Source:http://linkedlifedata.com/resource/pubmed/id/16603216
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2006-5-22
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pubmed:abstractText |
Expression of full-length and N-terminal deletion mutants of the coat protein (CP) of tomato bushy stunt virus (TBSV) using the recombinant baculovirus system resulted in spontaneously assembled virus-like particles (VLPs). Deletion of the majority of the R-domain sequence of the CP, residues 1-52 (CP-NDelta52) and 1-62 (CP-NDelta62), produced capsids similar to wild-type VLPs. Interestingly, the CP-NDelta62 mutant that retains the last 3 residues of R-domain is capable of forming both the T = 1 and T = 3 particles. However, between the two types of VLPs, formation of the T = 1 capsids appears to be preferred. Another mutant, CP-NDelta72, in which R-domain (residues 1-65) was completely removed but contains most of the beta-annulus and extended arm (betaA) regions exclusively formed T = 1 particles. These results suggest that as few as 3 residues (63-65) of the R-domain, which includes 2 basic amino acids together with the arm (betaA) and beta-annulus regions, may be sufficient for the formation of T = 3 particles. However, anywhere between 4 to 13 residues of the R-domain may be required for proper positioning of betaA and beta-annulus structural elements of the C-type subunits to facilitate an error free assembly of T = 3 capsids.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
349
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
222-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16603216-Amino Acid Sequence,
pubmed-meshheading:16603216-Animals,
pubmed-meshheading:16603216-Capsid,
pubmed-meshheading:16603216-Capsid Proteins,
pubmed-meshheading:16603216-Cell Line,
pubmed-meshheading:16603216-Microscopy, Electron, Transmission,
pubmed-meshheading:16603216-Models, Molecular,
pubmed-meshheading:16603216-Molecular Sequence Data,
pubmed-meshheading:16603216-Polymorphism, Genetic,
pubmed-meshheading:16603216-Protein Structure, Tertiary,
pubmed-meshheading:16603216-RNA, Viral,
pubmed-meshheading:16603216-Sequence Alignment,
pubmed-meshheading:16603216-Sequence Deletion,
pubmed-meshheading:16603216-Spodoptera,
pubmed-meshheading:16603216-Tombusvirus,
pubmed-meshheading:16603216-Virosomes
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pubmed:year |
2006
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pubmed:articleTitle |
Characterization of polymorphism displayed by the coat protein mutants of tomato bushy stunt virus.
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pubmed:affiliation |
Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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