Measurement of IgG antibodies to house dust mite and grass pollen by a solid‐phase radioimmunoassay
Identifieur interne : 000B70 ( Istex/Corpus ); précédent : 000B69; suivant : 000B71Measurement of IgG antibodies to house dust mite and grass pollen by a solid‐phase radioimmunoassay
Auteurs : G. Delespesse ; M. J. Debisschop ; J. FlamentSource :
- Clinical & Experimental Allergy [ 0954-7894 ] ; 1979-09.
Abstract
Polystyrene microtubes, coated with extracts of either Dermatophagoides pteronyssinus (DPT) or grass pollens, were used as the solid‐phase in a radioimmunoassay for the measurement of specific IgG antibodies to the corresponding allergen. Radiolabelled protein A from Staphylococcus aureus (SpA) was used to determine the IgG antibodies attached to the tubes. The binding of IgG from either normal or allergic sera to DPT‐coated tubes was antigen specific and mediated by the Fab fragment of the immunoglobulin. IgG antibodies purified by affinity chromatography from non‐allergic serum competed with IgE antibodies to DPT. IgE antibodies do not significantly interfere with the assay. Indeed, heating a reaginic serum resulted in a striking reduction of the (125I) anti‐IgE binding to allergen‐coated tubes without modifying the (125I)‐SpA binding. Furthermore, filtration of a reaginic serum through Sephacryl S‐200 separated a peak of IgE antibodies, characterized by a high binding of labelled a‐IgE and a low binding of (125I)‐SpA from the peak of IgG antibodies defined by low a‐IgE and high SpA binding. The solid phase method is more sensitive than a double‐antibody technique employing the same DPT extract as labelled antigen. Non‐allergic subjects had less IgG antibodies to DPT or grass pollens than allergic patients. In untreated patients, there was a good correlation between levels of IgG and IgE antibodies to grass pollens but not to DPT. Patients hyposensitized to house dust mite had on the average three times more specific IgG antibodies than untreated cases.
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DOI: 10.1111/j.1365-2222.1979.tb02515.x
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St Pierre, Dept Immunology, Brussels Free University, Belgium</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Clinical & Experimental Allergy</title><idno type="ISSN">0954-7894</idno><idno type="eISSN">1365-2222</idno><imprint><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1979-09">1979-09</date><biblScope unit="volume">9</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="503">503</biblScope><biblScope unit="page" to="514">514</biblScope></imprint><idno type="ISSN">0954-7894</idno></series><idno type="istex">7DF697D38A12DCC928C05E1B3DDAC39EA5511552</idno><idno type="DOI">10.1111/j.1365-2222.1979.tb02515.x</idno><idno type="ArticleID">CEA503</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0954-7894</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Polystyrene microtubes, coated with extracts of either Dermatophagoides pteronyssinus (DPT) or grass pollens, were used as the solid‐phase in a radioimmunoassay for the measurement of specific IgG antibodies to the corresponding allergen. Radiolabelled protein A from Staphylococcus aureus (SpA) was used to determine the IgG antibodies attached to the tubes. The binding of IgG from either normal or allergic sera to DPT‐coated tubes was antigen specific and mediated by the Fab fragment of the immunoglobulin. IgG antibodies purified by affinity chromatography from non‐allergic serum competed with IgE antibodies to DPT. IgE antibodies do not significantly interfere with the assay. Indeed, heating a reaginic serum resulted in a striking reduction of the (125I) anti‐IgE binding to allergen‐coated tubes without modifying the (125I)‐SpA binding. Furthermore, filtration of a reaginic serum through Sephacryl S‐200 separated a peak of IgE antibodies, characterized by a high binding of labelled a‐IgE and a low binding of (125I)‐SpA from the peak of IgG antibodies defined by low a‐IgE and high SpA binding. The solid phase method is more sensitive than a double‐antibody technique employing the same DPT extract as labelled antigen. Non‐allergic subjects had less IgG antibodies to DPT or grass pollens than allergic patients. In untreated patients, there was a good correlation between levels of IgG and IgE antibodies to grass pollens but not to DPT. Patients hyposensitized to house dust mite had on the average three times more specific IgG antibodies than untreated cases.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>G. DELESPESSE</name><affiliations><json:string>Hop. St Pierre, Dept Immunology, Brussels Free University, Belgium</json:string></affiliations></json:item><json:item><name>M. J. DEBISSCHOP</name><affiliations><json:string>Hop. St Pierre, Dept Immunology, Brussels Free University, Belgium</json:string></affiliations></json:item><json:item><name>J. FLAMENT</name><affiliations><json:string>Hop. 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Indeed, heating a reaginic serum resulted in a striking reduction of the (125I) anti‐IgE binding to allergen‐coated tubes without modifying the (125I)‐SpA binding. Furthermore, filtration of a reaginic serum through Sephacryl S‐200 separated a peak of IgE antibodies, characterized by a high binding of labelled a‐IgE and a low binding of (125I)‐SpA from the peak of IgG antibodies defined by low a‐IgE and high SpA binding. The solid phase method is more sensitive than a double‐antibody technique employing the same DPT extract as labelled antigen. Non‐allergic subjects had less IgG antibodies to DPT or grass pollens than allergic patients. In untreated patients, there was a good correlation between levels of IgG and IgE antibodies to grass pollens but not to DPT. 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Delespesse, Hôpital Saint‐Pierre Departement d'Immunologie, Rue Haute 322, 1000 Bruxelles, Belgium.</p></note><affiliation>Hop. St Pierre, Dept Immunology, Brussels Free University, Belgium</affiliation></author><author><persName><forename type="first">M. J.</forename><surname>DEBISSCHOP</surname></persName><affiliation>Hop. St Pierre, Dept Immunology, Brussels Free University, Belgium</affiliation></author><author><persName><forename type="first">J.</forename><surname>FLAMENT</surname></persName><affiliation>Hop. St Pierre, Dept Immunology, Brussels Free University, Belgium</affiliation></author></analytic><monogr><title level="j">Clinical & Experimental Allergy</title><idno type="pISSN">0954-7894</idno><idno type="eISSN">1365-2222</idno><idno type="DOI">10.1111/(ISSN)1365-2222</idno><imprint><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1979-09"></date><biblScope unit="volume">9</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="503">503</biblScope><biblScope unit="page" to="514">514</biblScope></imprint></monogr><idno type="istex">7DF697D38A12DCC928C05E1B3DDAC39EA5511552</idno><idno type="DOI">10.1111/j.1365-2222.1979.tb02515.x</idno><idno type="ArticleID">CEA503</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1979</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Polystyrene microtubes, coated with extracts of either Dermatophagoides pteronyssinus (DPT) or grass pollens, were used as the solid‐phase in a radioimmunoassay for the measurement of specific IgG antibodies to the corresponding allergen. Radiolabelled protein A from Staphylococcus aureus (SpA) was used to determine the IgG antibodies attached to the tubes. The binding of IgG from either normal or allergic sera to DPT‐coated tubes was antigen specific and mediated by the Fab fragment of the immunoglobulin. IgG antibodies purified by affinity chromatography from non‐allergic serum competed with IgE antibodies to DPT. IgE antibodies do not significantly interfere with the assay. Indeed, heating a reaginic serum resulted in a striking reduction of the (125I) anti‐IgE binding to allergen‐coated tubes without modifying the (125I)‐SpA binding. Furthermore, filtration of a reaginic serum through Sephacryl S‐200 separated a peak of IgE antibodies, characterized by a high binding of labelled a‐IgE and a low binding of (125I)‐SpA from the peak of IgG antibodies defined by low a‐IgE and high SpA binding. The solid phase method is more sensitive than a double‐antibody technique employing the same DPT extract as labelled antigen. Non‐allergic subjects had less IgG antibodies to DPT or grass pollens than allergic patients. In untreated patients, there was a good correlation between levels of IgG and IgE antibodies to grass pollens but not to DPT. Patients hyposensitized to house dust mite had on the average three times more specific IgG antibodies than untreated cases.</p></abstract></profileDesc><revisionDesc><change when="1979-09">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/7DF697D38A12DCC928C05E1B3DDAC39EA5511552/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Blackwell Publishing Ltd</publisherName><publisherLoc>Oxford, UK</publisherLoc></publisherInfo><doi origin="wiley" registered="yes">10.1111/(ISSN)1365-2222</doi><issn type="print">0954-7894</issn><issn type="electronic">1365-2222</issn><idGroup><id type="product" value="CEA"></id><id type="publisherDivision" value="ST"></id></idGroup><titleGroup><title type="main" sort="CLINICAL EXPERIMENTAL ALLERGY">Clinical & Experimental Allergy</title></titleGroup></publicationMeta><publicationMeta level="part" position="09005"><doi origin="wiley">10.1111/cea.1979.9.issue-5</doi><numberingGroup><numbering type="journalVolume" number="9">9</numbering><numbering type="journalIssue" number="5">5</numbering></numberingGroup><coverDate startDate="1979-09">September 1979</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="0050300" status="forIssue"><doi origin="wiley">10.1111/j.1365-2222.1979.tb02515.x</doi><idGroup><id type="unit" value="CEA503"></id></idGroup><countGroup><count type="pageTotal" number="12"></count></countGroup><eventGroup><event type="firstOnline" date="2006-04-27"></event><event type="publishedOnlineFinalForm" date="2006-04-27"></event><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:2.3.2 mode:FullText source:HeaderRef result:HeaderRef" date="2010-03-09"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-09"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-16"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="503">503</numbering><numbering type="pageLast" number="514">514</numbering></numberingGroup><correspondenceTo>Dr G. Delespesse, Hôpital Saint‐Pierre Departement d'Immunologie, Rue Haute 322, 1000 Bruxelles, Belgium.</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:CEA.CEA503.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>(Received 17 January 1979; accepted for publication 20 February 1979)</unparsedEditorialHistory><countGroup><count type="referenceTotal" number="22"></count><count type="linksCrossRef" number="4"></count></countGroup><titleGroup><title type="main">Measurement of IgG antibodies to house dust mite and grass pollen by a solid‐phase radioimmunoassay</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1" corresponding="yes"><personName><givenNames>G.</givenNames><familyName>DELESPESSE</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a1"><personName><givenNames>M. J.</givenNames><familyName>DEBISSCHOP</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a1"><personName><givenNames>J.</givenNames><familyName>FLAMENT</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="BE"><unparsedAffiliation>Hop. St Pierre, Dept Immunology, Brussels Free University, Belgium</unparsedAffiliation></affiliation></affiliationGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Summary</title><p>Polystyrene microtubes, coated with extracts of either <i>Dermatophagoides pteronyssinus</i> (DPT) or grass pollens, were used as the solid‐phase in a radioimmunoassay for the measurement of specific IgG antibodies to the corresponding allergen. Radiolabelled protein A from <i>Staphylococcus aureus</i> (SpA) was used to determine the IgG antibodies attached to the tubes. The binding of IgG from either normal or allergic sera to DPT‐coated tubes was antigen specific and mediated by the Fab fragment of the immunoglobulin. IgG antibodies purified by affinity chromatography from non‐allergic serum competed with IgE antibodies to DPT.</p><p>IgE antibodies do not significantly interfere with the assay. Indeed, heating a reaginic serum resulted in a striking reduction of the (<sup>125</sup>I) anti‐IgE binding to allergen‐coated tubes without modifying the (<sup>125</sup>I)‐SpA binding. Furthermore, filtration of a reaginic serum through Sephacryl S‐200 separated a peak of IgE antibodies, characterized by a high binding of labelled a‐IgE and a low binding of (<sup>125</sup>I)‐SpA from the peak of IgG antibodies defined by low a‐IgE and high SpA binding.</p><p>The solid phase method is more sensitive than a double‐antibody technique employing the same DPT extract as labelled antigen. Non‐allergic subjects had less IgG antibodies to DPT or grass pollens than allergic patients.</p><p>In untreated patients, there was a good correlation between levels of IgG and IgE antibodies to grass pollens but not to DPT. Patients hyposensitized to house dust mite had on the average three times more specific IgG antibodies than untreated cases.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Measurement of IgG antibodies to house dust mite and grass pollen by a solid‐phase radioimmunoassay</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Measurement of IgG antibodies to house dust mite and grass pollen by a solid‐phase radioimmunoassay</title></titleInfo><name type="personal"><namePart type="given">G.</namePart><namePart type="family">DELESPESSE</namePart><affiliation>Hop. St Pierre, Dept Immunology, Brussels Free University, Belgium</affiliation><description>Correspondence: Dr G. Delespesse, Hôpital Saint‐Pierre Departement d'Immunologie, Rue Haute 322, 1000 Bruxelles, Belgium.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M. J.</namePart><namePart type="family">DEBISSCHOP</namePart><affiliation>Hop. St Pierre, Dept Immunology, Brussels Free University, Belgium</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.</namePart><namePart type="family">FLAMENT</namePart><affiliation>Hop. St Pierre, Dept Immunology, Brussels Free University, Belgium</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">1979-09</dateIssued><edition>(Received 17 January 1979; accepted for publication 20 February 1979)</edition><copyrightDate encoding="w3cdtf">1979</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="references">22</extent></physicalDescription><abstract lang="en">Polystyrene microtubes, coated with extracts of either Dermatophagoides pteronyssinus (DPT) or grass pollens, were used as the solid‐phase in a radioimmunoassay for the measurement of specific IgG antibodies to the corresponding allergen. Radiolabelled protein A from Staphylococcus aureus (SpA) was used to determine the IgG antibodies attached to the tubes. The binding of IgG from either normal or allergic sera to DPT‐coated tubes was antigen specific and mediated by the Fab fragment of the immunoglobulin. IgG antibodies purified by affinity chromatography from non‐allergic serum competed with IgE antibodies to DPT. IgE antibodies do not significantly interfere with the assay. Indeed, heating a reaginic serum resulted in a striking reduction of the (125I) anti‐IgE binding to allergen‐coated tubes without modifying the (125I)‐SpA binding. Furthermore, filtration of a reaginic serum through Sephacryl S‐200 separated a peak of IgE antibodies, characterized by a high binding of labelled a‐IgE and a low binding of (125I)‐SpA from the peak of IgG antibodies defined by low a‐IgE and high SpA binding. The solid phase method is more sensitive than a double‐antibody technique employing the same DPT extract as labelled antigen. Non‐allergic subjects had less IgG antibodies to DPT or grass pollens than allergic patients. In untreated patients, there was a good correlation between levels of IgG and IgE antibodies to grass pollens but not to DPT. Patients hyposensitized to house dust mite had on the average three times more specific IgG antibodies than untreated cases.</abstract><relatedItem type="host"><titleInfo><title>Clinical & Experimental Allergy</title></titleInfo><genre type="Journal">journal</genre><identifier type="ISSN">0954-7894</identifier><identifier type="eISSN">1365-2222</identifier><identifier type="DOI">10.1111/(ISSN)1365-2222</identifier><identifier type="PublisherID">CEA</identifier><part><date>1979</date><detail type="volume"><caption>vol.</caption><number>9</number></detail><detail type="issue"><caption>no.</caption><number>5</number></detail><extent unit="pages"><start>503</start><end>514</end><total>12</total></extent></part></relatedItem><identifier type="istex">7DF697D38A12DCC928C05E1B3DDAC39EA5511552</identifier><identifier type="DOI">10.1111/j.1365-2222.1979.tb02515.x</identifier><identifier type="ArticleID">CEA503</identifier><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Blackwell Publishing Ltd</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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