Simultaneous purification of influenza haemagglutinin and neuraminidase proteins by immunochromatography
Identifieur interne : 000282 ( France/Analysis ); précédent : 000281; suivant : 000283Simultaneous purification of influenza haemagglutinin and neuraminidase proteins by immunochromatography
Auteurs : L. Gerantes [France] ; N. Kessler [France] ; G. Thomas [France] ; M. Aymard [France]Source :
- Journal of Virological Methods [ 0166-0934 ] ; 1996.
English descriptors
- Teeft :
- Active center, Active centre, Active site, Activity titration, Ammonium sulphate, Antigenic, Antigenic properties, Column volume, Different samples, Efficient technique, Fetuin substrate, Flow rate, Functional activity, Gerentes, Glycoprotein, Glycoprotein mixture, Hemagglutinin, Hemagglutinin activity, Heterologous system, Immunity studies, Influenza, Influenza virus, Influenza virus neuraminidase, Influenza virus strains, Inhibition tests, Initial activities, Initial virus sample, Laver, Mabs, Marker proteins, Molecular weight, Molecule, Monoclonal antibodies, Myeloma cells, Neuraminidase, Neuraminidase subunits, Page control, Partial degradation, Pure form, Purification, Recombinant virus, Sepharose, Sepharose column, Sepharose columns, Sialic acid, Spleen cells, Strength conditions, Supernatant, Virological, Virological methods, Virology, Virus, Virus neuraminidase, Virus sample.
Abstract
Abstract: A new and rapid method for co-purification of haemagglutinin (HA) and neuraminidase (NA) proteins from influenza A/H3N2 virases is described. Surface glycoproteins were first solubilized using a non-ionic detergent under high ionic strength conditions, then they were separated by chromatography on sepharose previously bound to monoclonal antibodies (MAbs) directed either against HA (IaH-chromatography) or against NA (IaN-chromatography). Depending on the protein specificity of the MAb immobilized on the column, HA or NA was bound to sepharose and the counterpart protein was free in the flow-through volume. laH-chromatography and IaN-chromatography proved equally efficient in term of recoveries (> 75%) and purity (≥ 99%) of both HA and NA but differences appeared when considering functional and antigenic properties of pure proteins. Those properties were highly retained in IaH- and IaN-derived HA as well as in IaH-derived NA while IaN-NA was partially degraded. laH-chromatography allowed the co-purification of HA and NA proteins in heterologous antigen-antibody system with a 50% rate of cross reactivity. IaH-HA and IaH-NA may be suitable for immunity studies, standardization of influenza vaccine and for diagnostic purposes.
Url:
DOI: 10.1016/0166-0934(96)02006-X
Affiliations:
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ISTEX:334A580D5E80A7E8026E109426608FEFE7784700Le document en format XML
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Aymard</name><affiliation wicri:level="3"><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08</wicri:regionArea><placeName><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region><settlement type="city">Lyon</settlement></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Virological Methods</title><title level="j" type="abbrev">VIRMET</title><idno type="ISSN">0166-0934</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996">1996</date><biblScope unit="volume">58</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="155">155</biblScope><biblScope unit="page" to="165">165</biblScope></imprint><idno type="ISSN">0166-0934</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0166-0934</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Active center</term><term>Active centre</term><term>Active site</term><term>Activity titration</term><term>Ammonium sulphate</term><term>Antigenic</term><term>Antigenic properties</term><term>Column volume</term><term>Different samples</term><term>Efficient technique</term><term>Fetuin substrate</term><term>Flow rate</term><term>Functional activity</term><term>Gerentes</term><term>Glycoprotein</term><term>Glycoprotein mixture</term><term>Hemagglutinin</term><term>Hemagglutinin activity</term><term>Heterologous system</term><term>Immunity studies</term><term>Influenza</term><term>Influenza virus</term><term>Influenza virus neuraminidase</term><term>Influenza virus strains</term><term>Inhibition tests</term><term>Initial activities</term><term>Initial virus sample</term><term>Laver</term><term>Mabs</term><term>Marker proteins</term><term>Molecular weight</term><term>Molecule</term><term>Monoclonal antibodies</term><term>Myeloma cells</term><term>Neuraminidase</term><term>Neuraminidase subunits</term><term>Page control</term><term>Partial degradation</term><term>Pure form</term><term>Purification</term><term>Recombinant virus</term><term>Sepharose</term><term>Sepharose column</term><term>Sepharose columns</term><term>Sialic acid</term><term>Spleen cells</term><term>Strength conditions</term><term>Supernatant</term><term>Virological</term><term>Virological methods</term><term>Virology</term><term>Virus</term><term>Virus neuraminidase</term><term>Virus sample</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: A new and rapid method for co-purification of haemagglutinin (HA) and neuraminidase (NA) proteins from influenza A/H3N2 virases is described. Surface glycoproteins were first solubilized using a non-ionic detergent under high ionic strength conditions, then they were separated by chromatography on sepharose previously bound to monoclonal antibodies (MAbs) directed either against HA (IaH-chromatography) or against NA (IaN-chromatography). Depending on the protein specificity of the MAb immobilized on the column, HA or NA was bound to sepharose and the counterpart protein was free in the flow-through volume. laH-chromatography and IaN-chromatography proved equally efficient in term of recoveries (> 75%) and purity (≥ 99%) of both HA and NA but differences appeared when considering functional and antigenic properties of pure proteins. Those properties were highly retained in IaH- and IaN-derived HA as well as in IaH-derived NA while IaN-NA was partially degraded. laH-chromatography allowed the co-purification of HA and NA proteins in heterologous antigen-antibody system with a 50% rate of cross reactivity. IaH-HA and IaH-NA may be suitable for immunity studies, standardization of influenza vaccine and for diagnostic purposes.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Rhône-Alpes</li></region><settlement><li>Lyon</li></settlement></list><tree><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Gerantes, L" sort="Gerantes, L" uniqKey="Gerantes L" first="L." last="Gerantes">L. Gerantes</name></region><name sortKey="Aymard, M" sort="Aymard, M" uniqKey="Aymard M" first="M." last="Aymard">M. Aymard</name><name sortKey="Kessler, N" sort="Kessler, N" uniqKey="Kessler N" first="N." last="Kessler">N. Kessler</name><name sortKey="Thomas, G" sort="Thomas, G" uniqKey="Thomas G" first="G." last="Thomas">G. Thomas</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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