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Analysis of minimal sequences on jc virus vp1 required for capsid assembly.
| Content Provider | CiteSeerX |
|---|---|
| Author | Ou, Wei-Chih Chen, Ling-Hua Wang, Meilin Hseu, Tzong-Hsiung Chang, Deching |
| 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 �rst 12 (D N12) and 19 (D N19) amino acids at the N-terminus and the last 16 (D C16), 17 (D C17), and 31 (D C31) amino acids at the C-terminus of VP1 were truncated and expressed in E. coli. The VP1 proteins of D N12 and D C16 were able to self-assemble into a virus-like particle similar to that of wild-type (WT) VP1. However, the mutant proteins of D N19, D C17, and D 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. |
| File Format | |
| Access Restriction | Open |
| Subject Keyword | Minimal Sequence Capsid Assembly Jc Virus Vp1 Amino Acid Virus-like Particle Electron Microscopy Vp1 Protein Mutant Protein Jcv Vp1 Polypeptide Carboxy-terminal Amino Acid Viral Capsid Sucrose Gradient Centrifugation Vp1 Molecule Capsomere Structure Pentameric Capsomere Structure Human Jc Virus |
| Content Type | Text |
