Mimicking rubella virus particles by using recombinant envelope glycoproteins and liposomes
The envelope glycoproteins E1 and E2 of rubella virus (RV) were engineered to display the FLAG epitope tag and a polyhistidine tag, at their amino and carboxy termini, respectively. These modified envelope proteins were produced in Sf9 insect cells utilizing baculovirus expression vectors, the E1 an...
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| Veröffentlicht in: | Journal of biotechnology 1999-10, Vol.75 (2), p.209-219 |
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| creator | Orellana, Adelina Mottershead, David van der Linden, Inge Keinänen, Kari Oker-Blom, Christian |
| description | The envelope glycoproteins E1 and E2 of rubella virus (RV) were engineered to display the FLAG epitope tag and a polyhistidine tag, at their amino and carboxy termini, respectively. These modified envelope proteins were produced in Sf9 insect cells utilizing baculovirus expression vectors, the E1 and E2 vectors giving rise to protein products of about 58 and 42 kDa, respectively. The recombinant proteins were purified by immobilized metal-ion affinity chromatography and reconstituted into liposomes via their hydrophobic transmembrane anchors. The liposomes were prepared by detergent dialysis in the presence of europium-DTPA chelate, enabling the subsequent measurement of the binding of the resultant proteoliposomes to the antibodies by time resolved fluorescence. RV mimicking proteoliposomes were recognized by antibodies specific for the E1 and E2 proteins, as well as the FLAG epitope tag. This type of virosome may prove useful for studies on the basic biological events of an RV infection or as diagnostic reagents. |
| doi_str_mv | 10.1016/S0168-1656(99)00162-5 |
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These modified envelope proteins were produced in Sf9 insect cells utilizing baculovirus expression vectors, the E1 and E2 vectors giving rise to protein products of about 58 and 42 kDa, respectively. The recombinant proteins were purified by immobilized metal-ion affinity chromatography and reconstituted into liposomes via their hydrophobic transmembrane anchors. The liposomes were prepared by detergent dialysis in the presence of europium-DTPA chelate, enabling the subsequent measurement of the binding of the resultant proteoliposomes to the antibodies by time resolved fluorescence. RV mimicking proteoliposomes were recognized by antibodies specific for the E1 and E2 proteins, as well as the FLAG epitope tag. This type of virosome may prove useful for studies on the basic biological events of an RV infection or as diagnostic reagents.</description><identifier>ISSN: 0168-1656</identifier><identifier>EISSN: 1873-4863</identifier><identifier>DOI: 10.1016/S0168-1656(99)00162-5</identifier><identifier>PMID: 10553659</identifier><identifier>CODEN: JBITD4</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Antibodies ; Antigens, Viral - genetics ; Baculovirus ; Biological and medical sciences ; Biotechnology ; Cells ; Chelating Agents - chemistry ; Chromatography ; Diagnostic products ; Dialysis ; Diseases ; Envelope proteins ; Europium - chemistry ; Europium-DTPA ; Fundamental and applied biological sciences. Psychology ; Glycoproteins - genetics ; Health. Pharmaceutical industry ; Immunoblotting ; Industrial applications and implications. Economical aspects ; Insect cells ; Lepidoptera - cytology ; Lepidoptera - genetics ; Liposomes ; Liposomes - chemistry ; Miscellaneous ; Molecular Mimicry ; Molecular Sequence Data ; Pentetic Acid - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Rubella - diagnosis ; Rubella virus ; Rubella virus - genetics ; Rubella virus - immunology ; Viral Envelope Proteins - genetics ; Viral Envelope Proteins - immunology ; Viral Envelope Proteins - isolation & purification</subject><ispartof>Journal of biotechnology, 1999-10, Vol.75 (2), p.209-219</ispartof><rights>1999 Elsevier Science B.V.</rights><rights>1999 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c452t-7989e290d390bfab9c4fc8cd0a83b852937b7a35fe3114eed5022eb7dba12293</citedby><cites>FETCH-LOGICAL-c452t-7989e290d390bfab9c4fc8cd0a83b852937b7a35fe3114eed5022eb7dba12293</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0168165699001625$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1991681$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10553659$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Orellana, Adelina</creatorcontrib><creatorcontrib>Mottershead, David</creatorcontrib><creatorcontrib>van der Linden, Inge</creatorcontrib><creatorcontrib>Keinänen, Kari</creatorcontrib><creatorcontrib>Oker-Blom, Christian</creatorcontrib><title>Mimicking rubella virus particles by using recombinant envelope glycoproteins and liposomes</title><title>Journal of biotechnology</title><addtitle>J Biotechnol</addtitle><description>The envelope glycoproteins E1 and E2 of rubella virus (RV) were engineered to display the FLAG epitope tag and a polyhistidine tag, at their amino and carboxy termini, respectively. These modified envelope proteins were produced in Sf9 insect cells utilizing baculovirus expression vectors, the E1 and E2 vectors giving rise to protein products of about 58 and 42 kDa, respectively. The recombinant proteins were purified by immobilized metal-ion affinity chromatography and reconstituted into liposomes via their hydrophobic transmembrane anchors. The liposomes were prepared by detergent dialysis in the presence of europium-DTPA chelate, enabling the subsequent measurement of the binding of the resultant proteoliposomes to the antibodies by time resolved fluorescence. RV mimicking proteoliposomes were recognized by antibodies specific for the E1 and E2 proteins, as well as the FLAG epitope tag. This type of virosome may prove useful for studies on the basic biological events of an RV infection or as diagnostic reagents.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antigens, Viral - genetics</subject><subject>Baculovirus</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cells</subject><subject>Chelating Agents - chemistry</subject><subject>Chromatography</subject><subject>Diagnostic products</subject><subject>Dialysis</subject><subject>Diseases</subject><subject>Envelope proteins</subject><subject>Europium - chemistry</subject><subject>Europium-DTPA</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins - genetics</subject><subject>Health. Pharmaceutical industry</subject><subject>Immunoblotting</subject><subject>Industrial applications and implications. Economical aspects</subject><subject>Insect cells</subject><subject>Lepidoptera - cytology</subject><subject>Lepidoptera - genetics</subject><subject>Liposomes</subject><subject>Liposomes - chemistry</subject><subject>Miscellaneous</subject><subject>Molecular Mimicry</subject><subject>Molecular Sequence Data</subject><subject>Pentetic Acid - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Rubella - diagnosis</subject><subject>Rubella virus</subject><subject>Rubella virus - genetics</subject><subject>Rubella virus - immunology</subject><subject>Viral Envelope Proteins - genetics</subject><subject>Viral Envelope Proteins - immunology</subject><subject>Viral Envelope Proteins - isolation & purification</subject><issn>0168-1656</issn><issn>1873-4863</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv3CAURlHUqpmk_QmpWFRVsnDKw9hmFVVR85BSZdHsukCAryMaGxywR5p_XzwzarObDQhx7ncvHITOKLmkhFbffuWlKWglqnMpL0g-sUIcoRVtal6UTcXfodU_5BidpPSHEFJKQT-gY0qE4JWQK_T7pxucfXH-GcfZQN9rvHZxTnjUcXK2h4TNBs9pC4ANg3Fe-wmDX0MfRsDP_caGMYYJnE9Y-xb3bgwpDJA-oved7hN82u-n6Onmx9P1XfHweHt__f2hsKVgU1HLRgKTpOWSmE4bacvONrYluuGmEUzy2tSaiw44pSVAKwhjYOrWaMry7Sn6uovNU7zOkCY1uGSXp3gIc1KVZGVJiDgIMlpyQUV9EKQ1r7KEJVHsQBtDShE6NUY36LhRlKhFk9pqUosDJaXaalJL3ed9g9kM0L6p2nnJwJc9oJPVfRe1ty7956TMsTRjVzsM8veuHUSVrANvoXVZ1qTa4A5M8hdoaK_1</recordid><startdate>19991008</startdate><enddate>19991008</enddate><creator>Orellana, Adelina</creator><creator>Mottershead, David</creator><creator>van der Linden, Inge</creator><creator>Keinänen, Kari</creator><creator>Oker-Blom, Christian</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>7QO</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19991008</creationdate><title>Mimicking rubella virus particles by using recombinant envelope glycoproteins and liposomes</title><author>Orellana, Adelina ; Mottershead, David ; van der Linden, Inge ; Keinänen, Kari ; Oker-Blom, Christian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c452t-7989e290d390bfab9c4fc8cd0a83b852937b7a35fe3114eed5022eb7dba12293</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antigens, Viral - genetics</topic><topic>Baculovirus</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cells</topic><topic>Chelating Agents - chemistry</topic><topic>Chromatography</topic><topic>Diagnostic products</topic><topic>Dialysis</topic><topic>Diseases</topic><topic>Envelope proteins</topic><topic>Europium - chemistry</topic><topic>Europium-DTPA</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins - genetics</topic><topic>Health. Pharmaceutical industry</topic><topic>Immunoblotting</topic><topic>Industrial applications and implications. Economical aspects</topic><topic>Insect cells</topic><topic>Lepidoptera - cytology</topic><topic>Lepidoptera - genetics</topic><topic>Liposomes</topic><topic>Liposomes - chemistry</topic><topic>Miscellaneous</topic><topic>Molecular Mimicry</topic><topic>Molecular Sequence Data</topic><topic>Pentetic Acid - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Rubella - diagnosis</topic><topic>Rubella virus</topic><topic>Rubella virus - genetics</topic><topic>Rubella virus - immunology</topic><topic>Viral Envelope Proteins - genetics</topic><topic>Viral Envelope Proteins - immunology</topic><topic>Viral Envelope Proteins - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Orellana, Adelina</creatorcontrib><creatorcontrib>Mottershead, David</creatorcontrib><creatorcontrib>van der Linden, Inge</creatorcontrib><creatorcontrib>Keinänen, Kari</creatorcontrib><creatorcontrib>Oker-Blom, Christian</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>Biotechnology Research Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Orellana, Adelina</au><au>Mottershead, David</au><au>van der Linden, Inge</au><au>Keinänen, Kari</au><au>Oker-Blom, Christian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mimicking rubella virus particles by using recombinant envelope glycoproteins and liposomes</atitle><jtitle>Journal of biotechnology</jtitle><addtitle>J Biotechnol</addtitle><date>1999-10-08</date><risdate>1999</risdate><volume>75</volume><issue>2</issue><spage>209</spage><epage>219</epage><pages>209-219</pages><issn>0168-1656</issn><eissn>1873-4863</eissn><coden>JBITD4</coden><abstract>The envelope glycoproteins E1 and E2 of rubella virus (RV) were engineered to display the FLAG epitope tag and a polyhistidine tag, at their amino and carboxy termini, respectively. These modified envelope proteins were produced in Sf9 insect cells utilizing baculovirus expression vectors, the E1 and E2 vectors giving rise to protein products of about 58 and 42 kDa, respectively. The recombinant proteins were purified by immobilized metal-ion affinity chromatography and reconstituted into liposomes via their hydrophobic transmembrane anchors. The liposomes were prepared by detergent dialysis in the presence of europium-DTPA chelate, enabling the subsequent measurement of the binding of the resultant proteoliposomes to the antibodies by time resolved fluorescence. RV mimicking proteoliposomes were recognized by antibodies specific for the E1 and E2 proteins, as well as the FLAG epitope tag. This type of virosome may prove useful for studies on the basic biological events of an RV infection or as diagnostic reagents.</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>10553659</pmid><doi>10.1016/S0168-1656(99)00162-5</doi><tpages>11</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Antibodies Antigens, Viral - genetics Baculovirus Biological and medical sciences Biotechnology Cells Chelating Agents - chemistry Chromatography Diagnostic products Dialysis Diseases Envelope proteins Europium - chemistry Europium-DTPA Fundamental and applied biological sciences. Psychology Glycoproteins - genetics Health. Pharmaceutical industry Immunoblotting Industrial applications and implications. Economical aspects Insect cells Lepidoptera - cytology Lepidoptera - genetics Liposomes Liposomes - chemistry Miscellaneous Molecular Mimicry Molecular Sequence Data Pentetic Acid - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Rubella - diagnosis Rubella virus Rubella virus - genetics Rubella virus - immunology Viral Envelope Proteins - genetics Viral Envelope Proteins - immunology Viral Envelope Proteins - isolation & purification |
| title | Mimicking rubella virus particles by using recombinant envelope glycoproteins and liposomes |
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