Source:http://linkedlifedata.com/resource/pubmed/id/12771434
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 6
|
pubmed:dateCreated |
2003-5-28
|
pubmed:abstractText |
The results of a previous study demonstrated that avian reovirus is highly resistant to the antiviral effects of interferon and suggested that the double-stranded RNA (dsRNA)-binding sigmaA protein might play an important role in that resistance. To gather more evidence on the interferon-inhibitory activity of sigmaA protein, its gene was cloned into the prokaryotic maltose-binding protein (MBP) gene fusion vector pMalC and into the recombinant vaccinia virus WRS2. The two recombinant sigmaA proteins displayed a dsRNA-binding affinity similar to that of sigmaA protein synthesized in avian reovirus-infected cells. Interestingly, MBP-sigmaA, but not MBP, was able to relieve the translation-inhibitory activity of dsRNA in reticulocyte lysates by blocking the activation of endogenous dsRNA-dependent enzymes. In addition, transient expression of sigmaA protein in HeLa cells rescued gene expression of a vaccinia virus mutant lacking the E3L gene, and insertion of the sigmaA-encoding gene into vaccinia virus conferred protection for the virus against interferon in chicken cells. Further studies demonstrated that expression of recombinant sigmaA in mammalian cells interfered with dsRNA-dependent protein kinase (PKR) function. From these results we conclude that sigmaA is capable of reversing the interferon-induced antiviral state by down-regulating PKR activity in a manner similar to other virus-encoded dsRNA-binding proteins.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Interferons,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Core Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/eIF-2 Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/sigmaA protein, avian reovirus
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0022-1317
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
84
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1629-39
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:12771434-Animals,
pubmed-meshheading:12771434-Antibodies, Viral,
pubmed-meshheading:12771434-Chick Embryo,
pubmed-meshheading:12771434-Gene Expression,
pubmed-meshheading:12771434-HeLa Cells,
pubmed-meshheading:12771434-Humans,
pubmed-meshheading:12771434-Interferons,
pubmed-meshheading:12771434-Orthoreovirus, Avian,
pubmed-meshheading:12771434-Protein Biosynthesis,
pubmed-meshheading:12771434-RNA, Double-Stranded,
pubmed-meshheading:12771434-RNA-Binding Proteins,
pubmed-meshheading:12771434-Recombinant Fusion Proteins,
pubmed-meshheading:12771434-Reticulocytes,
pubmed-meshheading:12771434-Vaccinia virus,
pubmed-meshheading:12771434-Viral Core Proteins,
pubmed-meshheading:12771434-Virus Replication,
pubmed-meshheading:12771434-eIF-2 Kinase
|
pubmed:year |
2003
|
pubmed:articleTitle |
Evidence that avian reovirus sigmaA protein is an inhibitor of the double-stranded RNA-dependent protein kinase.
|
pubmed:affiliation |
Departamento de Bioquímica y Biología Molecular, Facultad de Farmacia, Universidad de Santiago de Compostela, Spain.
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|