The Transcription/Replication Activity of the Polymerase of Influenza A Viruses Is Not Correlated with the Level of Proteolysis Induced by the PA Subunit
Identifieur interne : 000263 ( France/Analysis ); précédent : 000262; suivant : 000264The Transcription/Replication Activity of the Polymerase of Influenza A Viruses Is Not Correlated with the Level of Proteolysis Induced by the PA Subunit
Auteurs : Nadia Naffakh [France] ; Pascale Massin [France] ; Sylvie Van Der Werf [France]Source :
- Virology [ 0042-6822 ] ; 2001.
English descriptors
- KwdEn :
- Teeft :
- Amino, Amino acid, Amino acid substitutions, Amino acids, Assay, Avian, Avian origin, Cdna, Cell extracts, Cells cotransfected, Cells transfected, Coexpressed proteins, Control phmg plasmid, Encoding, Experiment representative, Galactosidase, Galactosidase levels, Galactosidase proteolysis, Galactosidase proteolyzed, Influenza, Influenza replication, Influenza virus, Influenza viruses, Krug, Molecular dynamics, Mrna, Mutant, Naffakh, Optical scanner, Ortin, Perales, Phmg, Phmg plasmid, Plasmid, Polyclonal serum, Polymerase, Polymerase activity, Posttransfection, Present study, Proteolysis, Proteolytic, Proteolytic activity, Proteolyzed, Replication, Replication activity, Reporter plasmid, Rna, Substitution, Subunit, Transcription, Transfected, Transfected cells, Virol, Western blot analysis.
Abstract
Abstract: The PA subunit of the influenza virus polymerase has been shown to induce degradation of coexpressed proteins, but its role in the replication activity of the polymerase is not fully understood. Here, PA proteins derived from several influenza A viruses were examined at 37 and 33°C for both the level of proteolysis they induced and the efficiency with which they ensured transcription/replication of a viral-like RNA within a polymerase complex reconstituted in vivo from cloned cDNAs. Two mutants of A/Victoria/3/75 PA showed a decreased ability to induce proteolysis as compared to the wild-type PA, but still appeared to be as active as the wild-type protein with respect to the polymerase activity. Furthermore, we observed that the ability of PR8-PA to induce proteolysis was severely impaired at 33°C as compared to 37°C, while the efficiency with which the PR8-derived polymerase complex ensured transcription/replication of the viral-like RNA was similar at both temperatures. Taken together, our observations suggest that the transcription/replication activity of the polymerase of influenza A viruses is not correlated with the level of proteolysis induced by the PA subunit.
Url:
DOI: 10.1006/viro.2001.0956
Affiliations:
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to="252">252</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>PA protein</term><term>influenza virus</term><term>proteolysis</term><term>replication</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Amino</term><term>Amino acid</term><term>Amino acid substitutions</term><term>Amino acids</term><term>Assay</term><term>Avian</term><term>Avian origin</term><term>Cdna</term><term>Cell extracts</term><term>Cells cotransfected</term><term>Cells transfected</term><term>Coexpressed proteins</term><term>Control phmg plasmid</term><term>Encoding</term><term>Experiment representative</term><term>Galactosidase</term><term>Galactosidase levels</term><term>Galactosidase proteolysis</term><term>Galactosidase proteolyzed</term><term>Influenza</term><term>Influenza replication</term><term>Influenza virus</term><term>Influenza viruses</term><term>Krug</term><term>Molecular dynamics</term><term>Mrna</term><term>Mutant</term><term>Naffakh</term><term>Optical scanner</term><term>Ortin</term><term>Perales</term><term>Phmg</term><term>Phmg plasmid</term><term>Plasmid</term><term>Polyclonal serum</term><term>Polymerase</term><term>Polymerase activity</term><term>Posttransfection</term><term>Present study</term><term>Proteolysis</term><term>Proteolytic</term><term>Proteolytic activity</term><term>Proteolyzed</term><term>Replication</term><term>Replication activity</term><term>Reporter plasmid</term><term>Rna</term><term>Substitution</term><term>Subunit</term><term>Transcription</term><term>Transfected</term><term>Transfected cells</term><term>Virol</term><term>Western blot analysis</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The PA subunit of the influenza virus polymerase has been shown to induce degradation of coexpressed proteins, but its role in the replication activity of the polymerase is not fully understood. Here, PA proteins derived from several influenza A viruses were examined at 37 and 33°C for both the level of proteolysis they induced and the efficiency with which they ensured transcription/replication of a viral-like RNA within a polymerase complex reconstituted in vivo from cloned cDNAs. Two mutants of A/Victoria/3/75 PA showed a decreased ability to induce proteolysis as compared to the wild-type PA, but still appeared to be as active as the wild-type protein with respect to the polymerase activity. Furthermore, we observed that the ability of PR8-PA to induce proteolysis was severely impaired at 33°C as compared to 37°C, while the efficiency with which the PR8-derived polymerase complex ensured transcription/replication of the viral-like RNA was similar at both temperatures. Taken together, our observations suggest that the transcription/replication activity of the polymerase of influenza A viruses is not correlated with the level of proteolysis induced by the PA subunit.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Paris</li></settlement></list><tree><country name="France"><region name="Île-de-France"><name sortKey="Naffakh, Nadia" sort="Naffakh, Nadia" uniqKey="Naffakh N" first="Nadia" last="Naffakh">Nadia Naffakh</name></region><name sortKey="Massin, Pascale" sort="Massin, Pascale" uniqKey="Massin P" first="Pascale" last="Massin">Pascale Massin</name><name sortKey="Van Der Werf, Sylvie" sort="Van Der Werf, Sylvie" uniqKey="Van Der Werf S" first="Sylvie" last="Van Der Werf">Sylvie Van Der Werf</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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