Linked Life Data

11517406

Source:http://linkedlifedata.com/resource/pubmed/id/11517406

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-8-22
pubmed:abstractText
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 (Delta N12) and 19 (Delta N19) amino acids at the N-terminus and the last 16 (Delta C16), 17 (Delta C17), and 31 (Delta C31) amino acids at the C-terminus of VP1 were truncated and expressed in E. coli. The VP1 proteins of Delta N12 and Delta C16 were able to self-assemble into a virus-like particle similar to that of wild-type (WT) VP1. However, the mutant proteins of Delta N19, Delta C17, and Delta 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1355-0284
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
298-301
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Analysis of minimal sequences on JC virus VP1 required for capsid assembly.
pubmed:affiliation
Institute of Molecular Biology, National Chung Cheng University, Chia-Yi, Taiwan, Republic of China.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't