Simultaneous purification of influenza haemagglutinin and neuraminidase proteins by immunochromatography
Identifieur interne : 000A98 ( Istex/Corpus ); précédent : 000A97; suivant : 000A99Simultaneous purification of influenza haemagglutinin and neuraminidase proteins by immunochromatography
Auteurs : L. Gerantes ; N. Kessler ; G. Thomas ; M. AymardSource :
- 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
Links to Exploration step
ISTEX:334A580D5E80A7E8026E109426608FEFE7784700Le document en format XML
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Gerantes</name><affiliations><json:string>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</json:string></affiliations></json:item><json:item><name>N. Kessler</name><affiliations><json:string>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</json:string></affiliations></json:item><json:item><name>G. Thomas</name><affiliations><json:string>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</json:string></affiliations></json:item><json:item><name>M. Aymard</name><affiliations><json:string>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Influenza</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Haemagglutinin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Neuraminidase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Purification</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Immunochromatography</value></json:item></subject><arkIstex>ark:/67375/6H6-3K2XFQT1-G</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><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.</abstract><qualityIndicators><score>8.016</score><pdfWordCount>3880</pdfWordCount><pdfCharCount>25150</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>11</pdfPageCount><pdfPageSize>540 x 720 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>178</abstractWordCount><abstractCharCount>1252</abstractCharCount><keywordCount>5</keywordCount></qualityIndicators><title>Simultaneous purification of influenza haemagglutinin and neuraminidase proteins by immunochromatography</title><pmid><json:string>8783161</json:string></pmid><pii><json:string>0166-0934(96)02006-X</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Doctoral dissertation</title><language><json:string>unknown</json:string></language></serie><host><title>Journal of Virological Methods</title><language><json:string>unknown</json:string></language><publicationDate>1996</publicationDate><issn><json:string>0166-0934</json:string></issn><pii><json:string>S0166-0934(00)X0003-1</json:string></pii><volume>58</volume><issue>1–2</issue><pages><first>155</first><last>165</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>10s</json:string><json:string>1996</json:string></date><geogName></geogName><orgName><json:string>France Accepted</json:string><json:string>WHO Influenza Center</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Chalumeau</json:string><json:string>G. Thomas</json:string><json:string>A. Douglas</json:string><json:string>A. D. Douglas</json:string><json:string>M. Aymard</json:string><json:string>N. Kessler</json:string></persName><placeName><json:string>Beijing</json:string><json:string>Antigenicity</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Brand and Skehel, 1972</json:string><json:string>MC Kimm-Breschkin et al., 1991</json:string><json:string>Kilbourne, 1969</json:string><json:string>Kida et al. (1982)</json:string><json:string>Webster and Darlington, 1969</json:string><json:string>L. Gerentes et al.</json:string><json:string>Laver and Valentine, 1969</json:string><json:string>Aymard-Henry et al. (1973)</json:string><json:string>MC Ilvain, 1921</json:string><json:string>Palmer et al. (1975)</json:string><json:string>Gallagher et al., 1984</json:string><json:string>Colman et al., 1983</json:string><json:string>Laver, 1964</json:string><json:string>Gallagher et al. (1984)</json:string><json:string>Weber and Osborn (1969)</json:string><json:string>Varghese et al., 1983</json:string><json:string>Dopheide and Ward, 1981</json:string><json:string>Wilson et al., 1981</json:string><json:string>Laemmli, 1970</json:string><json:string>Laver et al., 1984</json:string><json:string>Colman and Laver, 1981</json:string><json:string>Webster et al., 1984</json:string><json:string>Laver and Kilbourne, 1966</json:string><json:string>Liu et al., 1995</json:string><json:string>Block et al., 1982</json:string><json:string>Laver, 1978</json:string><json:string>Lowry et al. (1951)</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-3K2XFQT1-G</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - virology</json:string><json:string>2 - biotechnology & applied microbiology</json:string><json:string>2 - biochemical research methods</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - virology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Immunology and Microbiology</json:string><json:string>3 - Virology</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string><json:string>4 - microbiologie</json:string></inist></categories><publicationDate>1996</publicationDate><copyrightDate>1996</copyrightDate><doi><json:string>10.1016/0166-0934(96)02006-X</json:string></doi><id>334A580D5E80A7E8026E109426608FEFE7784700</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-3K2XFQT1-G/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-3K2XFQT1-G/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-3K2XFQT1-G/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Simultaneous purification of influenza haemagglutinin and neuraminidase proteins by immunochromatography</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1996</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note type="content">Section title: Research paper</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Simultaneous purification of influenza haemagglutinin and neuraminidase proteins by immunochromatography</title><author xml:id="author-0000"><persName><forename type="first">L.</forename><surname>Gerantes</surname></persName><note type="correspondence"><p>Corresponding author.</p></note><affiliation>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</affiliation></author><author xml:id="author-0001"><persName><forename type="first">N.</forename><surname>Kessler</surname></persName><affiliation>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</affiliation></author><author xml:id="author-0002"><persName><forename type="first">G.</forename><surname>Thomas</surname></persName><affiliation>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</affiliation></author><author xml:id="author-0003"><persName><forename type="first">M.</forename><surname>Aymard</surname></persName><affiliation>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</affiliation></author><idno type="istex">334A580D5E80A7E8026E109426608FEFE7784700</idno><idno type="ark">ark:/67375/6H6-3K2XFQT1-G</idno><idno type="DOI">10.1016/0166-0934(96)02006-X</idno><idno type="PII">0166-0934(96)02006-X</idno></analytic><monogr><title level="j">Journal of Virological Methods</title><title level="j" type="abbrev">VIRMET</title><idno type="pISSN">0166-0934</idno><idno type="PII">S0166-0934(00)X0003-1</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="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></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1996</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>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.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Influenza</term></item><item><term>Haemagglutinin</term></item><item><term>Neuraminidase</term></item><item><term>Purification</term></item><item><term>Immunochromatography</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1996">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-3K2XFQT1-G/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>VIRMET</jid><aid>9602006X</aid><ce:pii>0166-0934(96)02006-X</ce:pii><ce:doi>10.1016/0166-0934(96)02006-X</ce:doi><ce:copyright type="unknown" year="1996"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Research paper</ce:textfn></ce:dochead><ce:title>Simultaneous purification of influenza haemagglutinin and neuraminidase proteins by immunochromatography</ce:title><ce:author-group><ce:author><ce:given-name>L.</ce:given-name><ce:surname>Gerantes</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>N.</ce:given-name><ce:surname>Kessler</ce:surname></ce:author><ce:author><ce:given-name>G.</ce:given-name><ce:surname>Thomas</ce:surname></ce:author><ce:author><ce:given-name>M.</ce:given-name><ce:surname>Aymard</ce:surname></ce:author><ce:affiliation><ce:textfn>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Corresponding author.</ce:text></ce:correspondence></ce:author-group><ce:date-accepted day="21" month="12" year="1995"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>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.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Influenza</ce:text></ce:keyword><ce:keyword><ce:text>Haemagglutinin</ce:text></ce:keyword><ce:keyword><ce:text>Neuraminidase</ce:text></ce:keyword><ce:keyword><ce:text>Purification</ce:text></ce:keyword><ce:keyword><ce:text>Immunochromatography</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Simultaneous purification of influenza haemagglutinin and neuraminidase proteins by immunochromatography</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Simultaneous purification of influenza haemagglutinin and neuraminidase proteins by immunochromatography</title></titleInfo><name type="personal"><namePart type="given">L.</namePart><namePart type="family">Gerantes</namePart><affiliation>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</affiliation><description>Corresponding author.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">N.</namePart><namePart type="family">Kessler</namePart><affiliation>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G.</namePart><namePart type="family">Thomas</namePart><affiliation>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="family">Aymard</namePart><affiliation>Laboratoire de Virologie — Faculté de Médecine, Centre National de Référence de la Grippe, France Sud, 8 avenue Rockefeller, 69373 Lyon cedex 08, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1996</dateIssued><copyrightDate encoding="w3cdtf">1996</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract 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.</abstract><note type="content">Section title: Research paper</note><subject><genre>Keywords</genre><topic>Influenza</topic><topic>Haemagglutinin</topic><topic>Neuraminidase</topic><topic>Purification</topic><topic>Immunochromatography</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Virological Methods</title></titleInfo><titleInfo type="abbreviated"><title>VIRMET</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1996</dateIssued></originInfo><identifier type="ISSN">0166-0934</identifier><identifier type="PII">S0166-0934(00)X0003-1</identifier><part><date>1996</date><detail type="volume"><number>58</number><caption>vol.</caption></detail><detail type="issue"><number>1–2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>217</end></extent><extent unit="pages"><start>155</start><end>165</end></extent></part></relatedItem><identifier type="istex">334A580D5E80A7E8026E109426608FEFE7784700</identifier><identifier type="ark">ark:/67375/6H6-3K2XFQT1-G</identifier><identifier type="DOI">10.1016/0166-0934(96)02006-X</identifier><identifier type="PII">0166-0934(96)02006-X</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-3K2XFQT1-G/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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