Abstract
Human JC virus (JCV) belongs to the family of Polyomaviridae. The viral capsid is composed of 72 capsomeres. Five VP1 molecules make up a capsomere structure. To investigate the minimal sequences on JCV VP1 polypeptide required for capsid assembly, the first 12 ( j N12) and 19 ( j N19) amino acids at the Nterminus and the last 16 ( j C16), 17 ( j C17), and 31 ( j C31) amino acids at the C-terminus of VP1 were truncated and expressed in E. coli . The VP1 proteins of j N12 and j C16 were able to self-assemble into a virus-like particle similar to that of wild-type (WT) VP1. However, the mutant proteins of j N19, j C17, and j C31 formed a pentameric capsomere structure as demonstrated by a 10-50% sucrose gradient centrifugation and electron microscopy. These results suggest that the 12 amino-terminal and 16 carboxy-terminal amino acids of VP1 are dispensable for the formation of virus-like particles, and further truncation at either end of VP1 leads to the loss of this property. Journal of NeuroVirology (2001) 7, 298-301.