Conformational changes in influenza virus haemagglutinin and its monomer detected by monoclonal antibodies
Identifieur interne : 001591 ( Istex/Curation ); précédent : 001590; suivant : 001592Conformational changes in influenza virus haemagglutinin and its monomer detected by monoclonal antibodies
Auteurs : Ann N. Nestorowicz [Australie] ; David O. White [Australie] ; David C. Jackson [Australie]Source :
- Vaccine [ 0264-410X ] ; 1985.
English descriptors
- Teeft :
- Ambient temperature, Amino acid substitutions, Antibody, Antigenic, Antigenic determinants, Antigenic properties, Antigenic site, Antigenic sites, Antigenic structure, Binding properties, Bromelain, Centrifugation, Conformational changes, Determinant, Distinct epitopes, Epitope, Haemagglutinin, Influenza, Influenza virus, Influenza virus haemagglutinin, Influenza viruses, Initial concentration, Intact virus, Laver, Loop region, Monoclonal, Monoclonal antibodies, Monomer, Monomeric, Monomeric form, Nestorowicz, Pbsa, Radial position, Radioiodinated bromelain, Radiolabelled, Radiolabelled bromelain, Reactivity patterns, Room temperature, Sedimentation, Skehel, Substitution, Sucrose, Sucrose gradients, Tertiary structure, Trimer, Trimeric, Variant, Variant viruses, Virology, Virus.
Abstract
Abstract: Exposure of influenza virus haemagglutinin to pH 5 results in conformational changes occurring in the molecule which are accompanied by antigenic modifications. Furthermore, isolated haemagglutinin (HA) at a concentration of 0.1 nM undergoes dissociation from the trimeric to a monomeric form when exposed to pH 5. Whether present on intact virus or as the isolated monomer, each form of haemagglutinin from pH 5 exhibits similar alterations in antigenic characteristics. These forms of HA show modifications in the antigenic sites located in the hinge (site C), tip (site B) and subunit interface (site D) regions. Whereas binding of monoclonal antibodies recognizing the tip and interface is abrogated or diminished, binding of antibodies to the hinge region is greatly enhanced following exposure of virus or the monomeric form of HA to pH 5.
Url:
DOI: 10.1016/0264-410X(85)90099-4
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White</name><affiliation wicri:level="1"><mods:affiliation>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052, Australia</mods:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052</wicri:regionArea></affiliation></author><author><name sortKey="Jackson, David C" sort="Jackson, David C" uniqKey="Jackson D" first="David C." last="Jackson">David C. Jackson</name><affiliation wicri:level="1"><mods:affiliation>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052, Australia</mods:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:6AE61E75DF24149C180727F1D1CC926C4C051B7B</idno><date when="1985" year="1985">1985</date><idno type="doi">10.1016/0264-410X(85)90099-4</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-JLD2J8Q1-7/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001591</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001591</idno><idno type="wicri:Area/Istex/Curation">001591</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Conformational changes in influenza virus haemagglutinin and its monomer detected by monoclonal antibodies</title><author><name sortKey="Nestorowicz, Ann N" sort="Nestorowicz, Ann N" uniqKey="Nestorowicz A" first="Ann N." last="Nestorowicz">Ann N. Nestorowicz</name><affiliation wicri:level="1"><mods:affiliation>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052, Australia</mods:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052</wicri:regionArea></affiliation></author><author><name sortKey="White, David O" sort="White, David O" uniqKey="White D" first="David O." last="White">David O. White</name><affiliation wicri:level="1"><mods:affiliation>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052, Australia</mods:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052</wicri:regionArea></affiliation></author><author><name sortKey="Jackson, David C" sort="Jackson, David C" uniqKey="Jackson D" first="David C." last="Jackson">David C. Jackson</name><affiliation wicri:level="1"><mods:affiliation>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052, Australia</mods:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Microbiology, University of Melbourne, Parkville, Victoria 3052</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Vaccine</title><title level="j" type="abbrev">JVAC</title><idno type="ISSN">0264-410X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1985">1985</date><biblScope unit="volume">3</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="175">175</biblScope><biblScope unit="page" to="181">181</biblScope></imprint><idno type="ISSN">0264-410X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0264-410X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Ambient temperature</term><term>Amino acid substitutions</term><term>Antibody</term><term>Antigenic</term><term>Antigenic determinants</term><term>Antigenic properties</term><term>Antigenic site</term><term>Antigenic sites</term><term>Antigenic structure</term><term>Binding properties</term><term>Bromelain</term><term>Centrifugation</term><term>Conformational changes</term><term>Determinant</term><term>Distinct epitopes</term><term>Epitope</term><term>Haemagglutinin</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus haemagglutinin</term><term>Influenza viruses</term><term>Initial concentration</term><term>Intact virus</term><term>Laver</term><term>Loop region</term><term>Monoclonal</term><term>Monoclonal antibodies</term><term>Monomer</term><term>Monomeric</term><term>Monomeric form</term><term>Nestorowicz</term><term>Pbsa</term><term>Radial position</term><term>Radioiodinated bromelain</term><term>Radiolabelled</term><term>Radiolabelled bromelain</term><term>Reactivity patterns</term><term>Room temperature</term><term>Sedimentation</term><term>Skehel</term><term>Substitution</term><term>Sucrose</term><term>Sucrose gradients</term><term>Tertiary structure</term><term>Trimer</term><term>Trimeric</term><term>Variant</term><term>Variant viruses</term><term>Virology</term><term>Virus</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Exposure of influenza virus haemagglutinin to pH 5 results in conformational changes occurring in the molecule which are accompanied by antigenic modifications. Furthermore, isolated haemagglutinin (HA) at a concentration of 0.1 nM undergoes dissociation from the trimeric to a monomeric form when exposed to pH 5. Whether present on intact virus or as the isolated monomer, each form of haemagglutinin from pH 5 exhibits similar alterations in antigenic characteristics. These forms of HA show modifications in the antigenic sites located in the hinge (site C), tip (site B) and subunit interface (site D) regions. Whereas binding of monoclonal antibodies recognizing the tip and interface is abrogated or diminished, binding of antibodies to the hinge region is greatly enhanced following exposure of virus or the monomeric form of HA to pH 5.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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