Linked Life Data

6545074

Source:http://linkedlifedata.com/resource/pubmed/id/6545074

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-1-7
pubmed:abstractText
Sindbis virus containing [35S]methionine-labeled structural proteins was allowed to be taken up by primary chick embryo fibroblasts, and the fate of the core protein was studied. The experiments show that core protein of incoming viral particles is transferred to the large subunit of cellular ribosomes during the initial steps of virus infection. A similar transfer occurs in vitro if cores isolated from SIN virus particles are incubated in the postmitochondrial cytoplasmic fraction of cell lysates. In vivo transfer also occurs if the protein synthesis-inhibiting drugs puromycin or cycloheximide are present during virus uptake, whereas in the presence of chloroquine, which inhibits the release of viral cores into the cytoplasm, which is necessary for productive infection, a transfer of core protein to ribosomes cannot be observed. The latter result indicates that the transfer probably is part of the reactions leading to the release of viral genomic RNA into the cellular cytoplasm during the early stages of productive infection, and presumably does not reflect side reactions. It has been shown earlier that newly synthesized alphavirus core protein binds to the large ribosomal subunit prior to the assembly of viral core particles in infected cells [I. Ulmanen, H. Sonderlund, and L. Kääriäinen (1979) Virology 99, 265-276]. These data lead to the suggestion that the disassembly and assembly of alphavirus cores might be regulated by a process which could be called receptor-mediated core disassembly, in which acceptors exist for the protein components of viral nucleoproteins in uninfected cells which early in infection bind these proteins and thereby lead to disassembly of these complexes, and which later on have to be saturated with newly synthesized protein before efficient assembly of nucleoproteins can occur, and that the large ribosomal subunit functions as such a receptor during alphavirus replication.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
134
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
435-42
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Identification of a transfer of viral core protein to cellular ribosomes during the early stages of alphavirus infection.
pubmed:publicationType
Journal Article