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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-8-20
pubmed:abstractText
We produced a B cell hybridoma (TW2.3) from vaccinia virus-infected mice that secreted a monoclonal antibody (MAb) reactive with a 25-kDA early viral protein that was localized by laser scanning confocal microscopy to the nucleus and cytoplasmic viral factory regions of infected cells. By cell-free translation of mRNA selected by hybridization to a complete library of vaccinia virus DNA fragments, the immunoreactive polypeptide was mapped to open reading frame E3L. The RNA start site of an early promoter was located 26 nucleotides upstream of the first methionine codon of E3L. Evidence was obtained that translation initiation occurs in vivo and in vitro at both the first and second methionine codons to produce major and minor polypeptides of 25 and 19 kDa, respectively. Both polypeptides bound double-stranded RNA, confirming the recent report of H.-W. Chang, J. C. Watson, and B. L. Jacobs (Proc. Natl. Acad. Sci. USA 89, 4825-4829, 1992). Other vaccinia virus proteins were not required for the nuclear localization of the E3L protein, since MAb TW2.3 bound to the nuclei of uninfected cells that were transfected with the E3L gene under the control of the SV40 early promoter. We also demonstrated that the E3L protein can bind to nuclei of aldehyde fixed and detergent permeabilized uninfected cells. This binding was abrogated by treatment of the cells with RNase but not DNase. The nuclear and cytoplasmic locations of the double-stranded RNA binding protein are consistent with multiple functions in the vaccinia virus infectious cycle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
195
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
732-44
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed-meshheading:8337842-Amino Acid Sequence, pubmed-meshheading:8337842-Animals, pubmed-meshheading:8337842-Antibodies, Monoclonal, pubmed-meshheading:8337842-Base Sequence, pubmed-meshheading:8337842-Cell Line, pubmed-meshheading:8337842-Cell Nucleus, pubmed-meshheading:8337842-DNA, Viral, pubmed-meshheading:8337842-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8337842-Haplorhini, pubmed-meshheading:8337842-HeLa Cells, pubmed-meshheading:8337842-Humans, pubmed-meshheading:8337842-Mice, pubmed-meshheading:8337842-Molecular Sequence Data, pubmed-meshheading:8337842-Open Reading Frames, pubmed-meshheading:8337842-RNA, Double-Stranded, pubmed-meshheading:8337842-RNA-Binding Proteins, pubmed-meshheading:8337842-Transcription, Genetic, pubmed-meshheading:8337842-Vaccinia virus, pubmed-meshheading:8337842-Viral Proteins
pubmed:year
1993
pubmed:articleTitle
Nuclear localization of a double-stranded RNA-binding protein encoded by the vaccinia virus E3L gene.
pubmed:affiliation
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892.
pubmed:publicationType
Journal Article