MEI-LIN WANG2026-10-162026-10-162001-01-01Pure ID: 15426549Pure UUID: 281b4cf8-e352-49a9-b96b-cf949596ac5a10.1080/13550280152537139https://www.scopus.com/pages/publications/0034820497https://scholars.csmu.edu.tw/handle/123456789/32959Human 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 (ΔN12) and 19 (ΔN19) amino acids at the N-terminus and the last 16 (ΔC16), 17 (ΔC17), and 31 (ΔC31) amino acids at the C-terminus of VP1 were truncated and expressed in E. coli. The VP1 proteins of ΔN12 and ΔC16 were able to self-assemble into a virus-like particles similar to that of wild-type (WT) VP1. However, the mutant proteins of ΔN19, ΔC17, and ΔC31 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.4enjournal article