Expression of biologically active recombinant porcine interleukin-12 from Escherichia coli
The control of viral infections is of critical importance to livestock industries worldwide and is highlighted by costly infection outbreaks, such as that seen with foot and mouth disease virus. To ameliorate the impact of increasing problems with viral infections, new vaccine and anti-viral strateg...
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| Veröffentlicht in: | Veterinary immunology and immunopathology 2008-12, Vol.126 (3), p.373-376 |
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| creator | Morris, K.R. Bruce, M.P. Janardhana, V. Thomas, J.D. Bean, A.G.D. Strom, D.G. |
| description | The control of viral infections is of critical importance to livestock industries worldwide and is highlighted by costly infection outbreaks, such as that seen with foot and mouth disease virus. To ameliorate the impact of increasing problems with viral infections, new vaccine and anti-viral strategies are required and a greater understanding of the anti-viral response is essential. Furthermore, in pigs, evidence is still being gathered on the components of a defined anti-viral immune response. However, this has been greatly improved by the recent cloning and expression of critical cytokines involved in the anti-viral response. To assess the use of recombinant porcine interleukin-12 (rPoIL-12) as an immunotherapeutic and immunomodulator of swine, we have cloned and expressed rPoIL-12 as a single-chain fusion protein from
Esherichia coli (
E. coli). The fusion encodes the p40 and p35 subunits, linked by a glycine–serine linker and expressed as a C-terminal 6xHis tagged protein. rPoIL-12 stimulated the proliferation of human lymphoblasts and its activity on porcine cells was demonstrated by the ability of rPoIL-12 to increase the mRNA expression of porcine interleukin-18 receptor-α (poIL-18Rα) from porcine peripheral blood mononuclear cells (PoPMBCs). This data supports the inclusion of
E. coli produced rPoIL-12 in immunomodulation strategies in the pig. |
| doi_str_mv | 10.1016/j.vetimm.2008.07.015 |
| format | Article |
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Esherichia coli (
E. coli). The fusion encodes the p40 and p35 subunits, linked by a glycine–serine linker and expressed as a C-terminal 6xHis tagged protein. rPoIL-12 stimulated the proliferation of human lymphoblasts and its activity on porcine cells was demonstrated by the ability of rPoIL-12 to increase the mRNA expression of porcine interleukin-18 receptor-α (poIL-18Rα) from porcine peripheral blood mononuclear cells (PoPMBCs). This data supports the inclusion of
E. coli produced rPoIL-12 in immunomodulation strategies in the pig.</description><identifier>ISSN: 0165-2427</identifier><identifier>EISSN: 1873-2534</identifier><identifier>DOI: 10.1016/j.vetimm.2008.07.015</identifier><identifier>PMID: 18823664</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Animals ; cell-mediated immunity ; Cloning, Molecular ; cytokines ; disease prevention ; E. coli ; Escherichia coli ; Fusion protein ; Gene Expression Regulation - immunology ; immunostimulants ; Immunotherapy - methods ; Immunotherapy - veterinary ; in vitro studies ; Interleukin-12 ; Interleukin-12 - metabolism ; Interleukin-18 Receptor alpha Subunit - metabolism ; lymphocyte proliferation ; molecular cloning ; prokaryotic cells ; protective effect ; recombinant fusion proteins ; Recombinant Proteins - metabolism ; recombinant vaccines ; Sus scrofa - immunology ; Swine ; swine diseases ; vaccination ; vaccine development ; viral diseases of animals and humans ; Viral Vaccines - immunology</subject><ispartof>Veterinary immunology and immunopathology, 2008-12, Vol.126 (3), p.373-376</ispartof><rights>2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-9ced7f84b1966cd02dad8e39db2494e6b9242e5a32c6add38988f0936e9443273</citedby><cites>FETCH-LOGICAL-c415t-9ced7f84b1966cd02dad8e39db2494e6b9242e5a32c6add38988f0936e9443273</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.vetimm.2008.07.015$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18823664$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Morris, K.R.</creatorcontrib><creatorcontrib>Bruce, M.P.</creatorcontrib><creatorcontrib>Janardhana, V.</creatorcontrib><creatorcontrib>Thomas, J.D.</creatorcontrib><creatorcontrib>Bean, A.G.D.</creatorcontrib><creatorcontrib>Strom, D.G.</creatorcontrib><title>Expression of biologically active recombinant porcine interleukin-12 from Escherichia coli</title><title>Veterinary immunology and immunopathology</title><addtitle>Vet Immunol Immunopathol</addtitle><description>The control of viral infections is of critical importance to livestock industries worldwide and is highlighted by costly infection outbreaks, such as that seen with foot and mouth disease virus. To ameliorate the impact of increasing problems with viral infections, new vaccine and anti-viral strategies are required and a greater understanding of the anti-viral response is essential. Furthermore, in pigs, evidence is still being gathered on the components of a defined anti-viral immune response. However, this has been greatly improved by the recent cloning and expression of critical cytokines involved in the anti-viral response. To assess the use of recombinant porcine interleukin-12 (rPoIL-12) as an immunotherapeutic and immunomodulator of swine, we have cloned and expressed rPoIL-12 as a single-chain fusion protein from
Esherichia coli (
E. coli). The fusion encodes the p40 and p35 subunits, linked by a glycine–serine linker and expressed as a C-terminal 6xHis tagged protein. rPoIL-12 stimulated the proliferation of human lymphoblasts and its activity on porcine cells was demonstrated by the ability of rPoIL-12 to increase the mRNA expression of porcine interleukin-18 receptor-α (poIL-18Rα) from porcine peripheral blood mononuclear cells (PoPMBCs). This data supports the inclusion of
E. coli produced rPoIL-12 in immunomodulation strategies in the pig.</description><subject>Animals</subject><subject>cell-mediated immunity</subject><subject>Cloning, Molecular</subject><subject>cytokines</subject><subject>disease prevention</subject><subject>E. coli</subject><subject>Escherichia coli</subject><subject>Fusion protein</subject><subject>Gene Expression Regulation - immunology</subject><subject>immunostimulants</subject><subject>Immunotherapy - methods</subject><subject>Immunotherapy - veterinary</subject><subject>in vitro studies</subject><subject>Interleukin-12</subject><subject>Interleukin-12 - metabolism</subject><subject>Interleukin-18 Receptor alpha Subunit - metabolism</subject><subject>lymphocyte proliferation</subject><subject>molecular cloning</subject><subject>prokaryotic cells</subject><subject>protective effect</subject><subject>recombinant fusion proteins</subject><subject>Recombinant Proteins - metabolism</subject><subject>recombinant vaccines</subject><subject>Sus scrofa - immunology</subject><subject>Swine</subject><subject>swine diseases</subject><subject>vaccination</subject><subject>vaccine development</subject><subject>viral diseases of animals and humans</subject><subject>Viral Vaccines - immunology</subject><issn>0165-2427</issn><issn>1873-2534</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EokvhHyDIiVtSf8WxL0ioWj6kSj3QXrhYjj1pZ0nixc6u2n9fV1mJG5zmMM87mnmGkPeMNowydbFrjrDgNDWcUt3QrqGsfUE2THei5q2QL8mmYG3NJe_OyJucd5TS1mj9mpwxrblQSm7Ir-3DPkHOGOcqDlWPcYx36N04PlbOL3iEKoGPU4-zm5dqH5PHGSqcF0gjHH7jXDNeDSlO1Tb7e0jo79FVPo74lrwa3Jjh3amek9uv25vL7_XV9bcfl1-uai9Zu9TGQ-gGLXtmlPKB8uCCBmFCz6WRoHpTLoDWCe6VC0HocsJAjVBgpBS8E-fk0zp3n-KfA-TFTpg9jKObIR6yVUYLpqT5L8hMqyg3qoByBX2KOScY7D7h5NKjZdQ-y7c7u8q3z_It7WyRX2IfTvMP_QThb-hkuwAfV2Bw0bq7hNne_uSUiZIubckL8XkloAg7IiSbPcJcFGF5w2JDxH_v8ARkeKGO</recordid><startdate>20081215</startdate><enddate>20081215</enddate><creator>Morris, K.R.</creator><creator>Bruce, M.P.</creator><creator>Janardhana, V.</creator><creator>Thomas, J.D.</creator><creator>Bean, A.G.D.</creator><creator>Strom, D.G.</creator><general>Elsevier B.V</general><general>Amsterdam: Elsevier</general><scope>FBQ</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>7QL</scope><scope>7T5</scope><scope>7U9</scope><scope>C1K</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20081215</creationdate><title>Expression of biologically active recombinant porcine interleukin-12 from Escherichia coli</title><author>Morris, K.R. ; 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Esherichia coli (
E. coli). The fusion encodes the p40 and p35 subunits, linked by a glycine–serine linker and expressed as a C-terminal 6xHis tagged protein. rPoIL-12 stimulated the proliferation of human lymphoblasts and its activity on porcine cells was demonstrated by the ability of rPoIL-12 to increase the mRNA expression of porcine interleukin-18 receptor-α (poIL-18Rα) from porcine peripheral blood mononuclear cells (PoPMBCs). This data supports the inclusion of
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| subjects | Animals cell-mediated immunity Cloning, Molecular cytokines disease prevention E. coli Escherichia coli Fusion protein Gene Expression Regulation - immunology immunostimulants Immunotherapy - methods Immunotherapy - veterinary in vitro studies Interleukin-12 Interleukin-12 - metabolism Interleukin-18 Receptor alpha Subunit - metabolism lymphocyte proliferation molecular cloning prokaryotic cells protective effect recombinant fusion proteins Recombinant Proteins - metabolism recombinant vaccines Sus scrofa - immunology Swine swine diseases vaccination vaccine development viral diseases of animals and humans Viral Vaccines - immunology |
| title | Expression of biologically active recombinant porcine interleukin-12 from Escherichia coli |
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