Source:http://linkedlifedata.com/resource/pubmed/id/10499447
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1999-10-20
|
pubmed:databankReference | |
pubmed:abstractText |
An antigenic 30 K virion protein of Heliothis armigera entomopoxvirus (HaEPV) has been identified as a homologue of the chordopoxvirus (ChPV) VP8 major virion core protein. Like its homologue in vaccinia virus, the mature HaEPV 30 K protein is derived by post-translational cleavage of a precursor at a conserved AGA motif. The HaEPV 30 K protein is the first EPV structural virion protein to be described, and elucidation of its characteristics provides evidence for the assumption that morphological similarities observed between virions of the sub-families Entomopoxvirinae and Chordopoxvirinae by microscopy reflect corresponding similarities at a molecular level. Sequencing of the HaEPV genome adjacent to the 30K locus identified an ORF encoding a homologue of the regulatory sub-unit of the ChPV poly(A) polymerase enzyme; the conceptual product of this ORF showed 25-31% aa sequence identity to those of various ChPVs. The presence of this gene in the HaEPV genome supports the hypothesis that there is a substantial correspondence in basic metabolic processes of members of the two poxvirus sub-families, despite their utilization of divergent host groups. In contrast, the relative positions of the 30 K and poly(A) polymerase loci in the HaEPV genome provide further evidence of substantial genomic re-arrangement subsequent to divergence of these viral taxa.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Core Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Structural Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/vaccinia virus protein VP8
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0920-8569
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
19
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
23-31
|
pubmed:dateRevised |
2004-8-18
|
pubmed:meshHeading |
pubmed-meshheading:10499447-Amino Acid Sequence,
pubmed-meshheading:10499447-Animals,
pubmed-meshheading:10499447-DNA-Binding Proteins,
pubmed-meshheading:10499447-Entomopoxvirinae,
pubmed-meshheading:10499447-Lepidoptera,
pubmed-meshheading:10499447-Molecular Sequence Data,
pubmed-meshheading:10499447-Phylogeny,
pubmed-meshheading:10499447-Sequence Homology, Amino Acid,
pubmed-meshheading:10499447-Vaccinia virus,
pubmed-meshheading:10499447-Viral Core Proteins,
pubmed-meshheading:10499447-Viral Proteins,
pubmed-meshheading:10499447-Viral Structural Proteins
|
pubmed:year |
1999
|
pubmed:articleTitle |
Virions of Heliothis armigera entomopoxvirus contain a homologue of the vaccinia VP8 major core protein.
|
pubmed:affiliation |
Department of Plant Pathology, University of California, Davis 95616, USA. davidd@ento.csiro.au
|
pubmed:publicationType |
Journal Article
|