Immunoaffinity purification of native dimer forms of the flavivirus non-structural glycoprotein, NS1
The flavivirus non-structural glycoprotein, NS1 has been shown to elicit an immune response in animals which may confer protection from subsequent virus challenge (Schlesinger et al., 1985 and 1987). While previous reports have outlined methods for obtaining cell-associated NS1 in monomeric form for...
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| Veröffentlicht in: | Journal of virological methods 1990-12, Vol.30 (3), p.323-332 |
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| container_title | Journal of virological methods |
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| creator | Falconar, Andrew K.I. Young, Paul R. |
| description | The flavivirus non-structural glycoprotein, NS1 has been shown to elicit an immune response in animals which may confer protection from subsequent virus challenge (Schlesinger et al., 1985 and 1987). While previous reports have outlined methods for obtaining cell-associated NS1 in monomeric form for these studies, we describe here an efficient method for the immunoaffinity purification of both cell-associated and secreted NS1 in their native dimeric configuration. These dimer preparations were shown to be both more antigenic and immunogenic than their monomeric counterparts, a finding which may in part explain the reported failure to obtain solid protection of mice from homologous dengue virus challenge. In moderately sized virus growth experiments, greater than 1 mg quantities of purified NS1 were obtained. |
| doi_str_mv | 10.1016/0166-0934(90)90075-Q |
| format | Article |
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While previous reports have outlined methods for obtaining cell-associated NS1 in monomeric form for these studies, we describe here an efficient method for the immunoaffinity purification of both cell-associated and secreted NS1 in their native dimeric configuration. These dimer preparations were shown to be both more antigenic and immunogenic than their monomeric counterparts, a finding which may in part explain the reported failure to obtain solid protection of mice from homologous dengue virus challenge. 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While previous reports have outlined methods for obtaining cell-associated NS1 in monomeric form for these studies, we describe here an efficient method for the immunoaffinity purification of both cell-associated and secreted NS1 in their native dimeric configuration. These dimer preparations were shown to be both more antigenic and immunogenic than their monomeric counterparts, a finding which may in part explain the reported failure to obtain solid protection of mice from homologous dengue virus challenge. In moderately sized virus growth experiments, greater than 1 mg quantities of purified NS1 were obtained.</description><subject>Animals</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Biological and medical sciences</subject><subject>Capsid - immunology</subject><subject>Capsid - isolation & purification</subject><subject>Chromatography, Affinity</subject><subject>Dengue virus</subject><subject>Dengue Virus - analysis</subject><subject>Flavivirus</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immunoaffinity chromatography</subject><subject>Immunoblot</subject><subject>Mice</subject><subject>Microbiology</subject><subject>Techniques used in virology</subject><subject>Vero Cells</subject><subject>Viral Core Proteins - immunology</subject><subject>Viral Core Proteins - isolation & purification</subject><subject>Viral Nonstructural Proteins</subject><subject>Virology</subject><issn>0166-0934</issn><issn>1879-0984</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kF1rFDEUhoModVv9Bwpzo1RwNJ8zyY0gRW2htBT1OmSTE43MJNsks7D_3qy71LtehIRznvOe8CD0iuAPBJPhYztDjxXj5wq_UxiPor97glZEjqqVJX-KVg_Ic3Rayh-MsRgZO0EnlAgsmVwhdzXPS0zG-xBD3XWbJQcfrKkhxS75LrbXFjoXZsidT3ku-2r9DZ2fzDZsQ15KF1PsS82LrUs2U_dr2tm0yalCiO-7m-_kBXrmzVTg5fE-Qz-_fvlxcdlf3367uvh83VuGae0lEIKNGOTaYkU9uDUHvlZi9BicM05YKqWwg2LSc07ZoDwxg7dcUOXtMLIz9PaQ25bfL1CqnkOxME0mQlqKlpiRQVHRQH4AbU6lZPB6k8Ns8k4TrPdy9d6c3pvTCut_cvVdG3t9zF_WM7iHoaPN1n9z7JtizeSziTaU_9mKj1Qx2rhPBw6ajG2ArIsNEC24kMFW7VJ4_CN_AQ_vl5w</recordid><startdate>199012</startdate><enddate>199012</enddate><creator>Falconar, Andrew K.I.</creator><creator>Young, Paul R.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199012</creationdate><title>Immunoaffinity purification of native dimer forms of the flavivirus non-structural glycoprotein, NS1</title><author>Falconar, Andrew K.I. ; Young, Paul R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c302t-8e110a568bc092fedb4e4b957f0eddad5c2885c6938f442369f1a6fc4529fc673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Biological and medical sciences</topic><topic>Capsid - immunology</topic><topic>Capsid - isolation & purification</topic><topic>Chromatography, Affinity</topic><topic>Dengue virus</topic><topic>Dengue Virus - analysis</topic><topic>Flavivirus</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immunoaffinity chromatography</topic><topic>Immunoblot</topic><topic>Mice</topic><topic>Microbiology</topic><topic>Techniques used in virology</topic><topic>Vero Cells</topic><topic>Viral Core Proteins - immunology</topic><topic>Viral Core Proteins - isolation & purification</topic><topic>Viral Nonstructural Proteins</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Falconar, Andrew K.I.</creatorcontrib><creatorcontrib>Young, Paul R.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of virological methods</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Falconar, Andrew K.I.</au><au>Young, Paul R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immunoaffinity purification of native dimer forms of the flavivirus non-structural glycoprotein, NS1</atitle><jtitle>Journal of virological methods</jtitle><addtitle>J Virol Methods</addtitle><date>1990-12</date><risdate>1990</risdate><volume>30</volume><issue>3</issue><spage>323</spage><epage>332</epage><pages>323-332</pages><issn>0166-0934</issn><eissn>1879-0984</eissn><coden>JVMEDH</coden><abstract>The flavivirus non-structural glycoprotein, NS1 has been shown to elicit an immune response in animals which may confer protection from subsequent virus challenge (Schlesinger et al., 1985 and 1987). While previous reports have outlined methods for obtaining cell-associated NS1 in monomeric form for these studies, we describe here an efficient method for the immunoaffinity purification of both cell-associated and secreted NS1 in their native dimeric configuration. These dimer preparations were shown to be both more antigenic and immunogenic than their monomeric counterparts, a finding which may in part explain the reported failure to obtain solid protection of mice from homologous dengue virus challenge. In moderately sized virus growth experiments, greater than 1 mg quantities of purified NS1 were obtained.</abstract><cop>London</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>2150838</pmid><doi>10.1016/0166-0934(90)90075-Q</doi><tpages>10</tpages></addata></record> |
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| identifier | ISSN: 0166-0934 |
| ispartof | Journal of virological methods, 1990-12, Vol.30 (3), p.323-332 |
| issn | 0166-0934 1879-0984 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Animals Antibodies, Monoclonal - immunology Biological and medical sciences Capsid - immunology Capsid - isolation & purification Chromatography, Affinity Dengue virus Dengue Virus - analysis Flavivirus Fundamental and applied biological sciences. Psychology Immunoaffinity chromatography Immunoblot Mice Microbiology Techniques used in virology Vero Cells Viral Core Proteins - immunology Viral Core Proteins - isolation & purification Viral Nonstructural Proteins Virology |
| title | Immunoaffinity purification of native dimer forms of the flavivirus non-structural glycoprotein, NS1 |
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