Acylation of virol. spike glycoproteins: A feature of enveloped RNA viruses
Identifieur interne : 000789 ( Istex/Corpus ); précédent : 000788; suivant : 000790Acylation of virol. spike glycoproteins: A feature of enveloped RNA viruses
Auteurs : Michael F. G. SchmidtSource :
- 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
Links to Exploration step
ISTEX:5C9CB2299973B9C1B9AD27699F9233170274C864Le document en format XML
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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. 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Schmidt</name><affiliations><json:string>Institut fur Virologie, Justus-Liebig-Universitkt Giessen, 6300 Giessen, West Germany</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-KVN2ZZ1N-6</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><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.</abstract><qualityIndicators><score>8.083</score><pdfWordCount>4391</pdfWordCount><pdfCharCount>30386</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>12</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>141</abstractWordCount><abstractCharCount>941</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Acylation of virol. spike glycoproteins: A feature of enveloped RNA viruses</title><pmid><json:string>6278712</json:string></pmid><pii><json:string>0042-6822(82)90424-X</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. 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USA</title><language><json:string>unknown</json:string></language><volume>71</volume><pages><first>4011</first><last>4014</last></pages></serie><host><title>Virology</title><language><json:string>unknown</json:string></language><publicationDate>1982</publicationDate><issn><json:string>0042-6822</json:string></issn><pii><json:string>S0042-6822(00)X0656-3</json:string></pii><volume>116</volume><issue>1</issue><pages><first>327</first><last>338</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1982</json:string><json:string>6000</json:string></date><geogName><json:string>Semliki</json:string></geogName><orgName><json:string>-US It</json:string><json:string>Deutsche Forschungsgemeinschaft</json:string></orgName><orgName_funder><json:string>Deutsche Forschungsgemeinschaft</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>La Sota</json:string><json:string>Coronaviruses</json:string><json:string>E. G. Strauss</json:string><json:string>R. T. C. Huang</json:string><json:string>Spike Glycoproteins</json:string><json:string>Gisela Wengler</json:string><json:string>C. Reitz</json:string><json:string>W. Garten</json:string><json:string>Michaela Orlich</json:string><json:string>Eva Kroll</json:string><json:string>R. Rott</json:string><json:string>K. Holmes</json:string><json:string>El El</json:string></persName><placeName><json:string>Singapore</json:string><json:string>Germany</json:string><json:string>Heidelberg</json:string><json:string>Mannheim</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Brand and Skehel, 1972</json:string><json:string>Sturman et al., 1980</json:string><json:string>Schmidt et al., 1979</json:string><json:string>Lazarowitz and Choppin, 1975</json:string><json:string>Klenk et al., 1975</json:string><json:string>Huang et al. (1979)</json:string><json:string>Huang et al. (1981)</json:string><json:string>Skehel and Waterfield, 1975</json:string><json:string>Niemann and Klenk, 1981</json:string><json:string>Petri and Wagner, 1981</json:string><json:string>Schulze, 1972</json:string><json:string>Bonner and Laskey (1974)</json:string><json:string>Cursiefen and Becht, 1975</json:string><json:string>Rice and Strauss, 1981</json:string><json:string>Verhoeyen et al., 1980</json:string><json:string>Min-Jou et al., 1980</json:string><json:string>Sturman et al. (1980)</json:string><json:string>Storz et al, 1981b</json:string><json:string>Zilberstein et al. (1980)</json:string><json:string>Storz et al. (1981a)</json:string><json:string>Schmidt and Schlesinger, 1980b</json:string><json:string>Schmidt et al.</json:string><json:string>Kalkkinen et al., 1980</json:string><json:string>Porter et al., 1979</json:string><json:string>Storz et al., 1981a</json:string><json:string>Klenk et al., 1972</json:string><json:string>Schmidt and Schlesinger, 1980a</json:string><json:string>Schlesinger et al., 1980</json:string><json:string>Nagai et al., 1976</json:string><json:string>Lowry et al. (1951)</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-KVN2ZZ1N-6</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - virology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - virology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - Virology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string><json:string>4 - microbiologie</json:string></inist></categories><publicationDate>1982</publicationDate><copyrightDate>1982</copyrightDate><doi><json:string>10.1016/0042-6822(82)90424-X</json:string></doi><id>5C9CB2299973B9C1B9AD27699F9233170274C864</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KVN2ZZ1N-6/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KVN2ZZ1N-6/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-KVN2ZZ1N-6/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Acylation of virol. spike glycoproteins: A feature of enveloped RNA viruses</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1982</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Acylation of virol. spike glycoproteins: A feature of enveloped RNA viruses</title><author xml:id="author-0000"><persName><forename type="first">Michael F.G.</forename><surname>Schmidt</surname></persName><note type="biography">To whom reprint requests should be addressed.</note><affiliation>To whom reprint requests should be addressed.</affiliation><affiliation>Institut fur Virologie, Justus-Liebig-Universitkt Giessen, 6300 Giessen, West Germany</affiliation></author><idno type="istex">5C9CB2299973B9C1B9AD27699F9233170274C864</idno><idno type="ark">ark:/67375/6H6-KVN2ZZ1N-6</idno><idno type="DOI">10.1016/0042-6822(82)90424-X</idno><idno type="PII">0042-6822(82)90424-X</idno></analytic><monogr><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="pISSN">0042-6822</idno><idno type="PII">S0042-6822(00)X0656-3</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="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></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1982</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>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.</p></abstract></profileDesc><revisionDesc><change when="1982">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KVN2ZZ1N-6/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>YVIRO</jid><aid>8290424X</aid><ce:pii>0042-6822(82)90424-X</ce:pii><ce:doi>10.1016/0042-6822(82)90424-X</ce:doi><ce:copyright type="unknown" year="1982"></ce:copyright></item-info><head><ce:title>Acylation of virol. spike glycoproteins: A feature of enveloped RNA viruses</ce:title><ce:author-group><ce:author><ce:given-name>Michael F.G.</ce:given-name><ce:surname>Schmidt</ce:surname><ce:cross-ref refid="COR1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:affiliation><ce:textfn>Institut fur Virologie, Justus-Liebig-Universitkt Giessen, 6300 Giessen, West Germany</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>1</ce:label><ce:text>To whom reprint requests should be addressed.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="26" month="6" year="1981"></ce:date-received><ce:date-accepted day="9" month="9" year="1981"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>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 (HA<ce:inf>2</ce:inf>) 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.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Acylation of virol. spike glycoproteins: A feature of enveloped RNA viruses</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Acylation of virol. spike glycoproteins: A feature of enveloped RNA viruses</title></titleInfo><name type="personal"><namePart type="given">Michael F.G.</namePart><namePart type="family">Schmidt</namePart><affiliation>Institut fur Virologie, Justus-Liebig-Universitkt Giessen, 6300 Giessen, West Germany</affiliation><description>To whom reprint requests should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1982</dateIssued><copyrightDate encoding="w3cdtf">1982</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract 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.</abstract><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><titleInfo type="abbreviated"><title>YVIRO</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1982</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0656-3</identifier><part><date>1982</date><detail type="volume"><number>116</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>389</end></extent><extent unit="pages"><start>327</start><end>338</end></extent></part></relatedItem><identifier type="istex">5C9CB2299973B9C1B9AD27699F9233170274C864</identifier><identifier type="ark">ark:/67375/6H6-KVN2ZZ1N-6</identifier><identifier type="DOI">10.1016/0042-6822(82)90424-X</identifier><identifier type="PII">0042-6822(82)90424-X</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-KVN2ZZ1N-6/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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