Proteolytic cleavage of influenza virus hemagglutinins: primary structure of the connecting peptide between HA1 and HA2 determines proteolytic cleavability and pathogenicity of avian influenza viruses
Identifieur interne : 002723 ( Main/Exploration ); précédent : 002722; suivant : 002724Proteolytic cleavage of influenza virus hemagglutinins: primary structure of the connecting peptide between HA1 and HA2 determines proteolytic cleavability and pathogenicity of avian influenza viruses
Auteurs : F. X. Bosch [Allemagne] ; W. Garten [Allemagne] ; H.-D. Klenk [Allemagne] ; R. Rott [Allemagne]Source :
- Virology [ 0042-6822 ] ; 1981.
English descriptors
- Teeft :
- Activation process, Amino, Amino acid, Ampholines, Avian influenza viruses, Bosch, Cell lysates, Cell polypeptides, Cell types, Cellular enzyme, Cellular protease, Charge shift, Cleavability, Cleavable, Cleavage, Cleavage site, Equilibration, Equilibration buffer, Fowl plague virus, Hemagglutinin, Hemagglutinins, Human influenza viruses, Influenza, Influenza virus, Influenza virus hemagglutinin, Influenza virus hemagglutinins, Influenza viruses, Isoelectric, Isoelectric point, Isoelectric points, Klenk, Lysates, Lysis, Lysis buffer, Noncleavable, Nonpathogenic, Pathogenic, Pathogenic strains, Peptide, Polypeptide, Primary structure, Protease, Proteolytic, Proteolytic cleavability, Proteolytic cleavage, Rott, Second dimension, Servalyte, Soybean trypsin inhibitor, Structural basis, Subunit, Trypsin, Trypsin cleavage, Trypsin treatment, Virology, Virus, Virus hemagglutinins, Virus particles, Virus strains.
Abstract
Abstract: The structural basis for the different proteolytic cleavability of influenza virus hemagglutinin (HA) was investigated with a group of pathogenic and nonpathogenic avian influenza viruses belonging to the antigenic subtype H7 (Hav1). Infected cel lysates or lystates of purified virus particles were subjected to two-dimensional gel electrophoresis. The first dimension, isoelectric focusing,- was done under nonreducing conditions, the second dimension, SDS-PAGE, under reducing conditions. The results obtained permit the following conclusions: The amino acid sequence of the connecting peptide between HA1 and HA2 determines proteolytic cleavability by a trypsin-like cellular enzyme. Upon proteolytic cleavage of HA of pathogenic strains, peptides of differing positive charge were eliminated. These HAs have, however, significantly more basic connecting peptides than HAs of nonpathogenic viruses. HAs of nonpathogenic H7 strains appear to have a connecting peptide similar to the human influenza viruses, since treatment of these viruses with trypsin results in a similar small charge shift which probably corresponds to the elimination of one basic amino acid. Thus, the primary structure of the connecting peptide determines biological activation and thereby pathogenicity of these viruses.
Url:
DOI: 10.1016/0042-6822(81)90201-4
Affiliations:
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X." last="Bosch">F. X. Bosch</name><affiliation wicri:level="1"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Virologie, Justus-Liebig-Universität Giessen, D-6300 Giessen</wicri:regionArea><wicri:noRegion>D-6300 Giessen</wicri:noRegion><wicri:noRegion>D-6300 Giessen</wicri:noRegion></affiliation></author><author><name sortKey="Garten, W" sort="Garten, W" uniqKey="Garten W" first="W." last="Garten">W. Garten</name><affiliation wicri:level="1"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Virologie, Justus-Liebig-Universität Giessen, 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, H D" sort="Klenk, H D" uniqKey="Klenk H" first="H.-D." last="Klenk">H.-D. 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Rott</name><affiliation wicri:level="1"><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Virologie, Justus-Liebig-Universität Giessen, 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="725">725</biblScope><biblScope unit="page" to="735">735</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>Activation process</term><term>Amino</term><term>Amino acid</term><term>Ampholines</term><term>Avian influenza viruses</term><term>Bosch</term><term>Cell lysates</term><term>Cell polypeptides</term><term>Cell types</term><term>Cellular enzyme</term><term>Cellular protease</term><term>Charge shift</term><term>Cleavability</term><term>Cleavable</term><term>Cleavage</term><term>Cleavage site</term><term>Equilibration</term><term>Equilibration buffer</term><term>Fowl plague virus</term><term>Hemagglutinin</term><term>Hemagglutinins</term><term>Human influenza viruses</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus hemagglutinin</term><term>Influenza virus hemagglutinins</term><term>Influenza viruses</term><term>Isoelectric</term><term>Isoelectric point</term><term>Isoelectric points</term><term>Klenk</term><term>Lysates</term><term>Lysis</term><term>Lysis buffer</term><term>Noncleavable</term><term>Nonpathogenic</term><term>Pathogenic</term><term>Pathogenic strains</term><term>Peptide</term><term>Polypeptide</term><term>Primary structure</term><term>Protease</term><term>Proteolytic</term><term>Proteolytic cleavability</term><term>Proteolytic cleavage</term><term>Rott</term><term>Second dimension</term><term>Servalyte</term><term>Soybean trypsin inhibitor</term><term>Structural basis</term><term>Subunit</term><term>Trypsin</term><term>Trypsin cleavage</term><term>Trypsin treatment</term><term>Virology</term><term>Virus</term><term>Virus hemagglutinins</term><term>Virus particles</term><term>Virus strains</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The structural basis for the different proteolytic cleavability of influenza virus hemagglutinin (HA) was investigated with a group of pathogenic and nonpathogenic avian influenza viruses belonging to the antigenic subtype H7 (Hav1). Infected cel lysates or lystates of purified virus particles were subjected to two-dimensional gel electrophoresis. The first dimension, isoelectric focusing,- was done under nonreducing conditions, the second dimension, SDS-PAGE, under reducing conditions. The results obtained permit the following conclusions: The amino acid sequence of the connecting peptide between HA1 and HA2 determines proteolytic cleavability by a trypsin-like cellular enzyme. Upon proteolytic cleavage of HA of pathogenic strains, peptides of differing positive charge were eliminated. These HAs have, however, significantly more basic connecting peptides than HAs of nonpathogenic viruses. HAs of nonpathogenic H7 strains appear to have a connecting peptide similar to the human influenza viruses, since treatment of these viruses with trypsin results in a similar small charge shift which probably corresponds to the elimination of one basic amino acid. Thus, the primary structure of the connecting peptide determines biological activation and thereby pathogenicity of these viruses.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country></list><tree><country name="Allemagne"><noRegion><name sortKey="Bosch, F X" sort="Bosch, F X" uniqKey="Bosch F" first="F. X." last="Bosch">F. X. Bosch</name></noRegion><name sortKey="Garten, W" sort="Garten, W" uniqKey="Garten W" first="W." last="Garten">W. Garten</name><name sortKey="Klenk, H D" sort="Klenk, H D" uniqKey="Klenk H" first="H.-D." last="Klenk">H.-D. Klenk</name><name sortKey="Rott, R" sort="Rott, R" uniqKey="Rott R" first="R." last="Rott">R. Rott</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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