Nonsense mutations affecting the lengths of the NS1 nonstructural proteins of influenza A virus isolates
Identifieur interne : 002585 ( Main/Exploration ); précédent : 002584; suivant : 002586Nonsense mutations affecting the lengths of the NS1 nonstructural proteins of influenza A virus isolates
Auteurs : J. D. Parvin [États-Unis] ; J. F. Young [États-Unis] ; P. Palese [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1983.
English descriptors
- Teeft :
- Amino, Amino acids, Carboxy, Carboxy termini, Carboxy terminus, Cell proteins, Codon, High degree, Hlnl, Influenza, Influenza viruses, Large deletions, Mutation, Nonsense mutations, Nucleic acids, Opal, Palese, Polypeptide, Proc, Protein length, Reading frame, Rna, Short communications, Urea, Viral, Viral polypeptides.
Abstract
Abstract: The proteins from cells infected with influenza A virus field isolates were labeled with [35S]methionine and analyzed by SDS-polyacrylamide gel electrophoresis. By screening more than 100 field isolates, it was found that the NS1 proteins had the greatest mobility differences, far exceeding those observed among other corresponding viral polypeptides. Partial sequence determination of RNA segment eight from 12 viruses revealed the existence of nonsense mutations at six different positions in their NS1 coding regions. The termination codons consisted of opal, ochre, and amber mutations. The sizes predicted from these sequences of 202, 217, 219, 220, 230, and 237 amino acids were in agreement with the observed mobilities of the viral polypeptides on SDS-polyacrylamide gels. The observation of large deletions in the carboxy termini of the NS1 proteins of field virus isolates would suggest that a high degree of variation can be tolerated in this polypeptide without affecting its functional capability.
Url:
DOI: 10.1016/0042-6822(83)90280-5
Affiliations:
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D." last="Parvin">J. D. Parvin</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology, Mount Sinai School of Medicine of CUNY, Fifth Avenue and 100th Street, New York, New York 10029</wicri:regionArea><wicri:noRegion>New York 10029</wicri:noRegion></affiliation></author><author><name sortKey="Young, J F" sort="Young, J F" uniqKey="Young J" first="J. F." last="Young">J. F. Young</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology, Mount Sinai School of Medicine of CUNY, Fifth Avenue and 100th Street, New York, New York 10029</wicri:regionArea><wicri:noRegion>New York 10029</wicri:noRegion></affiliation></author><author><name sortKey="Palese, P" sort="Palese, P" uniqKey="Palese P" first="P." last="Palese">P. 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By screening more than 100 field isolates, it was found that the NS1 proteins had the greatest mobility differences, far exceeding those observed among other corresponding viral polypeptides. Partial sequence determination of RNA segment eight from 12 viruses revealed the existence of nonsense mutations at six different positions in their NS1 coding regions. The termination codons consisted of opal, ochre, and amber mutations. The sizes predicted from these sequences of 202, 217, 219, 220, 230, and 237 amino acids were in agreement with the observed mobilities of the viral polypeptides on SDS-polyacrylamide gels. The observation of large deletions in the carboxy termini of the NS1 proteins of field virus isolates would suggest that a high degree of variation can be tolerated in this polypeptide without affecting its functional capability.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Parvin, J D" sort="Parvin, J D" uniqKey="Parvin J" first="J. D." last="Parvin">J. D. Parvin</name></noRegion><name sortKey="Palese, P" sort="Palese, P" uniqKey="Palese P" first="P." last="Palese">P. Palese</name><name sortKey="Young, J F" sort="Young, J F" uniqKey="Young J" first="J. F." last="Young">J. F. Young</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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