Amino acid replacements leading to temperature-sensitive defects of the NS1 protein of influenza A virus
Identifieur interne : 001D65 ( Main/Exploration ); précédent : 001D64; suivant : 001D66Amino acid replacements leading to temperature-sensitive defects of the NS1 protein of influenza A virus
Auteurs : S. Ludwig [Allemagne] ; U. Vogel [Allemagne] ; Ch. Scholtissek [Allemagne]Source :
- Archives of Virology [ 0304-8608 ] ; 1995-05-01.
English descriptors
- Teeft :
- Acid replacements, Allelic genes, Almond, Amino, Amino acid replacement, Deletion, Extragenically, Federal republic, Fowl plague virus, Giessen, Hatada, Hybridization probes, Influenza, Influenza virus, Influenza viruses, Koennecke, Mrna, Mutant, Mutation, Nonpermissive, Nonpermissive temperature, Nonstructural, Northern blot analysis, Nucleocytoplasmic transport, Other genes, Phenotype, Post infection, Posttranscriptional, Posttranscriptional block, Primary chicken embryo cells, Protein genes, Protein synthesis, Reassortants, Scholtissek, Single base substitution, Viral, Virol, Virology, Vrna, Vrna synthesis.
Abstract
Summary: The nonstructural (NS) genes of two influenza virus temperature-sensitive (ts) reassortants have been sequenced and compared with the corresponding wild type sequences. Ts 412 has a single base substitution (G100 → A) leading to an amino acid replacement (Arg 25 → Lys) in the NS1 protein. Ts 451 also has a single base substitution (U273 → C) leading to an amino acid replacement (Ser 83 → Pro) in the NS1 protein. In ts 412 infected cells at the nonpermissive temperature very little M1 and HA mRNA and proteins are synthesized, suggesting that NS1 is involved in a transcriptional regulation process. The ts mutation in ts 451 could be extragenically suppressed by replacement of the PB1 and/or PA protein genes of the mutant by the allelic genes of PR8. Both observations suggest that NS1 cooperates with the polymerase complex.
Url:
DOI: 10.1007/BF01314970
Affiliations:
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Le document en format XML
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<term>Extragenically</term>
<term>Federal republic</term>
<term>Fowl plague virus</term>
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<term>Hybridization probes</term>
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<front><div type="abstract" xml:lang="en">Summary: The nonstructural (NS) genes of two influenza virus temperature-sensitive (ts) reassortants have been sequenced and compared with the corresponding wild type sequences. Ts 412 has a single base substitution (G100 → A) leading to an amino acid replacement (Arg 25 → Lys) in the NS1 protein. Ts 451 also has a single base substitution (U273 → C) leading to an amino acid replacement (Ser 83 → Pro) in the NS1 protein. In ts 412 infected cells at the nonpermissive temperature very little M1 and HA mRNA and proteins are synthesized, suggesting that NS1 is involved in a transcriptional regulation process. The ts mutation in ts 451 could be extragenically suppressed by replacement of the PB1 and/or PA protein genes of the mutant by the allelic genes of PR8. Both observations suggest that NS1 cooperates with the polymerase complex.</div>
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