Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1999-3-10
|
pubmed:abstractText |
The full-length major capsid protein, VP1, of the human polyomavirus JC virus was cloned and expressed in Escherichia coli. VP1 protein expressed in E. coli self-assembled into capsid-like particles and caused haemagglutination of human O-type red blood cells. Caesium chloride density-gradient centrifugation analysis revealed that the capsid-like particles consisted of virion-like pseudovirion and empty capsid-like pseudocapsid populations. The morphology of pseudo-virion and pseudocapsid particles was observed under the electron microscope. The pseudovirions contained DNA and RNA molecules but the pseudocapsids did not contain any nucleic acid, as analysed by DNA extraction. DNA-binding activity of VP1 was also demonstrated by the South-Western probing method in vitro. Furthermore, pseudocapsids were able to deliver exogenous DNA into human foetal kidney epithelial cells. These results indicate that recombinant JC virus VP1 is able to self-assemble into capsid-like particles and to package DNA in the absence of the minor capsid proteins, VP2 and VP3. This prokaryotic assembly system may facilitate the investigation of maturation mechanism(s) of polyomaviruses. Furthermore, capsid-like particles of JC virus VP1 generated in E. coli potentially could be used as a human gene transfer vector.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Capsid Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/VP1 protein, polyomavirus
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0022-1317
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
80 ( Pt 1)
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
39-46
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:9934681-Capsid,
pubmed-meshheading:9934681-Capsid Proteins,
pubmed-meshheading:9934681-Cell Line, Transformed,
pubmed-meshheading:9934681-DNA,
pubmed-meshheading:9934681-DNA, Viral,
pubmed-meshheading:9934681-Escherichia coli,
pubmed-meshheading:9934681-Gene Expression,
pubmed-meshheading:9934681-Genetic Vectors,
pubmed-meshheading:9934681-Hemagglutination Tests,
pubmed-meshheading:9934681-Humans,
pubmed-meshheading:9934681-JC Virus,
pubmed-meshheading:9934681-Kidney,
pubmed-meshheading:9934681-RNA,
pubmed-meshheading:9934681-Recombinant Fusion Proteins,
pubmed-meshheading:9934681-Virion,
pubmed-meshheading:9934681-Virus Assembly
|
pubmed:year |
1999
|
pubmed:articleTitle |
The major capsid protein, VP1, of human JC virus expressed in Escherichia coli is able to self-assemble into a capsid-like particle and deliver exogenous DNA into human kidney cells.
|
pubmed:affiliation |
Department of Microbiology, Chung Shan Medical and Dental College, Taichung, Taiwan, Republic of China.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|