Processing of virus-specific glycoproteins of varicella zoster virus
Identifieur interne : 000675 ( Istex/Corpus ); précédent : 000674; suivant : 000676Processing of virus-specific glycoproteins of varicella zoster virus
Auteurs : Junko Namazue ; Harvey Campo-Vera ; Kenji Kitamura ; Toshiomi Okuno ; Koichi YamanishiSource :
- Virology [ 0042-6822 ] ; 1985.
English descriptors
- Teeft :
- Cell cultures, Cell extracts, Complex type, Endo, Glycoprotein, Glycosylation, Golgi apparatus, Herpes, Herpes simplex virus, Herpes simplex virus glycoproteins, Immunoprecipitates, Molecular weight, Monensin, Monoclonal, Monoclonal antibodies, Okuno, Oligosaccharide, Polypeptide, Precursor, Precursor proteins, Product protein, Product proteins, Sample buffer, Simplex, Tunicamycin, Vesicular stomatitis virus, Virol.
Abstract
Abstract: Monoclonal antibodies to varicella zoster virus (VZV) glycoproteins were used to study the processing of three glycoproteins with molecular weights of 83K–94K (gp 2), 64K (gp 3), and 55K (gp 5). Immunoprecipitation experiments performed with VZV-infected cells, pulse labeled with [3H]glucosamine in the presence of tunicamycin, suggest that O-linked oligosaccharide is present on the glycoprotein of gp 2. Use of the enzyme endo-β-N-acetylglucosaminidase H revealed that the fully processed form of gp 3 had high-mannose type and that of gp 5 had only complex type of N-linked oligosaccharides. Experiments with monensin suggest that the precursor form (116K) of gp 3 is cleaved during the processing from Golgi apparatus to cell surface membrane. The extension of O-linked oligosaccharide chain and the complex type of N-linked oligosaccharide chains also occurs during this processing.
Url:
DOI: 10.1016/0042-6822(85)90112-6
Links to Exploration step
ISTEX:A3F5A9DCDEFB811AFFF020BB19A144FBCEE7E0CFLe document en format XML
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Microbial Diseases, Osaka University, Suita, Osaka 565, Japan</mods:affiliation></affiliation></author><author><name sortKey="Kitamura, Kenji" sort="Kitamura, Kenji" uniqKey="Kitamura K" first="Kenji" last="Kitamura">Kenji Kitamura</name><affiliation><mods:affiliation>Department of Pediatrics, School of Medicine, Mie University, Tsu, Mie 514, Japan</mods:affiliation></affiliation></author><author><name sortKey="Okuno, Toshiomi" sort="Okuno, Toshiomi" uniqKey="Okuno T" first="Toshiomi" last="Okuno">Toshiomi Okuno</name><affiliation><mods:affiliation>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan</mods:affiliation></affiliation></author><author><name sortKey="Yamanishi, Koichi" sort="Yamanishi, Koichi" uniqKey="Yamanishi K" first="Koichi" last="Yamanishi">Koichi Yamanishi</name><affiliation><mods:affiliation>To whom reprint requests should be addressed.</mods:affiliation></affiliation><affiliation><mods:affiliation>Department 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simplex virus glycoproteins</term><term>Immunoprecipitates</term><term>Molecular weight</term><term>Monensin</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Okuno</term><term>Oligosaccharide</term><term>Polypeptide</term><term>Precursor</term><term>Precursor proteins</term><term>Product protein</term><term>Product proteins</term><term>Sample buffer</term><term>Simplex</term><term>Tunicamycin</term><term>Vesicular stomatitis virus</term><term>Virol</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Monoclonal antibodies to varicella zoster virus (VZV) glycoproteins were used to study the processing of three glycoproteins with molecular weights of 83K–94K (gp 2), 64K (gp 3), and 55K (gp 5). Immunoprecipitation experiments performed with VZV-infected cells, pulse labeled with [3H]glucosamine in the presence of tunicamycin, suggest that O-linked oligosaccharide is present on the glycoprotein of gp 2. Use of the enzyme endo-β-N-acetylglucosaminidase H revealed that the fully processed form of gp 3 had high-mannose type and that of gp 5 had only complex type of N-linked oligosaccharides. Experiments with monensin suggest that the precursor form (116K) of gp 3 is cleaved during the processing from Golgi apparatus to cell surface membrane. The extension of O-linked oligosaccharide chain and the complex type of N-linked oligosaccharide chains also occurs during this processing.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>polypeptide</json:string><json:string>glycoprotein</json:string><json:string>oligosaccharide</json:string><json:string>monoclonal</json:string><json:string>monoclonal antibodies</json:string><json:string>tunicamycin</json:string><json:string>monensin</json:string><json:string>cell extracts</json:string><json:string>endo</json:string><json:string>immunoprecipitates</json:string><json:string>okuno</json:string><json:string>herpes</json:string><json:string>glycosylation</json:string><json:string>virol</json:string><json:string>precursor</json:string><json:string>complex type</json:string><json:string>simplex</json:string><json:string>golgi apparatus</json:string><json:string>herpes simplex virus glycoproteins</json:string><json:string>molecular weight</json:string><json:string>vesicular stomatitis virus</json:string><json:string>sample buffer</json:string><json:string>precursor proteins</json:string><json:string>product proteins</json:string><json:string>product protein</json:string><json:string>cell cultures</json:string><json:string>herpes simplex virus</json:string></teeft></keywords><author><json:item><name>Junko Namazue</name><affiliations><json:string>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan</json:string></affiliations></json:item><json:item><name>Harvey Campo-Vera</name><affiliations><json:string>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan</json:string></affiliations></json:item><json:item><name>Kenji Kitamura</name><affiliations><json:string>Department of Pediatrics, School of Medicine, Mie University, Tsu, Mie 514, Japan</json:string></affiliations></json:item><json:item><name>Toshiomi Okuno</name><affiliations><json:string>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan</json:string></affiliations></json:item><json:item><name>Koichi Yamanishi</name><affiliations><json:string>To whom reprint requests should be addressed.</json:string><json:string>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-MJ1NNF78-X</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Monoclonal antibodies to varicella zoster virus (VZV) glycoproteins were used to study the processing of three glycoproteins with molecular weights of 83K–94K (gp 2), 64K (gp 3), and 55K (gp 5). Immunoprecipitation experiments performed with VZV-infected cells, pulse labeled with [3H]glucosamine in the presence of tunicamycin, suggest that O-linked oligosaccharide is present on the glycoprotein of gp 2. Use of the enzyme endo-β-N-acetylglucosaminidase H revealed that the fully processed form of gp 3 had high-mannose type and that of gp 5 had only complex type of N-linked oligosaccharides. Experiments with monensin suggest that the precursor form (116K) of gp 3 is cleaved during the processing from Golgi apparatus to cell surface membrane. The extension of O-linked oligosaccharide chain and the complex type of N-linked oligosaccharide chains also occurs during this processing.</abstract><qualityIndicators><score>6.734</score><pdfWordCount>3150</pdfWordCount><pdfCharCount>22898</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>8</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>132</abstractWordCount><abstractCharCount>898</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Processing of virus-specific glycoproteins of varicella zoster virus</title><pmid><json:string>2998004</json:string></pmid><pii><json:string>0042-6822(85)90112-6</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. 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Immunoprecipitation experiments performed with VZV-infected cells, pulse labeled with [3H]glucosamine in the presence of tunicamycin, suggest that O-linked oligosaccharide is present on the glycoprotein of gp 2. Use of the enzyme endo-β-N-acetylglucosaminidase H revealed that the fully processed form of gp 3 had high-mannose type and that of gp 5 had only complex type of N-linked oligosaccharides. Experiments with monensin suggest that the precursor form (116K) of gp 3 is cleaved during the processing from Golgi apparatus to cell surface membrane. The extension of O-linked oligosaccharide chain and the complex type of N-linked oligosaccharide chains also occurs during this processing.</p></abstract></profileDesc><revisionDesc><change when="1985">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-MJ1NNF78-X/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>85901126</aid><ce:pii>0042-6822(85)90112-6</ce:pii><ce:doi>10.1016/0042-6822(85)90112-6</ce:doi><ce:copyright type="unknown" year="1985"></ce:copyright></item-info><head><ce:title>Processing of virus-specific glycoproteins of varicella zoster virus</ce:title><ce:author-group><ce:author><ce:given-name>Junko</ce:given-name><ce:surname>Namazue</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Harvey</ce:given-name><ce:surname>Campo-Vera</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Kenji</ce:given-name><ce:surname>Kitamura</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Toshiomi</ce:given-name><ce:surname>Okuno</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Koichi</ce:given-name><ce:surname>Yamanishi</ce:surname><ce:cross-ref refid="COR1"><ce:sup>1</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Pediatrics, School of Medicine, Mie University, Tsu, Mie 514, Japan</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="1984"></ce:date-received><ce:date-accepted day="16" month="1" year="1985"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Monoclonal antibodies to varicella zoster virus (VZV) glycoproteins were used to study the processing of three glycoproteins with molecular weights of 83K–94K (gp 2), 64K (gp 3), and 55K (gp 5). Immunoprecipitation experiments performed with VZV-infected cells, pulse labeled with [<ce:sup loc="pre">3</ce:sup>H]glucosamine in the presence of tunicamycin, suggest that O-linked oligosaccharide is present on the glycoprotein of gp 2. Use of the enzyme endo-β-<ce:italic>N</ce:italic>-acetylglucosaminidase H revealed that the fully processed form of gp 3 had high-mannose type and that of gp 5 had only complex type of N-linked oligosaccharides. Experiments with monensin suggest that the precursor form (116K) of gp 3 is cleaved during the processing from Golgi apparatus to cell surface membrane. The extension of O-linked oligosaccharide chain and the complex type of N-linked oligosaccharide chains also occurs during this processing.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Processing of virus-specific glycoproteins of varicella zoster virus</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Processing of virus-specific glycoproteins of varicella zoster virus</title></titleInfo><name type="personal"><namePart type="given">Junko</namePart><namePart type="family">Namazue</namePart><affiliation>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Harvey</namePart><namePart type="family">Campo-Vera</namePart><affiliation>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Kenji</namePart><namePart type="family">Kitamura</namePart><affiliation>Department of Pediatrics, School of Medicine, Mie University, Tsu, Mie 514, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Toshiomi</namePart><namePart type="family">Okuno</namePart><affiliation>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Koichi</namePart><namePart type="family">Yamanishi</namePart><affiliation>To whom reprint requests should be addressed.</affiliation><affiliation>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565, Japan</affiliation><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">1985</dateIssued><copyrightDate encoding="w3cdtf">1985</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Monoclonal antibodies to varicella zoster virus (VZV) glycoproteins were used to study the processing of three glycoproteins with molecular weights of 83K–94K (gp 2), 64K (gp 3), and 55K (gp 5). Immunoprecipitation experiments performed with VZV-infected cells, pulse labeled with [3H]glucosamine in the presence of tunicamycin, suggest that O-linked oligosaccharide is present on the glycoprotein of gp 2. Use of the enzyme endo-β-N-acetylglucosaminidase H revealed that the fully processed form of gp 3 had high-mannose type and that of gp 5 had only complex type of N-linked oligosaccharides. Experiments with monensin suggest that the precursor form (116K) of gp 3 is cleaved during the processing from Golgi apparatus to cell surface membrane. The extension of O-linked oligosaccharide chain and the complex type of N-linked oligosaccharide chains also occurs during this processing.</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">1985</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0330-3</identifier><part><date>1985</date><detail type="volume"><number>143</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>358</end></extent><extent unit="pages"><start>252</start><end>259</end></extent></part></relatedItem><identifier type="istex">A3F5A9DCDEFB811AFFF020BB19A144FBCEE7E0CF</identifier><identifier type="ark">ark:/67375/6H6-MJ1NNF78-X</identifier><identifier type="DOI">10.1016/0042-6822(85)90112-6</identifier><identifier type="PII">0042-6822(85)90112-6</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-MJ1NNF78-X/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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