Carbohydrates of influenza virus IV. Strain-dependent variations
Identifieur interne : 002739 ( Main/Exploration ); précédent : 002738; suivant : 002740Carbohydrates of influenza virus IV. Strain-dependent variations
Auteurs : Ralph T. Schwarz [Allemagne] ; Hans-Dieter Klenk [Allemagne]Source :
- Virology [ 0042-6822 ] ; 1981.
English descriptors
- Teeft :
- Attachment site, Carbohydrate, Carbohydrate moiety, Carbohydrate side chains, Chick embryo cells, Compans, Complex type, Different serotypes, Dopheide, Fucose, Glucosamine, Glycopeptide, Glycopeptide patterns, Glycopeptides, Glycoprotein, Glycosylation, Glycosylation inhibitor, Glycosylation site, Hemagglutinin, Hemagglutinin fragments, Hemagglutinins, Hlnl, Important determinant, Influenza, Influenza virus, Influenza virus glycoproteins, Intermediate type, Keil, Klenk, Mannose, Nakamura, Neuraminidase, Oligosaccharide, Oligosaccharide side chains, Polyacrylamide, Polypeptide, Primary structure, Pronase, Pronase digestion, Proteolytic cleavage, Radioactive sugars, Same serotype, Schwarz, Serotype, Serotypes, Side chain, Side chains, Single side chain, Viral, Viral glycoproteins, Virology, Virus preparations.
Abstract
Abstract: The carbohydrates of the glycoproteins of 21 influenza A strains containing hemagglutinin and neuraminidase of all serotypes known to date have been compared by analysis of glycopeptides labeled with radioactive sugars. Analysis of incompletely glycosylated glycoproteins synthesized in the presence of glycosylation inhibitors allowed the determination of the number of oligosaccharide aide chains on HA2. With all strains, the neuraminidase contains side chains of both the complex type I and the mannose-rich type II. There are distinct quantitative and qualitative differences between the strains in the distribution of type I and type II side chains on the hemagglutinin fragments HA1 and HA2. The majority of the hemagglutinin oligosaccharides is located on HA1. These side chains are usually of type I. Only the hemagglutinins of serotype H3 have, in addition, a substantial amount of type II side chains on HA1. Most strains have on HA2 a single side chain which is usually of type I. With serotype H5 this side chain is free of fucose, and with serotype H8 it appears to be missing completely. Serotypes H7 and H10 have, in addition to the type I, a type II side chain on HA2. These observations strengthen the concept that the primary structure of the polypeptide chain is an important determinant for the carbohydrate moiety of the hemagglutinin.
Url:
DOI: 10.1016/0042-6822(81)90186-0
Affiliations:
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Strain-dependent variations</title><author><name sortKey="Schwarz, Ralph T" sort="Schwarz, Ralph T" uniqKey="Schwarz R" first="Ralph T." last="Schwarz">Ralph T. Schwarz</name><affiliation wicri:level="1"><country xml:lang="fr" wicri:curation="lc">Allemagne</country><wicri:regionArea>Institut für Virologie, Justus-Liebig-Universität, Frankfurter Str. 107, D-6300 Giessen</wicri:regionArea><wicri:noRegion>D-6300 Giessen</wicri:noRegion><wicri:noRegion>D-6300 Giessen</wicri:noRegion></affiliation></author><author><name sortKey="Klenk, Hans Dieter" sort="Klenk, Hans Dieter" uniqKey="Klenk H" first="Hans-Dieter" last="Klenk">Hans-Dieter Klenk</name><affiliation wicri:level="1"><country xml:lang="fr" wicri:curation="lc">Allemagne</country><wicri:regionArea>Institut für Virologie, Justus-Liebig-Universität, Frankfurter Str. 107, D-6300 Giessen</wicri:regionArea><wicri:noRegion>D-6300 Giessen</wicri:noRegion><wicri:noRegion>D-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="1981">1981</date><biblScope unit="volume">113</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="584">584</biblScope><biblScope unit="page" to="593">593</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>Attachment site</term><term>Carbohydrate</term><term>Carbohydrate moiety</term><term>Carbohydrate side chains</term><term>Chick embryo cells</term><term>Compans</term><term>Complex type</term><term>Different serotypes</term><term>Dopheide</term><term>Fucose</term><term>Glucosamine</term><term>Glycopeptide</term><term>Glycopeptide patterns</term><term>Glycopeptides</term><term>Glycoprotein</term><term>Glycosylation</term><term>Glycosylation inhibitor</term><term>Glycosylation site</term><term>Hemagglutinin</term><term>Hemagglutinin fragments</term><term>Hemagglutinins</term><term>Hlnl</term><term>Important determinant</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus glycoproteins</term><term>Intermediate type</term><term>Keil</term><term>Klenk</term><term>Mannose</term><term>Nakamura</term><term>Neuraminidase</term><term>Oligosaccharide</term><term>Oligosaccharide side chains</term><term>Polyacrylamide</term><term>Polypeptide</term><term>Primary structure</term><term>Pronase</term><term>Pronase digestion</term><term>Proteolytic cleavage</term><term>Radioactive sugars</term><term>Same serotype</term><term>Schwarz</term><term>Serotype</term><term>Serotypes</term><term>Side chain</term><term>Side chains</term><term>Single side chain</term><term>Viral</term><term>Viral glycoproteins</term><term>Virology</term><term>Virus preparations</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The carbohydrates of the glycoproteins of 21 influenza A strains containing hemagglutinin and neuraminidase of all serotypes known to date have been compared by analysis of glycopeptides labeled with radioactive sugars. Analysis of incompletely glycosylated glycoproteins synthesized in the presence of glycosylation inhibitors allowed the determination of the number of oligosaccharide aide chains on HA2. With all strains, the neuraminidase contains side chains of both the complex type I and the mannose-rich type II. There are distinct quantitative and qualitative differences between the strains in the distribution of type I and type II side chains on the hemagglutinin fragments HA1 and HA2. The majority of the hemagglutinin oligosaccharides is located on HA1. These side chains are usually of type I. Only the hemagglutinins of serotype H3 have, in addition, a substantial amount of type II side chains on HA1. Most strains have on HA2 a single side chain which is usually of type I. With serotype H5 this side chain is free of fucose, and with serotype H8 it appears to be missing completely. Serotypes H7 and H10 have, in addition to the type I, a type II side chain on HA2. These observations strengthen the concept that the primary structure of the polypeptide chain is an important determinant for the carbohydrate moiety of the hemagglutinin.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country></list><tree><country name="Allemagne"><noRegion><name sortKey="Schwarz, Ralph T" sort="Schwarz, Ralph T" uniqKey="Schwarz R" first="Ralph T." last="Schwarz">Ralph T. Schwarz</name></noRegion><name sortKey="Klenk, Hans Dieter" sort="Klenk, Hans Dieter" uniqKey="Klenk H" first="Hans-Dieter" last="Klenk">Hans-Dieter Klenk</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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