An 18-amino acid deletion in an influenza neuraminidase
Identifieur interne : 002456 ( Main/Exploration ); précédent : 002455; suivant : 002457An 18-amino acid deletion in an influenza neuraminidase
Auteurs : M. C. Els [États-Unis] ; G. M. Air [États-Unis] ; K. G. Murti [États-Unis] ; R. G. Webster [États-Unis] ; W. G. Laver [Australie]Source :
- Virology [ 0042-6822 ] ; 1985.
English descriptors
- Teeft :
- Academic press, Amino, Amino acid, Amino acid sequence, Amino acids, Antigenic, Antigenic sites, Biological activity, Blok, Blood cells, Cysteine residue, Deletion, Denaturing conditions, Electron density, Electron micrographs, Electron microscopy, Fetuin, Gene segments, Hydrophobic sequence, Influenza, Influenza neuraminidase, Influenza type, Influenza virus, Influenza virus neuraminidase, Influenza viruses, Large substrate, Laver, Monoclonal, Monoclonal antibodies, Neuraminidase, Neuraminidase activity, Neuraminidase gene, Neuraminidase genes, Nucleotide sequence coding, Original reassortant, Parental, Parental virus, Polypeptide chains, Rosette, Signal peptide, Stock virus, Stubby, Uncloned parent virus, Virus, Vrna segments.
Abstract
Abstract: The genes coding for the neuraminidase (NA) enzyme in antigenic variants of influenza virus X-7(F1) (which contains the NA of A/RI/5+/57) are shorter than other N2 neuraminidase genes. When the parent X-7(F1) virus was cloned at limiting dilution prior to selection of variants with monoclonal antibodies, a minor component with a shorter neuraminidase gene was cloned out, and this deletion was retained in all the variants. Sequence analysis has shown that there is a single deletion, 54 nucleotides long, which occurs in the coding region of the NA, The 18 deleted amino acids are from the stalk region of the protein, which is a thin structure containing the four polypeptide chains of the tetrameric enzyme which separates the enzymatically and antigenically active “head” from the hydrophobic sequence embedded in the viral membrane. The deletion can be seen as a shortened stalk when rosettes of detergent-released NA are examined by electron microscopy, which confirms that the NA stalk is a highly extended structure. Although the more abundant hemagglutinin (HA) would probably extend beyond the shortened NA molecule on the surface of the virus, the NA head is still accessible to all of the available monoclonal antibodies to the different antigenic sites on the molecule. Enzymatic activity toward a small substrate molecule, N-acetyl neuraminyl lactose, is the same for both the parental X-7(F1) virus and the strain having the deleted NA; however, the latter virus is slower to cleave a large substrate, fetuin, and elutes from red cells at a reduced rate.
Url:
DOI: 10.1016/0042-6822(85)90332-0
Affiliations:
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C." last="Els">M. C. Els</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Alabama</region></placeName><wicri:cityArea>Department of Microbiology, University of Alabama at Birmingham, Birmingham</wicri:cityArea></affiliation></author><author><name sortKey="Air, G M" sort="Air, G M" uniqKey="Air G" first="G. M." last="Air">G. M. Air</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Alabama</region></placeName><wicri:cityArea>Department of Microbiology, University of Alabama at Birmingham, Birmingham</wicri:cityArea></affiliation></author><author><name sortKey="Murti, K G" sort="Murti, K G" uniqKey="Murti K" first="K. G." last="Murti">K. G. 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Box 334, Canberra City, ACT 2601</wicri:regionArea><wicri:noRegion>ACT 2601</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="1985">1985</date><biblScope unit="volume">142</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="241">241</biblScope><biblScope unit="page" to="247">247</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>Academic press</term><term>Amino</term><term>Amino acid</term><term>Amino acid sequence</term><term>Amino acids</term><term>Antigenic</term><term>Antigenic sites</term><term>Biological activity</term><term>Blok</term><term>Blood cells</term><term>Cysteine residue</term><term>Deletion</term><term>Denaturing conditions</term><term>Electron density</term><term>Electron micrographs</term><term>Electron microscopy</term><term>Fetuin</term><term>Gene segments</term><term>Hydrophobic sequence</term><term>Influenza</term><term>Influenza neuraminidase</term><term>Influenza type</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Influenza viruses</term><term>Large substrate</term><term>Laver</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Neuraminidase</term><term>Neuraminidase activity</term><term>Neuraminidase gene</term><term>Neuraminidase genes</term><term>Nucleotide sequence coding</term><term>Original reassortant</term><term>Parental</term><term>Parental virus</term><term>Polypeptide chains</term><term>Rosette</term><term>Signal peptide</term><term>Stock virus</term><term>Stubby</term><term>Uncloned parent virus</term><term>Virus</term><term>Vrna segments</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The genes coding for the neuraminidase (NA) enzyme in antigenic variants of influenza virus X-7(F1) (which contains the NA of A/RI/5+/57) are shorter than other N2 neuraminidase genes. When the parent X-7(F1) virus was cloned at limiting dilution prior to selection of variants with monoclonal antibodies, a minor component with a shorter neuraminidase gene was cloned out, and this deletion was retained in all the variants. Sequence analysis has shown that there is a single deletion, 54 nucleotides long, which occurs in the coding region of the NA, The 18 deleted amino acids are from the stalk region of the protein, which is a thin structure containing the four polypeptide chains of the tetrameric enzyme which separates the enzymatically and antigenically active “head” from the hydrophobic sequence embedded in the viral membrane. The deletion can be seen as a shortened stalk when rosettes of detergent-released NA are examined by electron microscopy, which confirms that the NA stalk is a highly extended structure. Although the more abundant hemagglutinin (HA) would probably extend beyond the shortened NA molecule on the surface of the virus, the NA head is still accessible to all of the available monoclonal antibodies to the different antigenic sites on the molecule. Enzymatic activity toward a small substrate molecule, N-acetyl neuraminyl lactose, is the same for both the parental X-7(F1) virus and the strain having the deleted NA; however, the latter virus is slower to cleave a large substrate, fetuin, and elutes from red cells at a reduced rate.</div></front></TEI><affiliations><list><country><li>Australie</li><li>États-Unis</li></country><region><li>Alabama</li><li>Tennessee</li></region></list><tree><country name="États-Unis"><region name="Alabama"><name sortKey="Els, M C" sort="Els, M C" uniqKey="Els M" first="M. C." last="Els">M. C. Els</name></region><name sortKey="Air, G M" sort="Air, G M" uniqKey="Air G" first="G. M." last="Air">G. M. Air</name><name sortKey="Murti, K G" sort="Murti, K G" uniqKey="Murti K" first="K. G." last="Murti">K. G. Murti</name><name sortKey="Webster, R G" sort="Webster, R G" uniqKey="Webster R" first="R. G." last="Webster">R. G. Webster</name></country><country name="Australie"><noRegion><name sortKey="Laver, W G" sort="Laver, W G" uniqKey="Laver W" first="W. G." last="Laver">W. G. Laver</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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