Identification of defects in the neuraminidase gene of four temperature-sensitive mutants of A/WSN/33 influenza virus
Identifieur interne : 002373 ( Main/Exploration ); précédent : 002372; suivant : 002374Identification of defects in the neuraminidase gene of four temperature-sensitive mutants of A/WSN/33 influenza virus
Auteurs : Timothy J. Bos [États-Unis] ; Debi P. Nayak [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1986.
English descriptors
- Teeft :
- Amino, Amino acid changes, Cell surface, Enzymatic activity, Enzyme activity, Glycoprotein, Head domain, Influenza, Influenza neuraminidase, Influenza virus, Influenza virus neuraminidase, Localized change, Mdbk, Mdbk cells, Monoclonal, Monoclonal antibody, Mutant, Mutation, Mutation sites, Nayak, Neuraminidase, Neuraminidase gene, Nonessential, Nonpermissive, Nonpermissive temperature, Nucleotide, Nucleotide changes, Palese, Permissive temperature, Phenotype, Point mutations, Revertant, Revertants, Sialic, Sialic acid binding site, Sugiura, Tsll, Ueda, Unique mutations, Varghese, Viral, Viral protein, Virology, Virus, Virus particles, Wild type, Wild type phenotype, Wild type virus.
Abstract
Abstract: Four influenza (A/WSN/33) mutants, temperature sensitive (ts) for neuraminidase (NA) (Sugiura et al., 1972, 1975) were analyzed. All four ts mutants were found to be defective at the nonpermissive temperature (39.5°) both in enzymatic activity and in transport to the cell surface. Upon shift down to the permissive temperature (33°), enzymatic activity and transport to the cell surface were both restored suggesting that the mutational defect is reversible. Comparative sequence analysis of the NA gene from ts mutants, their revertants and wild type WSN viruses revealed that in each case single point mutations causing amino acid substitutions were associated with the ts defect. The positions of each point mutation when mapped in the three-dimensional structure of NA varied. However, all four amino acid substitutions were located in β-sheet strands of the head region. Several other amino acid changes not essential for the ts phenotype were found in each mutant NA. The nonessential changes were localized either in the stalk region or in the loop structures of the head, but none in the β-sheet strands. Because both enzymatic activity and transport of NA were affected in all four mutants, we propose that the mutational phenotype is caused by a change in overall conformation rather than a localized change in the sialic acid binding site.
Url:
DOI: 10.1016/0042-6822(86)90432-0
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 000774
- to stream Istex, to step Curation: 000774
- to stream Istex, to step Checkpoint: 001065
- to stream Main, to step Merge: 002489
- to stream Main, to step Curation: 002373
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Identification of defects in the neuraminidase gene of four temperature-sensitive mutants of A/WSN/33 influenza virus</title>
<author><name sortKey="Bos, Timothy J" sort="Bos, Timothy J" uniqKey="Bos T" first="Timothy J." last="Bos">Timothy J. Bos</name>
</author>
<author><name sortKey="Nayak, Debi P" sort="Nayak, Debi P" uniqKey="Nayak D" first="Debi P." last="Nayak">Debi P. Nayak</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">ISTEX</idno>
<idno type="RBID">ISTEX:A18C161DD1760D7C1D7A3275C5B1D7EB0A8335E0</idno>
<date when="1986" year="1986">1986</date>
<idno type="doi">10.1016/0042-6822(86)90432-0</idno>
<idno type="url">https://api.istex.fr/ark:/67375/6H6-Q1NHRG21-B/fulltext.pdf</idno>
<idno type="wicri:Area/Istex/Corpus">000774</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000774</idno>
<idno type="wicri:Area/Istex/Curation">000774</idno>
<idno type="wicri:Area/Istex/Checkpoint">001065</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001065</idno>
<idno type="wicri:doubleKey">0042-6822:1986:Bos T:identification:of:defects</idno>
<idno type="wicri:Area/Main/Merge">002489</idno>
<idno type="wicri:Area/Main/Curation">002373</idno>
<idno type="wicri:Area/Main/Exploration">002373</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title level="a">Identification of defects in the neuraminidase gene of four temperature-sensitive mutants of A/WSN/33 influenza virus</title>
<author><name sortKey="Bos, Timothy J" sort="Bos, Timothy J" uniqKey="Bos T" first="Timothy J." last="Bos">Timothy J. Bos</name>
<affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Jonsson Comprehensive Cancer Center, and Department of Microbiology and Immunology, UCLA School of Medicine, Los Angeles, California 90024</wicri:regionArea>
<wicri:noRegion>California 90024</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Nayak, Debi P" sort="Nayak, Debi P" uniqKey="Nayak D" first="Debi P." last="Nayak">Debi P. Nayak</name>
<affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Jonsson Comprehensive Cancer Center, and Department of Microbiology and Immunology, UCLA School of Medicine, Los Angeles, California 90024</wicri:regionArea>
<wicri:noRegion>California 90024</wicri:noRegion>
</affiliation>
</author>
</analytic>
<monogr></monogr>
<series><title level="j">Virology</title>
<title level="j" type="abbrev">YVIRO</title>
<idno type="ISSN">0042-6822</idno>
<imprint><publisher>ELSEVIER</publisher>
<date type="published" when="1986">1986</date>
<biblScope unit="volume">154</biblScope>
<biblScope unit="issue">1</biblScope>
<biblScope unit="page" from="85">85</biblScope>
<biblScope unit="page" to="96">96</biblScope>
</imprint>
<idno type="ISSN">0042-6822</idno>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><idno type="ISSN">0042-6822</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Amino</term>
<term>Amino acid changes</term>
<term>Cell surface</term>
<term>Enzymatic activity</term>
<term>Enzyme activity</term>
<term>Glycoprotein</term>
<term>Head domain</term>
<term>Influenza</term>
<term>Influenza neuraminidase</term>
<term>Influenza virus</term>
<term>Influenza virus neuraminidase</term>
<term>Localized change</term>
<term>Mdbk</term>
<term>Mdbk cells</term>
<term>Monoclonal</term>
<term>Monoclonal antibody</term>
<term>Mutant</term>
<term>Mutation</term>
<term>Mutation sites</term>
<term>Nayak</term>
<term>Neuraminidase</term>
<term>Neuraminidase gene</term>
<term>Nonessential</term>
<term>Nonpermissive</term>
<term>Nonpermissive temperature</term>
<term>Nucleotide</term>
<term>Nucleotide changes</term>
<term>Palese</term>
<term>Permissive temperature</term>
<term>Phenotype</term>
<term>Point mutations</term>
<term>Revertant</term>
<term>Revertants</term>
<term>Sialic</term>
<term>Sialic acid binding site</term>
<term>Sugiura</term>
<term>Tsll</term>
<term>Ueda</term>
<term>Unique mutations</term>
<term>Varghese</term>
<term>Viral</term>
<term>Viral protein</term>
<term>Virology</term>
<term>Virus</term>
<term>Virus particles</term>
<term>Wild type</term>
<term>Wild type phenotype</term>
<term>Wild type virus</term>
</keywords>
</textClass>
<langUsage><language ident="en">en</language>
</langUsage>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Abstract: Four influenza (A/WSN/33) mutants, temperature sensitive (ts) for neuraminidase (NA) (Sugiura et al., 1972, 1975) were analyzed. All four ts mutants were found to be defective at the nonpermissive temperature (39.5°) both in enzymatic activity and in transport to the cell surface. Upon shift down to the permissive temperature (33°), enzymatic activity and transport to the cell surface were both restored suggesting that the mutational defect is reversible. Comparative sequence analysis of the NA gene from ts mutants, their revertants and wild type WSN viruses revealed that in each case single point mutations causing amino acid substitutions were associated with the ts defect. The positions of each point mutation when mapped in the three-dimensional structure of NA varied. However, all four amino acid substitutions were located in β-sheet strands of the head region. Several other amino acid changes not essential for the ts phenotype were found in each mutant NA. The nonessential changes were localized either in the stalk region or in the loop structures of the head, but none in the β-sheet strands. Because both enzymatic activity and transport of NA were affected in all four mutants, we propose that the mutational phenotype is caused by a change in overall conformation rather than a localized change in the sialic acid binding site.</div>
</front>
</TEI>
<affiliations><list><country><li>États-Unis</li>
</country>
</list>
<tree><country name="États-Unis"><noRegion><name sortKey="Bos, Timothy J" sort="Bos, Timothy J" uniqKey="Bos T" first="Timothy J." last="Bos">Timothy J. Bos</name>
</noRegion>
<name sortKey="Nayak, Debi P" sort="Nayak, Debi P" uniqKey="Nayak D" first="Debi P." last="Nayak">Debi P. Nayak</name>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002373 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002373 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= H2N2V1 |flux= Main |étape= Exploration |type= RBID |clé= ISTEX:A18C161DD1760D7C1D7A3275C5B1D7EB0A8335E0 |texte= Identification of defects in the neuraminidase gene of four temperature-sensitive mutants of A/WSN/33 influenza virus }}
This area was generated with Dilib version V0.6.33. |