cDNA cloning of biologically active chicken interleukin-18
By searching a chicken EST database, we identified a cDNA clone that appeared to contain the entire open reading frame (ORF) of chicken interleukin-18 (ChIL-18). The encoded protein consists of 198 amino acids and exhibits approximately 30% sequence identity to IL-18 of humans and various others mam...
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| Veröffentlicht in: | Journal of interferon & cytokine research 2000-10, Vol.20 (10), p.879-883 |
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| container_title | Journal of interferon & cytokine research |
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| creator | Schneider, K Puehler, F Baeuerle, D Elvers, S Staeheli, P Kaspers, B Weining, K C |
| description | By searching a chicken EST database, we identified a cDNA clone that appeared to contain the entire open reading frame (ORF) of chicken interleukin-18 (ChIL-18). The encoded protein consists of 198 amino acids and exhibits approximately 30% sequence identity to IL-18 of humans and various others mammals. Sequence comparisons reveals a putative caspase-1 cleavage site at aspartic acid 29 of the primary translation product, indicating that mature ChIL-18 might consist of 169 amino acids. Bacterially expressed ChIL-18 in which the N-terminal 29 amino acids of the putative precursor molecule were replaced by a histidine tag induced the synthesis of interferon-gamma (IFN-gamma) in cultured primary chicken spleen cells, indicating that the recombinant protein is biologically active. |
| doi_str_mv | 10.1089/10799900050163244 |
| format | Article |
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The encoded protein consists of 198 amino acids and exhibits approximately 30% sequence identity to IL-18 of humans and various others mammals. Sequence comparisons reveals a putative caspase-1 cleavage site at aspartic acid 29 of the primary translation product, indicating that mature ChIL-18 might consist of 169 amino acids. Bacterially expressed ChIL-18 in which the N-terminal 29 amino acids of the putative precursor molecule were replaced by a histidine tag induced the synthesis of interferon-gamma (IFN-gamma) in cultured primary chicken spleen cells, indicating that the recombinant protein is biologically active.</description><identifier>ISSN: 1079-9907</identifier><identifier>EISSN: 1557-7465</identifier><identifier>DOI: 10.1089/10799900050163244</identifier><identifier>PMID: 11054275</identifier><language>eng</language><publisher>United States: Mary Ann Liebert, Inc</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; Chickens ; Cloning, Molecular ; DNA, Complementary - isolation & purification ; g-Interferon ; Horses ; Humans ; Interleukin-18 - genetics ; Interleukin-18 - physiology ; Mice ; Molecular Sequence Data ; Rats ; Recombinant Proteins - pharmacology ; Sequence Homology, Amino Acid ; Swine</subject><ispartof>Journal of interferon & cytokine research, 2000-10, Vol.20 (10), p.879-883</ispartof><rights>Copyright Mary Ann Liebert Inc. 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Bacterially expressed ChIL-18 in which the N-terminal 29 amino acids of the putative precursor molecule were replaced by a histidine tag induced the synthesis of interferon-gamma (IFN-gamma) in cultured primary chicken spleen cells, indicating that the recombinant protein is biologically active.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cattle</subject><subject>Chickens</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary - isolation & purification</subject><subject>g-Interferon</subject><subject>Horses</subject><subject>Humans</subject><subject>Interleukin-18 - genetics</subject><subject>Interleukin-18 - physiology</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Rats</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Sequence Homology, Amino Acid</subject><subject>Swine</subject><issn>1079-9907</issn><issn>1557-7465</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkE1LAzEQhoMotlZ_gBdZPHhbzfdkvZX6CUUvel6yMVvTppu62RX67410QdCDpxmY531hHoROCb4kWBVXBENRFBhjgYlklPM9NCZCQA5civ20p3ueABihoxiXCZSKFodoRAgWnIIYo2tz8zTNjA-NaxZZqLPKBR8Wzmjvt5k2nfu0mXl3ZmWbzDWdbb3tV67JiTpGB7X20Z4Mc4Je725fZg_5_Pn-cTad54ZL3uUgCgam1qoW3BLgBGilJCtqI5WUVOBKqbrizEiutNCVUZhJzAQGKWgFhk3Qxa5304aP3sauXLtorPe6saGPJVAGnCvyL0gAKAUMCTz_BS5D3zbpiZImf0ktxwkiO8i0IcbW1uWmdWvdbkuCy2_95R_9KXM2FPfV2r79JAbf7AsFuHvt</recordid><startdate>20001001</startdate><enddate>20001001</enddate><creator>Schneider, K</creator><creator>Puehler, F</creator><creator>Baeuerle, D</creator><creator>Elvers, S</creator><creator>Staeheli, P</creator><creator>Kaspers, B</creator><creator>Weining, K C</creator><general>Mary Ann Liebert, Inc</general><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>3V.</scope><scope>7QL</scope><scope>7T5</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20001001</creationdate><title>cDNA cloning of biologically active chicken interleukin-18</title><author>Schneider, K ; Puehler, F ; Baeuerle, D ; Elvers, S ; Staeheli, P ; Kaspers, B ; Weining, K C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c464t-75937cfa8f54e174172b8639fc6866250b88fb43c648a5abc803603507652b7c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Cattle</topic><topic>Chickens</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary - isolation & purification</topic><topic>g-Interferon</topic><topic>Horses</topic><topic>Humans</topic><topic>Interleukin-18 - genetics</topic><topic>Interleukin-18 - physiology</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Rats</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Sequence Homology, Amino Acid</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schneider, K</creatorcontrib><creatorcontrib>Puehler, F</creatorcontrib><creatorcontrib>Baeuerle, D</creatorcontrib><creatorcontrib>Elvers, S</creatorcontrib><creatorcontrib>Staeheli, P</creatorcontrib><creatorcontrib>Kaspers, B</creatorcontrib><creatorcontrib>Weining, K C</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of interferon & cytokine research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schneider, K</au><au>Puehler, F</au><au>Baeuerle, D</au><au>Elvers, S</au><au>Staeheli, P</au><au>Kaspers, B</au><au>Weining, K C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>cDNA cloning of biologically active chicken interleukin-18</atitle><jtitle>Journal of interferon & cytokine research</jtitle><addtitle>J Interferon Cytokine Res</addtitle><date>2000-10-01</date><risdate>2000</risdate><volume>20</volume><issue>10</issue><spage>879</spage><epage>883</epage><pages>879-883</pages><issn>1079-9907</issn><eissn>1557-7465</eissn><abstract>By searching a chicken EST database, we identified a cDNA clone that appeared to contain the entire open reading frame (ORF) of chicken interleukin-18 (ChIL-18). The encoded protein consists of 198 amino acids and exhibits approximately 30% sequence identity to IL-18 of humans and various others mammals. Sequence comparisons reveals a putative caspase-1 cleavage site at aspartic acid 29 of the primary translation product, indicating that mature ChIL-18 might consist of 169 amino acids. Bacterially expressed ChIL-18 in which the N-terminal 29 amino acids of the putative precursor molecule were replaced by a histidine tag induced the synthesis of interferon-gamma (IFN-gamma) in cultured primary chicken spleen cells, indicating that the recombinant protein is biologically active.</abstract><cop>United States</cop><pub>Mary Ann Liebert, Inc</pub><pmid>11054275</pmid><doi>10.1089/10799900050163244</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Base Sequence Cattle Chickens Cloning, Molecular DNA, Complementary - isolation & purification g-Interferon Horses Humans Interleukin-18 - genetics Interleukin-18 - physiology Mice Molecular Sequence Data Rats Recombinant Proteins - pharmacology Sequence Homology, Amino Acid Swine |
| title | cDNA cloning of biologically active chicken interleukin-18 |
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