2 domain to host Histo-Blood Group Antigens (HBGAs), thereby preventing viral attachment and entry.