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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2007-9-3
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pubmed:abstractText |
Tobacco mosaic virus (TMV) coat protein (CP) in absence of RNA self-assembles into several different structures depending on pH and ionic strength. Transgenic plants that produce self-assembling CP are resistant to TMV infection, a phenomenon referred to as coat-protein-mediated resistance (CP-MR). The mutant CP Thr42Trp (CP(T42W)) produces enhanced CP-MR compared to wild-type CP. To establish the relationship between the formation of 20S CP aggregates and CP-MR, virus-like particles (VLPs) produced by TMV variants that yield high levels of CP-MR were characterized. We demonstrate that non-helical structures are found in VLPs formed in vivo by CP(T42W) but not by wild-type CP and suggest that the mutation shifts the intracellular equilibrium of aggregates from low to higher proportions of non-helical 20S aggregates. A similar shift in equilibrium of aggregates was observed with CP(D77R), another mutant that confers high level of CP-MR. The mutant CP(D50R) confers a level of CP-MR similar to wild-type CP and aggregates in a manner similar to wild-type CP. We conclude that increased CP-MR is correlated with a shift in intracellular equilibrium of CP aggregates, including aggregates that interfere with virus replication.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-10212932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-10212933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-10212946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-10582108,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-10704307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-11891326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-14745003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-16078876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-16528051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-16773235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-2082726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-2131099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-2294644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-2330673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-2448951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-2769760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-3207689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-3369086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-6879170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-726261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-734434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-7579612,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-7831832,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-888358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-9311885,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-9449360,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17493658-9449361
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0042-6822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
366
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
98-106
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17493658-Amino Acid Substitution,
pubmed-meshheading:17493658-Capsid Proteins,
pubmed-meshheading:17493658-Cloning, Molecular,
pubmed-meshheading:17493658-Cryoelectron Microscopy,
pubmed-meshheading:17493658-DNA, Viral,
pubmed-meshheading:17493658-Drug Resistance, Viral,
pubmed-meshheading:17493658-Genetic Variation,
pubmed-meshheading:17493658-Microscopy, Electron,
pubmed-meshheading:17493658-Models, Molecular,
pubmed-meshheading:17493658-Protein Conformation,
pubmed-meshheading:17493658-Tobacco Mosaic Virus,
pubmed-meshheading:17493658-Transcription, Genetic
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pubmed:year |
2007
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pubmed:articleTitle |
Aggregation of TMV CP plays a role in CP functions and in coat-protein-mediated resistance.
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pubmed:affiliation |
Donald Danforth Plant Science Center, 975 North Warson Road, St. Louis, MO 63132, USA. sasurmendi@cnia.inta.gov.ar
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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