Source:http://linkedlifedata.com/resource/pubmed/id/15571717
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2004-12-1
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| pubmed:abstractText |
The strongly conserved amino acid sequences of the P8 outer capsid proteins of Rice dwarf virus (RDV) and Rice gall dwarf virus (RGDV) and the distribution of electrostatic potential on the proteins at the interfaces between structural proteins suggested the possibility that P8-trimers of RGDV might bind to the 3-fold symmetrical axes of RDV core particles, with vertical interaction between heterologous P3 and P8 proteins and lateral binding of homologous P8 proteins, thereby allowing formation of the double-layered capsids that are characteristic of viruses that belong to the family Reoviridae. We proved this hypothesis using chimeric virus-like particles composed of the P3 core capsid protein of RDV and the P8 outer capsid protein of RGDV, which were co-expressed in a baculovirus expression system. This is the first report on the molecular biological proof of the mechanism of the assembly of the double-layered capsids with disparate icosahedral lattices.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0022-2836
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
14
|
| pubmed:volume |
345
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
229-37
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:15571717-Amino Acid Sequence,
pubmed-meshheading:15571717-Baculoviridae,
pubmed-meshheading:15571717-Blotting, Western,
pubmed-meshheading:15571717-Capsid,
pubmed-meshheading:15571717-Capsid Proteins,
pubmed-meshheading:15571717-Crystallography, X-Ray,
pubmed-meshheading:15571717-Dimerization,
pubmed-meshheading:15571717-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15571717-Magnesium Chloride,
pubmed-meshheading:15571717-Microscopy, Electron,
pubmed-meshheading:15571717-Models, Molecular,
pubmed-meshheading:15571717-Molecular Sequence Data,
pubmed-meshheading:15571717-Protein Conformation,
pubmed-meshheading:15571717-Protein Structure, Tertiary,
pubmed-meshheading:15571717-Proteins,
pubmed-meshheading:15571717-Reoviridae,
pubmed-meshheading:15571717-Sequence Homology, Amino Acid,
pubmed-meshheading:15571717-Software,
pubmed-meshheading:15571717-Static Electricity
|
| pubmed:year |
2005
|
| pubmed:articleTitle |
Transcapsidation and the conserved interactions of two major structural proteins of a pair of phytoreoviruses confirm the mechanism of assembly of the outer capsid layer.
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| pubmed:affiliation |
Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|