H2N2V1, Main, Exploration, bibRecord, 002024

Heterogeneous forms of polymerase proteins exist in influenza A virus-infected cells

Identifieur interne : 002024 ( Main/Exploration ); précédent : 002023; suivant : 002025

Heterogeneous forms of polymerase proteins exist in influenza A virus-infected cells

Auteurs : Ramesh K. Akkina [États-Unis] ; James C. Richardson [États-Unis] ; Marcela C. Aguilera [États-Unis] ; Yang Chi-Ming [États-Unis]

Source :

Virus Research [ 0168-1702 ] ; 1991.

RBID : ISTEX:C280B8B2BF588A4DC9F7E36CFB5306A26BDDA2A1

English descriptors

Teeft :
- Additional forms, Additional proteins, Akkina, Antiserum, Cell lysates, Immunoprecipitation, Influenza, Influenza polymerase, Influenza virus, Influenza viruses, Krug, Limited proteolysis peptide mapping, Lysates, Lysis buffer, Mdbk cells, Monospecific, Monospecific antisera, Mrna, Normal counterparts, Normal rabbit serum, Pblb, Peptide, Plenum press, Polymerase, Polymerase antisera, Polymerase proteins, Polypeptide, Protein, Pulse chase experiments, Radiolabeled, Radiolabeled virus, Replication, Rnps, Subunit, Viral, Viral replication, Virus, Vrna, Vrna synthesis.

Abstract

Abstract: In influenza virus-infected cells a virus coded polymerase that consists of three polypeptide subunits, namely PB1, PB2 and PA, mediates both transcription and replication. Radioimmunoprecipitation with monospecific antisera to each of the polymerase proteins revealed additional forms of PB1 and PA proteins in infected cells. PA antiserum detected two additional proteins of 62k and 60k and PB1 antiserum recognized two additional proteins of 85k and 70k. Further investigation was carried out on the 62k PA and 85k PB1 related proteins. Limited proteolysis peptide mapping showed that these proteins are subsets of their normal counterparts. These new forms of polymerase proteins are designated as “b” forms (PAb and PB1b) to distinguish them from the previously recognized forms designated as “a” forms (PAa and PB1a). Both PAb and PBIb proteins were found in cells infected with all the influenza type A viruses tested indicating that they are evolutionarily conserved. Pulse chase experiments showed that the “b” forms are not derived from “a” forms. This suggested that “b” forms are translated independently. The “b” forms were not detected in purified virus but were found to be associated with intracellular RNP templates, suggesting a role for these proteins in intracellular virus replication events.

Url:

https://api.istex.fr/ark:/67375/6H6-DC0KP179-Z/fulltext.pdf

DOI: 10.1016/0168-1702(91)90091-9

Affiliations:

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Le document en format XML

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<term>Immunoprecipitation</term>
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<term>Influenza polymerase</term>
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<term>Influenza viruses</term>
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<term>Limited proteolysis peptide mapping</term>
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<term>Polymerase antisera</term>
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<front><div type="abstract" xml:lang="en">Abstract: In influenza virus-infected cells a virus coded polymerase that consists of three polypeptide subunits, namely PB1, PB2 and PA, mediates both transcription and replication. Radioimmunoprecipitation with monospecific antisera to each of the polymerase proteins revealed additional forms of PB1 and PA proteins in infected cells. PA antiserum detected two additional proteins of 62k and 60k and PB1 antiserum recognized two additional proteins of 85k and 70k. Further investigation was carried out on the 62k PA and 85k PB1 related proteins. Limited proteolysis peptide mapping showed that these proteins are subsets of their normal counterparts. These new forms of polymerase proteins are designated as “b” forms (PAb and PB1b) to distinguish them from the previously recognized forms designated as “a” forms (PAa and PB1a). Both PAb and PBIb proteins were found in cells infected with all the influenza type A viruses tested indicating that they are evolutionarily conserved. Pulse chase experiments showed that the “b” forms are not derived from “a” forms. This suggested that “b” forms are translated independently. The “b” forms were not detected in purified virus but were found to be associated with intracellular RNP templates, suggesting a role for these proteins in intracellular virus replication events.</div>
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Heterogeneous forms of polymerase proteins exist in influenza A virus-infected cells

Heterogeneous forms of polymerase proteins exist in influenza A virus-infected cells

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Abstract

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