Selection and Characterization of Recombinant Dromedary Antiovalbumin Antibody Fragments That Do Not Cross-React with Ovalbumin-Related Protein X: Use for Immunoaffinity
Ovalbumin-related protein X (OVAX) and ovalbumin are two very close ovalbumin-related serpins. As primary data on OVAX remain recent, information about possible cross-reaction of available antiovalbumin antibodies with OVAX is still missing. Using labeled purified OVAX and dot ligand blotting, we id...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2012-12, Vol.60 (49), p.12157-12163 |
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| container_end_page | 12163 |
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| container_issue | 49 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Bruneau, Gilles Anouassi, Abdelhaq Réhault-Godbert, Sophie Canépa, Sylvie Blanc, Michel R |
| description | Ovalbumin-related protein X (OVAX) and ovalbumin are two very close ovalbumin-related serpins. As primary data on OVAX remain recent, information about possible cross-reaction of available antiovalbumin antibodies with OVAX is still missing. Using labeled purified OVAX and dot ligand blotting, we identified 49 recombinant dromedary antiovalbumin single domain antibody (sdAb) fragments that were unable to bind OVAX. Discrimination between OVAX and ovalbumin was confirmed for two of the corresponding sdAb fragments by surface plasmon resonance and Western ligand blotting (WLB) characterizations. Furthermore, they were covalently linked to Sepharose and used as an affinity matrix for ovalbumin depletion. At least 90% of the original ovalbumin was eliminated from the allantoic fluid of 14 day old chicken embryo in one step. These sdAb fragments, which bind ovalbumin with nanomolar affinity, should also contribute to a better characterization of ovalbumin preparations. |
| doi_str_mv | 10.1021/jf303053t |
| format | Article |
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As primary data on OVAX remain recent, information about possible cross-reaction of available antiovalbumin antibodies with OVAX is still missing. Using labeled purified OVAX and dot ligand blotting, we identified 49 recombinant dromedary antiovalbumin single domain antibody (sdAb) fragments that were unable to bind OVAX. Discrimination between OVAX and ovalbumin was confirmed for two of the corresponding sdAb fragments by surface plasmon resonance and Western ligand blotting (WLB) characterizations. Furthermore, they were covalently linked to Sepharose and used as an affinity matrix for ovalbumin depletion. At least 90% of the original ovalbumin was eliminated from the allantoic fluid of 14 day old chicken embryo in one step. These sdAb fragments, which bind ovalbumin with nanomolar affinity, should also contribute to a better characterization of ovalbumin preparations.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf303053t</identifier><identifier>PMID: 23181906</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>agarose ; allantoic fluid ; Animals ; Antibodies - genetics ; Antibodies - immunology ; Antibodies - metabolism ; Biological and medical sciences ; Blotting, Western ; Camelus - immunology ; Chick Embryo ; chickens ; cross reaction ; Cross Reactions - genetics ; Cross Reactions - immunology ; dromedaries ; Food industries ; Fundamental and applied biological sciences. Psychology ; Iodine Radioisotopes - analysis ; Life Sciences ; Other ; ovalbumin ; Ovalbumin - immunology ; Ovalbumin - metabolism ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Serpins - immunology ; Surface Plasmon Resonance</subject><ispartof>Journal of agricultural and food chemistry, 2012-12, Vol.60 (49), p.12157-12163</ispartof><rights>Copyright © 2012 American Chemical Society</rights><rights>2014 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-a363t-58c618edaf78934a9a4bf723c304295a16e1188884e6c9a8d79f469ffee28aa83</cites><orcidid>0000-0003-2800-3417 ; 0009-0001-5125-2588</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf303053t$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf303053t$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,315,781,785,886,2766,27078,27926,27927,56740,56790</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26721369$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23181906$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01129680$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Bruneau, Gilles</creatorcontrib><creatorcontrib>Anouassi, Abdelhaq</creatorcontrib><creatorcontrib>Réhault-Godbert, Sophie</creatorcontrib><creatorcontrib>Canépa, Sylvie</creatorcontrib><creatorcontrib>Blanc, Michel R</creatorcontrib><title>Selection and Characterization of Recombinant Dromedary Antiovalbumin Antibody Fragments That Do Not Cross-React with Ovalbumin-Related Protein X: Use for Immunoaffinity</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Ovalbumin-related protein X (OVAX) and ovalbumin are two very close ovalbumin-related serpins. As primary data on OVAX remain recent, information about possible cross-reaction of available antiovalbumin antibodies with OVAX is still missing. Using labeled purified OVAX and dot ligand blotting, we identified 49 recombinant dromedary antiovalbumin single domain antibody (sdAb) fragments that were unable to bind OVAX. Discrimination between OVAX and ovalbumin was confirmed for two of the corresponding sdAb fragments by surface plasmon resonance and Western ligand blotting (WLB) characterizations. Furthermore, they were covalently linked to Sepharose and used as an affinity matrix for ovalbumin depletion. At least 90% of the original ovalbumin was eliminated from the allantoic fluid of 14 day old chicken embryo in one step. These sdAb fragments, which bind ovalbumin with nanomolar affinity, should also contribute to a better characterization of ovalbumin preparations.</description><subject>agarose</subject><subject>allantoic fluid</subject><subject>Animals</subject><subject>Antibodies - genetics</subject><subject>Antibodies - immunology</subject><subject>Antibodies - metabolism</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Camelus - immunology</subject><subject>Chick Embryo</subject><subject>chickens</subject><subject>cross reaction</subject><subject>Cross Reactions - genetics</subject><subject>Cross Reactions - immunology</subject><subject>dromedaries</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Iodine Radioisotopes - analysis</subject><subject>Life Sciences</subject><subject>Other</subject><subject>ovalbumin</subject><subject>Ovalbumin - immunology</subject><subject>Ovalbumin - metabolism</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - immunology</subject><subject>Serpins - immunology</subject><subject>Surface Plasmon Resonance</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkc9uEzEQxlcIREPhwAuAL0hwWPDY-8fLLQqUVoooahuJ22rWsRtHu3axvUXhjXhLnCZNLvgy8jc_fxp_k2WvgX4EyuDTWnPKacnjk2wCJaN5CSCeZhOamrkoKzjJXoSwppSKsqbPsxPGQUBDq0n291r1SkbjLEG7JLMVepRRefMHH0SnyZWSbuiMRRvJF-8GtUS_IVOb-vfYd-Ng7MOtc8sNOfN4OygbA7lZYeId-e4imXkXQn6lkjX5beKKXD6-TGKPUS3JD--iSk4_P5NFUEQ7Ty6GYbQOtTbWxM3L7JnGPqhX-3qaLc6-3szO8_nlt4vZdJ4jr3jMSyErEGlGXYuGF9hg0emacclpwZoSoVIpnHQKVckGxbJudFE1WivFBKLgp9mHne8K-_bOmyH9tnVo2vPpvN1qFIA1laD3kNj3O_bOu1-jCrEdTJCq79EqN4YWGBdAuRBwtJXbLLzSB2-g7XaL7WGLiX2ztx27FPeBfFxbAt7tAQwSe-3RShOOXFUz4FWTuLc7TqNr8dYnZnHNKBSUQiq0PjqhDO3ajd6mbP8z0j_av7sJ</recordid><startdate>20121212</startdate><enddate>20121212</enddate><creator>Bruneau, Gilles</creator><creator>Anouassi, Abdelhaq</creator><creator>Réhault-Godbert, Sophie</creator><creator>Canépa, Sylvie</creator><creator>Blanc, Michel R</creator><general>American Chemical Society</general><scope>FBQ</scope><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><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-2800-3417</orcidid><orcidid>https://orcid.org/0009-0001-5125-2588</orcidid></search><sort><creationdate>20121212</creationdate><title>Selection and Characterization of Recombinant Dromedary Antiovalbumin Antibody Fragments That Do Not Cross-React with Ovalbumin-Related Protein X: Use for Immunoaffinity</title><author>Bruneau, Gilles ; Anouassi, Abdelhaq ; Réhault-Godbert, Sophie ; Canépa, Sylvie ; Blanc, Michel R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a363t-58c618edaf78934a9a4bf723c304295a16e1188884e6c9a8d79f469ffee28aa83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>agarose</topic><topic>allantoic fluid</topic><topic>Animals</topic><topic>Antibodies - genetics</topic><topic>Antibodies - immunology</topic><topic>Antibodies - metabolism</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Camelus - immunology</topic><topic>Chick Embryo</topic><topic>chickens</topic><topic>cross reaction</topic><topic>Cross Reactions - genetics</topic><topic>Cross Reactions - immunology</topic><topic>dromedaries</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Iodine Radioisotopes - analysis</topic><topic>Life Sciences</topic><topic>Other</topic><topic>ovalbumin</topic><topic>Ovalbumin - immunology</topic><topic>Ovalbumin - metabolism</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - immunology</topic><topic>Serpins - immunology</topic><topic>Surface Plasmon Resonance</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bruneau, Gilles</creatorcontrib><creatorcontrib>Anouassi, Abdelhaq</creatorcontrib><creatorcontrib>Réhault-Godbert, Sophie</creatorcontrib><creatorcontrib>Canépa, Sylvie</creatorcontrib><creatorcontrib>Blanc, Michel R</creatorcontrib><collection>AGRIS</collection><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><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bruneau, Gilles</au><au>Anouassi, Abdelhaq</au><au>Réhault-Godbert, Sophie</au><au>Canépa, Sylvie</au><au>Blanc, Michel R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Selection and Characterization of Recombinant Dromedary Antiovalbumin Antibody Fragments That Do Not Cross-React with Ovalbumin-Related Protein X: Use for Immunoaffinity</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2012-12-12</date><risdate>2012</risdate><volume>60</volume><issue>49</issue><spage>12157</spage><epage>12163</epage><pages>12157-12163</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Ovalbumin-related protein X (OVAX) and ovalbumin are two very close ovalbumin-related serpins. As primary data on OVAX remain recent, information about possible cross-reaction of available antiovalbumin antibodies with OVAX is still missing. Using labeled purified OVAX and dot ligand blotting, we identified 49 recombinant dromedary antiovalbumin single domain antibody (sdAb) fragments that were unable to bind OVAX. Discrimination between OVAX and ovalbumin was confirmed for two of the corresponding sdAb fragments by surface plasmon resonance and Western ligand blotting (WLB) characterizations. Furthermore, they were covalently linked to Sepharose and used as an affinity matrix for ovalbumin depletion. At least 90% of the original ovalbumin was eliminated from the allantoic fluid of 14 day old chicken embryo in one step. These sdAb fragments, which bind ovalbumin with nanomolar affinity, should also contribute to a better characterization of ovalbumin preparations.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>23181906</pmid><doi>10.1021/jf303053t</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0003-2800-3417</orcidid><orcidid>https://orcid.org/0009-0001-5125-2588</orcidid></addata></record> |
| fulltext | fulltext |
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| ispartof | Journal of agricultural and food chemistry, 2012-12, Vol.60 (49), p.12157-12163 |
| issn | 0021-8561 1520-5118 |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | agarose allantoic fluid Animals Antibodies - genetics Antibodies - immunology Antibodies - metabolism Biological and medical sciences Blotting, Western Camelus - immunology Chick Embryo chickens cross reaction Cross Reactions - genetics Cross Reactions - immunology dromedaries Food industries Fundamental and applied biological sciences. Psychology Iodine Radioisotopes - analysis Life Sciences Other ovalbumin Ovalbumin - immunology Ovalbumin - metabolism Recombinant Proteins - genetics Recombinant Proteins - immunology Serpins - immunology Surface Plasmon Resonance |
| title | Selection and Characterization of Recombinant Dromedary Antiovalbumin Antibody Fragments That Do Not Cross-React with Ovalbumin-Related Protein X: Use for Immunoaffinity |
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