Processing of virus-specific glycoproteins of varicella zoster virus
Identifieur interne : 001620 ( Main/Exploration ); précédent : 001619; suivant : 001621Processing of virus-specific glycoproteins of varicella zoster virus
Auteurs : Junko Namazue [Japon] ; Harvey Campo-Vera [Japon] ; Kenji Kitamura [Japon] ; Toshiomi Okuno [Japon] ; Koichi Yamanishi [Japon]Source :
- 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
Affiliations:
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xml:lang="fr">Japon</country><wicri:regionArea>Department of Pediatrics, School of Medicine, Mie University, Tsu, Mie 514</wicri:regionArea><wicri:noRegion>Mie 514</wicri:noRegion></affiliation></author><author><name sortKey="Okuno, Toshiomi" sort="Okuno, Toshiomi" uniqKey="Okuno T" first="Toshiomi" last="Okuno">Toshiomi Okuno</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565</wicri:regionArea><wicri:noRegion>Osaka 565</wicri:noRegion></affiliation></author><author><name sortKey="Yamanishi, Koichi" sort="Yamanishi, Koichi" uniqKey="Yamanishi K" first="Koichi" last="Yamanishi">Koichi Yamanishi</name><affiliation></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Virology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565</wicri:regionArea><wicri:noRegion>Osaka 565</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">143</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="252">252</biblScope><biblScope unit="page" to="259">259</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>Cell cultures</term><term>Cell extracts</term><term>Complex type</term><term>Endo</term><term>Glycoprotein</term><term>Glycosylation</term><term>Golgi apparatus</term><term>Herpes</term><term>Herpes simplex virus</term><term>Herpes 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><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Namazue, Junko" sort="Namazue, Junko" uniqKey="Namazue J" first="Junko" last="Namazue">Junko Namazue</name></noRegion><name sortKey="Campo Vera, Harvey" sort="Campo Vera, Harvey" uniqKey="Campo Vera H" first="Harvey" last="Campo-Vera">Harvey Campo-Vera</name><name sortKey="Kitamura, Kenji" sort="Kitamura, Kenji" uniqKey="Kitamura K" first="Kenji" last="Kitamura">Kenji Kitamura</name><name sortKey="Okuno, Toshiomi" sort="Okuno, Toshiomi" uniqKey="Okuno T" first="Toshiomi" last="Okuno">Toshiomi Okuno</name><name sortKey="Yamanishi, Koichi" sort="Yamanishi, Koichi" uniqKey="Yamanishi K" first="Koichi" last="Yamanishi">Koichi Yamanishi</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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