Assembly of homogeneous norovirus-like particles accomplished by amino acid substitution

Abstract

Infection of insect cells with recombinant baculoviruses carrying the VP1 gene from Chiba strain norovirus resulted in the production of 57 and 50 kDa proteins, and the assembly of a smaller, 23 nm form of the virus-like particles (VLPs), together with the normal, 38 nm form of the VLPs. The N-terminal residues of the 57 and 50 kDa proteins were Ala4 and Thr45, respectively. When the tripeptide Leu43-Ala44-Thr45 was changed to Ala-Pro-Val, only 38 nm VLPs were assembled. The 38 nm VLPs showed essentially the same pattern of carbohydrate binding as the 23 nm VLPs, despite the significant difference in the degree of Lewis b antigen binding.