Radioimmunoassay analysis of baculovirus granulins and polyhedrins
Identifieur interne : 000949 ( Istex/Corpus ); précédent : 000948; suivant : 000950Radioimmunoassay analysis of baculovirus granulins and polyhedrins
Auteurs : Max D. Summers ; Pepper HoopsSource :
- Virology [ 0042-6822 ] ; 1980.
English descriptors
- Teeft :
- Acmnpv, Acmnpv polyhedrin, Antigenic, Antigenic determinants, Antiserum, Assay, Baculovirus, Baculoviruses, Cell lysates, Determinant, Dicapua, Final concentration, Granulin, Granulin proteins, Granulins, Immunodiffusion, Immunological, Immunological analysis, Immunoreactivity, Nuclear polyhedrosis viruses, Peptide, Polyhedrin, Polyhedrin proteins, Polyhedrins, Polyhedron, Polyhedrosis, Protease, Radioimmunoassay, Room temperature, Sfgv, Sfgv granulin, Tngv, Tngv granulin, Tngv granulin antiserum, Tnsnpv polyhedrin, Trichoplusia, Tris buffer, Tryptic, Tryptic peptides, Viral.
Abstract
Abstract: Granulin and polyhedrin proteins were purified by preparative sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis from the baculoviruses Autographa californica, Rachiplusia ou, Heliothis zea, Heliothis armigera, Trichoplusia ni, and Spodoptera frugiperda. Antisera were raised against Autographa californica (Ac) polyhedrin and Trichoplusia ni (Tn) granulin and analyzed for homologous and heterologous immunoreactivity by immunodiffusion and radioimmunoassay (RIA). Ac polyhedrin and Tn granulin antisera recognized antigenic determinants on several baculovirus polyhedrin and granulin proteins even though the heterologous proteins had different immunoreactivities when compared by competition radioimmunoassay. Antigenic differences among granulin and polyhedrin proteins were also detected by altered slopes of the competition reaction curves. Antiserum raised against Ac polyhedrin which was purified in the presence of SDS was tested by competition RIA for its ability to detect and react with native polyhedrin produced in the infected TN-368 cells. Ac polyhedrin antiserum had similar if not identical ability to bind to native polyhedrin and to polyhedrin purified in the presence of SDS.
Url:
DOI: 10.1016/0042-6822(80)90128-2
Links to Exploration step
ISTEX:7C4E286BD3F79303C61798D0AA6D5597EBDBEA73Le document en format XML
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Summers</name><affiliation><mods:affiliation>The Department of Entomology, Texas A&M University, College Station, Texas 77843, USA</mods:affiliation></affiliation></author><author><name sortKey="Hoops, Pepper" sort="Hoops, Pepper" uniqKey="Hoops P" first="Pepper" last="Hoops">Pepper Hoops</name><affiliation><mods:affiliation>The Department of Entomology, Texas A&M University, College Station, Texas 77843, USA</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:7C4E286BD3F79303C61798D0AA6D5597EBDBEA73</idno><date when="1980" year="1980">1980</date><idno type="doi">10.1016/0042-6822(80)90128-2</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-M9D4D045-L/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000949</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000949</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Radioimmunoassay analysis of baculovirus granulins and polyhedrins</title><author><name sortKey="Summers, Max D" sort="Summers, Max D" uniqKey="Summers M" first="Max D." last="Summers">Max D. Summers</name><affiliation><mods:affiliation>The Department of Entomology, Texas A&M University, College Station, Texas 77843, USA</mods:affiliation></affiliation></author><author><name sortKey="Hoops, Pepper" sort="Hoops, Pepper" uniqKey="Hoops P" first="Pepper" last="Hoops">Pepper Hoops</name><affiliation><mods:affiliation>The Department of Entomology, Texas A&M University, College Station, Texas 77843, USA</mods:affiliation></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="1980">1980</date><biblScope unit="volume">103</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="89">89</biblScope><biblScope unit="page" to="98">98</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>Acmnpv</term><term>Acmnpv polyhedrin</term><term>Antigenic</term><term>Antigenic determinants</term><term>Antiserum</term><term>Assay</term><term>Baculovirus</term><term>Baculoviruses</term><term>Cell lysates</term><term>Determinant</term><term>Dicapua</term><term>Final concentration</term><term>Granulin</term><term>Granulin proteins</term><term>Granulins</term><term>Immunodiffusion</term><term>Immunological</term><term>Immunological analysis</term><term>Immunoreactivity</term><term>Nuclear polyhedrosis viruses</term><term>Peptide</term><term>Polyhedrin</term><term>Polyhedrin proteins</term><term>Polyhedrins</term><term>Polyhedron</term><term>Polyhedrosis</term><term>Protease</term><term>Radioimmunoassay</term><term>Room temperature</term><term>Sfgv</term><term>Sfgv granulin</term><term>Tngv</term><term>Tngv granulin</term><term>Tngv granulin antiserum</term><term>Tnsnpv polyhedrin</term><term>Trichoplusia</term><term>Tris buffer</term><term>Tryptic</term><term>Tryptic peptides</term><term>Viral</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Granulin and polyhedrin proteins were purified by preparative sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis from the baculoviruses Autographa californica, Rachiplusia ou, Heliothis zea, Heliothis armigera, Trichoplusia ni, and Spodoptera frugiperda. Antisera were raised against Autographa californica (Ac) polyhedrin and Trichoplusia ni (Tn) granulin and analyzed for homologous and heterologous immunoreactivity by immunodiffusion and radioimmunoassay (RIA). Ac polyhedrin and Tn granulin antisera recognized antigenic determinants on several baculovirus polyhedrin and granulin proteins even though the heterologous proteins had different immunoreactivities when compared by competition radioimmunoassay. Antigenic differences among granulin and polyhedrin proteins were also detected by altered slopes of the competition reaction curves. Antiserum raised against Ac polyhedrin which was purified in the presence of SDS was tested by competition RIA for its ability to detect and react with native polyhedrin produced in the infected TN-368 cells. Ac polyhedrin antiserum had similar if not identical ability to bind to native polyhedrin and to polyhedrin purified in the presence of SDS.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>polyhedrin</json:string><json:string>granulin</json:string><json:string>polyhedrins</json:string><json:string>tngv</json:string><json:string>granulins</json:string><json:string>baculovirus</json:string><json:string>tngv granulin</json:string><json:string>immunodiffusion</json:string><json:string>antigenic</json:string><json:string>immunoreactivity</json:string><json:string>radioimmunoassay</json:string><json:string>polyhedrosis</json:string><json:string>acmnpv</json:string><json:string>sfgv</json:string><json:string>polyhedron</json:string><json:string>viral</json:string><json:string>baculoviruses</json:string><json:string>acmnpv polyhedrin</json:string><json:string>determinant</json:string><json:string>assay</json:string><json:string>protease</json:string><json:string>tryptic</json:string><json:string>trichoplusia</json:string><json:string>dicapua</json:string><json:string>immunological</json:string><json:string>antigenic determinants</json:string><json:string>sfgv granulin</json:string><json:string>tryptic peptides</json:string><json:string>antiserum</json:string><json:string>peptide</json:string><json:string>tris buffer</json:string><json:string>granulin proteins</json:string><json:string>room temperature</json:string><json:string>cell lysates</json:string><json:string>nuclear polyhedrosis viruses</json:string><json:string>final concentration</json:string><json:string>immunological analysis</json:string><json:string>tngv granulin antiserum</json:string><json:string>polyhedrin proteins</json:string><json:string>tnsnpv polyhedrin</json:string></teeft></keywords><author><json:item><name>Max D. Summers</name><affiliations><json:string>The Department of Entomology, Texas A&M University, College Station, Texas 77843, USA</json:string></affiliations></json:item><json:item><name>Pepper Hoops</name><affiliations><json:string>The Department of Entomology, Texas A&M University, College Station, Texas 77843, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-M9D4D045-L</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Granulin and polyhedrin proteins were purified by preparative sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis from the baculoviruses Autographa californica, Rachiplusia ou, Heliothis zea, Heliothis armigera, Trichoplusia ni, and Spodoptera frugiperda. Antisera were raised against Autographa californica (Ac) polyhedrin and Trichoplusia ni (Tn) granulin and analyzed for homologous and heterologous immunoreactivity by immunodiffusion and radioimmunoassay (RIA). Ac polyhedrin and Tn granulin antisera recognized antigenic determinants on several baculovirus polyhedrin and granulin proteins even though the heterologous proteins had different immunoreactivities when compared by competition radioimmunoassay. Antigenic differences among granulin and polyhedrin proteins were also detected by altered slopes of the competition reaction curves. Antiserum raised against Ac polyhedrin which was purified in the presence of SDS was tested by competition RIA for its ability to detect and react with native polyhedrin produced in the infected TN-368 cells. Ac polyhedrin antiserum had similar if not identical ability to bind to native polyhedrin and to polyhedrin purified in the presence of SDS.</abstract><qualityIndicators><score>8.37</score><pdfWordCount>4450</pdfWordCount><pdfCharCount>30552</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>10</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>160</abstractWordCount><abstractCharCount>1219</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Radioimmunoassay analysis of baculovirus granulins and polyhedrins</title><pmid><json:string>18631650</json:string></pmid><pii><json:string>0042-6822(80)90128-2</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>A Manual of Quantitative Immunoelectrophoresis</title><language><json:string>unknown</json:string></language><pages><first>161</first><last>164</last></pages><editor><json:item><name>N. 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(1973)</json:string><json:string>Searle Model 1195</json:string><json:string>Summers and Smith, 1976</json:string><json:string>Volkman et al., 1976</json:string><json:string>Summers and Egawa, 1973</json:string><json:string>Carroll et al., 1978</json:string><json:string>Hink, 1970</json:string><json:string>Sum- reactions were also detected with ACM NPV mers and Smith, 1976</json:string><json:string>Smith and Summers, 1979</json:string><json:string>Summers and Smith, 1975, 1976</json:string><json:string>Smith and Summers, 1978, 1979</json:string><json:string>Crawford and Kalmakoff, 1977</json:string><json:string>Volkman and Summers, 1975, 1976</json:string><json:string>Summers and Kawanishi, 1978</json:string><json:string>Kozlov et al., 1976</json:string><json:string>Ouchterlony, 1958</json:string><json:string>Volkman et al. (1976)</json:string><json:string>Lane and Robbins, 1978</json:string><json:string>McCarthy and DiCapua, 1979</json:string><json:string>Harboe and Ingild (1973)</json:string><json:string>Greenwood et al., 1963</json:string><json:string>Crozier and Meynadier, 1972a, b, 1973, 1975</json:string><json:string>Summers and Smith, 1976, 1978</json:string><json:string>Kozlov et al., 1975</json:string><json:string>Rohrmann et al., 1977</json:string><json:string>DiCapua and Norton, 1979</json:string><json:string>Maruniak and Summers, 1978</json:string><json:string>Ohba et al. (1977)</json:string><json:string>Eppstein and Thoma, 1975</json:string><json:string>Summers and Smith, 1978</json:string><json:string>Laemmli, 1970</json:string><json:string>Volkman and Sumers, 1976</json:string><json:string>Yagi et al., 1978</json:string><json:string>Lowry et al. 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Antisera were raised against Autographa californica (Ac) polyhedrin and Trichoplusia ni (Tn) granulin and analyzed for homologous and heterologous immunoreactivity by immunodiffusion and radioimmunoassay (RIA). Ac polyhedrin and Tn granulin antisera recognized antigenic determinants on several baculovirus polyhedrin and granulin proteins even though the heterologous proteins had different immunoreactivities when compared by competition radioimmunoassay. Antigenic differences among granulin and polyhedrin proteins were also detected by altered slopes of the competition reaction curves. Antiserum raised against Ac polyhedrin which was purified in the presence of SDS was tested by competition RIA for its ability to detect and react with native polyhedrin produced in the infected TN-368 cells. Ac polyhedrin antiserum had similar if not identical ability to bind to native polyhedrin and to polyhedrin purified in the presence of SDS.</p></abstract></profileDesc><revisionDesc><change when="1980">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-M9D4D045-L/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>YVIRO</jid><aid>80901282</aid><ce:pii>0042-6822(80)90128-2</ce:pii><ce:doi>10.1016/0042-6822(80)90128-2</ce:doi><ce:copyright type="unknown" year="1980"></ce:copyright></item-info><head><ce:title>Radioimmunoassay analysis of baculovirus granulins and polyhedrins</ce:title><ce:author-group><ce:author><ce:given-name>Max D.</ce:given-name><ce:surname>Summers</ce:surname><ce:cross-ref refid="COR1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Pepper</ce:given-name><ce:surname>Hoops</ce:surname></ce:author><ce:affiliation><ce:textfn>The Department of Entomology, Texas A&M University, College Station, Texas 77843, USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>1</ce:label><ce:text>To whom reprint requests should be addressed.</ce:text></ce:correspondence></ce:author-group><ce:date-accepted day="16" month="1" year="1980"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Granulin and polyhedrin proteins were purified by preparative sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis from the baculoviruses <ce:italic>Autographa californica, Rachiplusia ou, Heliothis zea, Heliothis armigera, Trichoplusia ni</ce:italic>, and Spodoptera frugiperda. Antisera were raised against <ce:italic>Autographa californica</ce:italic> (Ac) polyhedrin and <ce:italic>Trichoplusia ni</ce:italic> (Tn) granulin and analyzed for homologous and heterologous immunoreactivity by immunodiffusion and radioimmunoassay (RIA). Ac polyhedrin and Tn granulin antisera recognized antigenic determinants on several baculovirus polyhedrin and granulin proteins even though the heterologous proteins had different immunoreactivities when compared by competition radioimmunoassay. Antigenic differences among granulin and polyhedrin proteins were also detected by altered slopes of the competition reaction curves. Antiserum raised against Ac polyhedrin which was purified in the presence of SDS was tested by competition RIA for its ability to detect and react with native polyhedrin produced in the infected TN-368 cells. Ac polyhedrin antiserum had similar if not identical ability to bind to native polyhedrin and to polyhedrin purified in the presence of SDS.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Radioimmunoassay analysis of baculovirus granulins and polyhedrins</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Radioimmunoassay analysis of baculovirus granulins and polyhedrins</title></titleInfo><name type="personal"><namePart type="given">Max D.</namePart><namePart type="family">Summers</namePart><affiliation>The Department of Entomology, Texas A&M University, College Station, Texas 77843, USA</affiliation><description>To whom reprint requests should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Pepper</namePart><namePart type="family">Hoops</namePart><affiliation>The Department of Entomology, Texas A&M University, College Station, Texas 77843, USA</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">1980</dateIssued><copyrightDate encoding="w3cdtf">1980</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Granulin and polyhedrin proteins were purified by preparative sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis from the baculoviruses Autographa californica, Rachiplusia ou, Heliothis zea, Heliothis armigera, Trichoplusia ni, and Spodoptera frugiperda. Antisera were raised against Autographa californica (Ac) polyhedrin and Trichoplusia ni (Tn) granulin and analyzed for homologous and heterologous immunoreactivity by immunodiffusion and radioimmunoassay (RIA). Ac polyhedrin and Tn granulin antisera recognized antigenic determinants on several baculovirus polyhedrin and granulin proteins even though the heterologous proteins had different immunoreactivities when compared by competition radioimmunoassay. Antigenic differences among granulin and polyhedrin proteins were also detected by altered slopes of the competition reaction curves. Antiserum raised against Ac polyhedrin which was purified in the presence of SDS was tested by competition RIA for its ability to detect and react with native polyhedrin produced in the infected TN-368 cells. Ac polyhedrin antiserum had similar if not identical ability to bind to native polyhedrin and to polyhedrin purified in the presence of SDS.</abstract><relatedItem type="host"><titleInfo><title>Virology</title></titleInfo><titleInfo type="abbreviated"><title>YVIRO</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">1980</dateIssued></originInfo><identifier type="ISSN">0042-6822</identifier><identifier type="PII">S0042-6822(00)X0288-7</identifier><part><date>1980</date><detail type="volume"><number>103</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>265</end></extent><extent unit="pages"><start>89</start><end>98</end></extent></part></relatedItem><identifier type="istex">7C4E286BD3F79303C61798D0AA6D5597EBDBEA73</identifier><identifier type="ark">ark:/67375/6H6-M9D4D045-L</identifier><identifier type="DOI">10.1016/0042-6822(80)90128-2</identifier><identifier type="PII">0042-6822(80)90128-2</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-M9D4D045-L/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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