Noroviruses account for the bulk of infectious gastroenteritis in adults worldwide. Although Norovirus gastroenteritis is self-limiting, the economic burden of infection is considerable and uncontrolled manifestations can result in death. Noroviruses form an antigenically diverse group of agents and cross-reactive immunity is poor. These features present a considerable challenge for vaccine development. Current approaches have been based on the use of empty virus-like particles produced by self-assembly of the virus capsid protein. In this study we employed a new approach for engineering stable particles of Hawaii virus capsid protein by deleting those immunodominant regions (P2subdomains) that evoke type-specific responses and bridging the resulting gap with a synthetic poly-glycine chain. This construct was expressed using the baculovirus system and the obtained purified protein was examined by EM which showed that the new engineering approach is permitting some form of structural assembly. Our study points a way to produce a more pan-reactive vaccine in future studies by producing antisera directed predominantly at the most conserved S-domain of Norovirus capsid.