Identification of the defects in the hemagglutinin gene of two temperature-sensitive mutants of A/WSN/33 influenza virus
Identifieur interne : 002372 ( Main/Exploration ); précédent : 002371; suivant : 002373Identification of the defects in the hemagglutinin gene of two temperature-sensitive mutants of A/WSN/33 influenza virus
Auteurs : Setsuko Nakajima [Japon] ; Donald J. Brown [États-Unis] ; Masahiro Ueda [Japon] ; Katsuhisa Nakajima [Japon] ; Akira Sugiura [Japon] ; Asit K. Pattnaik [États-Unis] ; Debi P. Nayak [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1986.
English descriptors
- Teeft :
- Academic press, Acid change, Acid changes, Acid sequencesof, Amino, Amino acid, Amino acid change, Amino acid changes, Amino acid residues, Amino acid substitutions, Amino acids, Cell surface, Compensatory changes, Critical site, Cytoplasmic domain, Gene segments, Globular, Globular head, Heat lability, Heat stability, Hemagglutinin, Hemagglutinin gene, Influenza, Influenza virus, Influenza virus hemagglutinin, Influenza viruses, Intracellular transport, Mdbk cells, Mutant, Mutation, Mutation sites, Nayak, Nonpermissive temperature, Nucleotide, Nucleotide changes, Nucleotide positions, Nucleotide sequences, Nucleotide substitutions, Personal communication, Phenotype, Polypeptide, Present study, Psheet structure, Revertant, Revertant clones, Revertant viruses, Revertants, Sequence analysis, Structural features, Substitution, Sugiura, Tertiary structure, Tyrosine residue, Ueda, Various viruses, Viral, Viral rnas, Virus, Wild type, Wild type virus.
Abstract
Abstract: Two temperature-sensitive mutants of WSN influenza virus, ts-61S and ts-134, possess defects in the hemagglutinin (HA) gene. These defects are characterized as a defective intracellular transport of the HA at the nonpermissive temperature and a marked thermolability. The nucleic acid sequences of the HA gene of these two viruses, as well as a series of revertant viruses, were determined. The deduced amino acid sequences demonstrate that the HA of ts-61S varied from the wild type protein by three amino acids while that of ts-134 differed by two residues. For both mutants, analysis of revertant viruses indicated that the phenotype of transport inhibition at the nonpermissive temperature and heat lability were associated with a single amino acid change in the globular portion of the molecule. In the case of ts-61S, the critical change in the HA was the replacement of a serine residue at position 110 with that of a proline. The mutational defect in the HA of ts-134 was due to the substitution of a tyrosine residue at position 159 with that of a histidine residue. Four of five revertants of ts-134 were suppressor revertants, of which some of the compensatory changes did not restore thermostability to the HA.
Url:
DOI: 10.1016/0042-6822(86)90454-X
Affiliations:
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These defects are characterized as a defective intracellular transport of the HA at the nonpermissive temperature and a marked thermolability. The nucleic acid sequences of the HA gene of these two viruses, as well as a series of revertant viruses, were determined. The deduced amino acid sequences demonstrate that the HA of ts-61S varied from the wild type protein by three amino acids while that of ts-134 differed by two residues. For both mutants, analysis of revertant viruses indicated that the phenotype of transport inhibition at the nonpermissive temperature and heat lability were associated with a single amino acid change in the globular portion of the molecule. In the case of ts-61S, the critical change in the HA was the replacement of a serine residue at position 110 with that of a proline. The mutational defect in the HA of ts-134 was due to the substitution of a tyrosine residue at position 159 with that of a histidine residue. Four of five revertants of ts-134 were suppressor revertants, of which some of the compensatory changes did not restore thermostability to the HA.</div></front></TEI><affiliations><list><country><li>Japon</li><li>États-Unis</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><country name="Japon"><region name="Région de Kantō"><name sortKey="Nakajima, Setsuko" sort="Nakajima, Setsuko" uniqKey="Nakajima S" first="Setsuko" last="Nakajima">Setsuko Nakajima</name></region><name sortKey="Nakajima, Katsuhisa" sort="Nakajima, Katsuhisa" uniqKey="Nakajima K" first="Katsuhisa" last="Nakajima">Katsuhisa Nakajima</name><name sortKey="Sugiura, Akira" sort="Sugiura, Akira" uniqKey="Sugiura A" first="Akira" last="Sugiura">Akira Sugiura</name><name sortKey="Ueda, Masahiro" sort="Ueda, Masahiro" uniqKey="Ueda M" first="Masahiro" last="Ueda">Masahiro Ueda</name></country><country name="États-Unis"><noRegion><name sortKey="Brown, Donald J" sort="Brown, Donald J" uniqKey="Brown D" first="Donald J." last="Brown">Donald J. Brown</name></noRegion><name sortKey="Nayak, Debi P" sort="Nayak, Debi P" uniqKey="Nayak D" first="Debi P." last="Nayak">Debi P. Nayak</name><name sortKey="Pattnaik, Asit K" sort="Pattnaik, Asit K" uniqKey="Pattnaik A" first="Asit K." last="Pattnaik">Asit K. Pattnaik</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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