The norovirus N-terminal protein varies in relative size across the genus, and the encoding sequence bears no similarity to other cellular or viral proteins. Alignment of the N-term protein sequences of various noroviruses indicates little similarity between genogroups within the first 180 residues, however towards the Cterminal end of the protein similarity between the amino acid residues increases. Recent studies investigating the functions of the Norwalk virus N-terminal protein have successfully demonstrated association with the Golgi apparatus in transfected cells [15] . In addition this study also identified a picornaviral 2B like region within the N-terminal protein, suggesting that the protein is involved with host cell membrane interactions, reinforcing other findings that have suggested that the Norwalk virus N-terminal protein disrupts intracellular protein trafficking, including proteins destined for the host cell membrane [16] . A 3C protease-mediated cleavage event within the N-terminal protein (37 kDa) was described for Camberwell virus, a genogroup 2 norovirus, yielding proteins of 22 kDa and 15 kDa [17] . Based on these observations and location within the genome it was hypothesised that the Nterminal protein of noroviruses corresponds to the 2AB region in picornaviruses.