Palmitoylation of the influenza a virus M2 protein
Identifieur interne : 002081 ( Main/Exploration ); précédent : 002080; suivant : 002082Palmitoylation of the influenza a virus M2 protein
Auteurs : R. J. Sugrue [Royaume-Uni] ; R. B. Belshe [États-Unis] ; A. J. Hay [Royaume-Uni]Source :
- Virology [ 0042-6822 ] ; 1990.
English descriptors
- Teeft :
- Academic press, Amantadine, Amino acid sequences, Cell surface, Cysteine, Equine, Equine viruses, Fatty acid acylation, Human transferrin receptor, Hydroxylamine, Hydroxylamine treatment, Immune precipitates, Influenza, Influenza virus, Influenza viruses, Membrane fusion, Molecular basis, Monolayers, Nonreducing conditions, Nucleotide sequence, Other virus strains, Palmitate, Palmitate addition, Palmitate association, Palmitate moiety, Room temperature, Schmidt, Semliki forest virus, Sequence analysis, Several equine viruses, Sodium chloride, Sodium phosphate, Soyabean trypsin inhibitor, Sugrue, Thioester linkage, Virus, Virus strains.
Abstract
Abstract: The M2 proteins of a variety of influenza A viruses of different subtypes were shown to possess associated palmitate. Susceptibility to removal by reduction or treatment with hydroxylamine is consistent with attachment via a thioester linkage to cysteine. The absence of the acyl group from the M2 proteins of several equine viruses of the H3N8 subtype correlates with the replacement of cysteine 50 with phenylalanine and points to this as the site of palmitate attachement.
Url:
DOI: 10.1016/0042-6822(90)90272-S
Affiliations:
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J." last="Sugrue">R. J. Sugrue</name><affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Virology Division, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA</wicri:regionArea><wicri:noRegion>London NW7 1AA</wicri:noRegion></affiliation></author><author><name sortKey="Belshe, R B" sort="Belshe, R B" uniqKey="Belshe R" first="R. B." last="Belshe">R. B. Belshe</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Missouri (État)</region></placeName><wicri:cityArea>Division of Infectious Diseases, Saint Louis University School of Medicine, 1402 South Grand Boulevard, Saint Louis</wicri:cityArea></affiliation></author><author><name sortKey="Hay, A J" sort="Hay, A J" uniqKey="Hay A" first="A. J." last="Hay">A. J. Hay</name><affiliation></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Virology Division, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA</wicri:regionArea><wicri:noRegion>London NW7 1AA</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="1990">1990</date><biblScope unit="volume">179</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="51">51</biblScope><biblScope unit="page" to="56">56</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>Amantadine</term><term>Amino acid sequences</term><term>Cell surface</term><term>Cysteine</term><term>Equine</term><term>Equine viruses</term><term>Fatty acid acylation</term><term>Human transferrin receptor</term><term>Hydroxylamine</term><term>Hydroxylamine treatment</term><term>Immune precipitates</term><term>Influenza</term><term>Influenza virus</term><term>Influenza viruses</term><term>Membrane fusion</term><term>Molecular basis</term><term>Monolayers</term><term>Nonreducing conditions</term><term>Nucleotide sequence</term><term>Other virus strains</term><term>Palmitate</term><term>Palmitate addition</term><term>Palmitate association</term><term>Palmitate moiety</term><term>Room temperature</term><term>Schmidt</term><term>Semliki forest virus</term><term>Sequence analysis</term><term>Several equine viruses</term><term>Sodium chloride</term><term>Sodium phosphate</term><term>Soyabean trypsin inhibitor</term><term>Sugrue</term><term>Thioester linkage</term><term>Virus</term><term>Virus strains</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The M2 proteins of a variety of influenza A viruses of different subtypes were shown to possess associated palmitate. Susceptibility to removal by reduction or treatment with hydroxylamine is consistent with attachment via a thioester linkage to cysteine. The absence of the acyl group from the M2 proteins of several equine viruses of the H3N8 subtype correlates with the replacement of cysteine 50 with phenylalanine and points to this as the site of palmitate attachement.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li><li>États-Unis</li></country><region><li>Missouri (État)</li></region></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Sugrue, R J" sort="Sugrue, R J" uniqKey="Sugrue R" first="R. J." last="Sugrue">R. J. Sugrue</name></noRegion><name sortKey="Hay, A J" sort="Hay, A J" uniqKey="Hay A" first="A. J." last="Hay">A. J. Hay</name></country><country name="États-Unis"><region name="Missouri (État)"><name sortKey="Belshe, R B" sort="Belshe, R B" uniqKey="Belshe R" first="R. B." last="Belshe">R. B. 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