Acylation of virol. spike glycoproteins: A feature of enveloped RNA viruses
Identifieur interne : 001688 ( Main/Exploration ); précédent : 001687; suivant : 001689Acylation of virol. spike glycoproteins: A feature of enveloped RNA viruses
Auteurs : Michael F. G. Schmidt [Allemagne]Source :
- Virology [ 0042-6822 ] ; 1982.
English descriptors
- Teeft :
- Acid, Acylation, Bilayer, Biol, Bromide, Chick, Chick embryo cells, Chorioallantoic membrane, Coomassie, Coronavirus, Culture fluid, Cultured cells, Cyanogen, Different host cells, Embryo, Envelope glycoproteins, Fatty, Fatty acid, Fatty acid binding, Fatty acids, Fluorogram, Glycoprotein, Hemagglutinin, Huang, Influenza, Influenza hemagglutinin, Influenza virus, Influenza virus hemagglutinin, Influenza viruses, Insect cells, Klenk, Lipid, Loading buffer, Membrane proteins, Newcastle disease virus, Palmitic acid, Peptide, Polypeptide, Protein hydrolysate, Right panel, Room temperature, Rott, Schlesinger, Schmidt, Semliki, Semliki forest virus, Sindbis, Sindbis virus, Spike, Spike glycoproteins, Stomatitis, Thyroid cells, Trypsin, Vesicular, Vesicular stomatitis virus, Viral, Viral glycoprotein, Viral glycoproteins, Viral lipid bilayer, Viral spike glycoproteins, Virology, Virus, Virus particles, West germany.
Abstract
Abstract: The covalent attachment of fatty acids to the glycoproteins of orthomyxo-, paramyxo, alpha-, and coronavirus was studied. All enveloped viruses analyzed afford covalently bound fatty acid in at least one species of their spike glycoproteins. No internal components of the viruses studied including the hydrophobic M proteins of myxo- and rhabdoviruses contained fatty acid. Analysis of myxovirus particles devoid of the exposed portions of their spikes revealed that fatty acids are linked to the hydrophobic tail fragment of the glycoprotein which is associated with the viral lipid bilayer. With influenza virus hemagglutinin the fatty acid attachment site could be located at the cyanogen bromide peptide of the small subunit (HA2) which contains the membrane-embedded region of the polypeptide. The binding of fatty acids to viral glycoproteins occurs in a wide range of host cells including mammalian, avian, and insect cells.
Url:
DOI: 10.1016/0042-6822(82)90424-X
Affiliations:
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G." last="Schmidt">Michael F. G. Schmidt</name><affiliation wicri:level="1"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut fur Virologie, Justus-Liebig-Universitkt Giessen, 6300 Giessen</wicri:regionArea><wicri:noRegion>6300 Giessen</wicri:noRegion><wicri:noRegion>6300 Giessen</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="1982">1982</date><biblScope unit="volume">116</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="327">327</biblScope><biblScope unit="page" to="338">338</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>Acid</term><term>Acylation</term><term>Bilayer</term><term>Biol</term><term>Bromide</term><term>Chick</term><term>Chick embryo cells</term><term>Chorioallantoic membrane</term><term>Coomassie</term><term>Coronavirus</term><term>Culture fluid</term><term>Cultured cells</term><term>Cyanogen</term><term>Different host cells</term><term>Embryo</term><term>Envelope glycoproteins</term><term>Fatty</term><term>Fatty acid</term><term>Fatty acid binding</term><term>Fatty acids</term><term>Fluorogram</term><term>Glycoprotein</term><term>Hemagglutinin</term><term>Huang</term><term>Influenza</term><term>Influenza hemagglutinin</term><term>Influenza virus</term><term>Influenza virus hemagglutinin</term><term>Influenza viruses</term><term>Insect cells</term><term>Klenk</term><term>Lipid</term><term>Loading buffer</term><term>Membrane proteins</term><term>Newcastle disease virus</term><term>Palmitic acid</term><term>Peptide</term><term>Polypeptide</term><term>Protein hydrolysate</term><term>Right panel</term><term>Room temperature</term><term>Rott</term><term>Schlesinger</term><term>Schmidt</term><term>Semliki</term><term>Semliki forest virus</term><term>Sindbis</term><term>Sindbis virus</term><term>Spike</term><term>Spike glycoproteins</term><term>Stomatitis</term><term>Thyroid cells</term><term>Trypsin</term><term>Vesicular</term><term>Vesicular stomatitis virus</term><term>Viral</term><term>Viral glycoprotein</term><term>Viral glycoproteins</term><term>Viral lipid bilayer</term><term>Viral spike glycoproteins</term><term>Virology</term><term>Virus</term><term>Virus particles</term><term>West germany</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The covalent attachment of fatty acids to the glycoproteins of orthomyxo-, paramyxo, alpha-, and coronavirus was studied. All enveloped viruses analyzed afford covalently bound fatty acid in at least one species of their spike glycoproteins. No internal components of the viruses studied including the hydrophobic M proteins of myxo- and rhabdoviruses contained fatty acid. Analysis of myxovirus particles devoid of the exposed portions of their spikes revealed that fatty acids are linked to the hydrophobic tail fragment of the glycoprotein which is associated with the viral lipid bilayer. With influenza virus hemagglutinin the fatty acid attachment site could be located at the cyanogen bromide peptide of the small subunit (HA2) which contains the membrane-embedded region of the polypeptide. The binding of fatty acids to viral glycoproteins occurs in a wide range of host cells including mammalian, avian, and insect cells.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country></list><tree><country name="Allemagne"><noRegion><name sortKey="Schmidt, Michael F G" sort="Schmidt, Michael F G" uniqKey="Schmidt M" first="Michael F. G." last="Schmidt">Michael F. G. Schmidt</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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