Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1997-6-9
pubmed:abstractText
Previous investigations into recombination in cowpea chlorotic mottle bromovirus (CCMV) resulted in the recovery of an unusual recombinant virus, 3-57, which caused a symptomless infection of cowpeas but formed no detectable virions. Sequence analysis of cDNA clones derived from 3-57 determined that mutations near the 5' terminus of the capsid protein gene introduced an early translational termination codon. Further mutations introduced a new in-frame start codon that allowed translation of the 3' two-thirds of the capsid protein gene. Based on the mutations observed in 3-57, wild-type CCMV clones were modified to determine if the carboxyl two-thirds of the capsid protein functions independently of the complete protein in long-distance movement. Analysis of these mutants determined that while virion formation is not required for systemic infection, the carboxy-terminal two-thirds of the capsid protein is both required and sufficient for systemic movement of viral RNA. This indicates that the CCMV capsid protein is multifunctional, with a distinct long-distance movement function in addition to its role in virion formation.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-1472715, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-1690559, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-1727594, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-1733093, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-1905801, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-2014641, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-2053275, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-2053278, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-2308940, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-2795712, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-3418781, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-4975324, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-7743132, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-7769722, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-7772801, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-7780307, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-7856075, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-8128222, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-8517020, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151887-911786
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4862-5
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The carboxy-terminal two-thirds of the cowpea chlorotic mottle bromovirus capsid protein is incapable of virion formation yet supports systemic movement.
pubmed:affiliation
Genetics Program, Michigan State University, East Lansing 48824, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't