ArticlebioRxiv : the preprint server for biology2025
Mutational Analysis of Human Norovirus VP2 Elucidates Critical Molecular Interactions for Virus Assembly.
Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Human noroviruses ( Importance: Human noroviruses (HuNoVs) are the leading cause of epidemic and sporadic gastroenteritis in all age groups worldwide. Yet, we currently lack vaccines or therapeutics for these pathogens. Knowledge about HuNoV biology is limited, including the fundamental mechanisms governing particle assembly. Modern structural techniques have not resolved the complete structure of pandemic GII.4 norovirus that includes the localization of the interior capsid proteins VP2 and VPg. Furthermore, VP2's functional role(s) during infection remains obscure. Studies of feline and murine caliciviruses show VP2 may be involved in delivering the viral genome into cells, suggesting it synergizes with VP1 and VPg. We identify a motif on the N-terminal α-helical domain of VP2, adjacent to a unique insertion site, that is essential for interaction with the major capsid protein VP1. We show VP2 uniquely binds the translation initiation protein, VPg, via its disordered C-terminus. These findings reveal principles of HuNoV capsid protein interactions and highlight VP2 as a bridge facilitating capsid assembly.
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