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Amino acid replacements leading to temperature-sensitive defects of the NS1 protein of influenza A virus

Identifieur interne : 001D65 ( Main/Exploration ); précédent : 001D64; suivant : 001D66

Amino 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 :

RBID : ISTEX:F0A839116136728C5C6A0366BBCE0A7F805288C8

English descriptors

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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<term>Deletion</term>
<term>Extragenically</term>
<term>Federal republic</term>
<term>Fowl plague virus</term>
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<term>Hybridization probes</term>
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<term>Protein synthesis</term>
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<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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