Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technology and ELISA
The reactivity of monoclonal antibodies (Mabs) raised against a cyclic peptide representing a chimeric V3 loop of HIV-1 gp120 with different peptide analogues was studied with a biosensor system (BIAcore) and by ELISA. In both assays, the Mabs cross-reacted extensively with the V3 regions of differe...
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| Veröffentlicht in: | Journal of immunological methods 1994-12, Vol.176 (2), p.221-234 |
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| container_title | Journal of immunological methods |
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| creator | Richalet-Sécordel, Pascale M. Zeder-Lutz, Gabrielle Plaue, Serge Sommermeyer-Leroux, Ghislaine Van Regenmortel, Marc H.V. |
| description | The reactivity of monoclonal antibodies (Mabs) raised against a cyclic peptide representing a chimeric V3 loop of HIV-1 gp120 with different peptide analogues was studied with a biosensor system (BIAcore) and by ELISA. In both assays, the Mabs cross-reacted extensively with the V3 regions of different HIV-1 strains and recognized the cyclic form of the peptide immunogen better than its linear form. The highest degree of cross-reactivity was observed with peptides that shared a Lys
312 with the chimeric sequence. Dissociation rate constants of ten Mabs measured with the BIAcore with respect to different peptides increased with increasing numbers of substitutions in the flanking regions of the V3 tip sequence Gly Pro Gly Arg. Immobilization of the cyclic peptide on the sensor chip via a thiol group added near the end of the loop structure preserved the conformation of the peptide. In view of the good correlation between the BIAcore and ELISA results, biosensor data should be useful for selecting peptides to be used in diagnostic solid phase assays. |
| doi_str_mv | 10.1016/0022-1759(94)90316-6 |
| format | Article |
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312 with the chimeric sequence. Dissociation rate constants of ten Mabs measured with the BIAcore with respect to different peptides increased with increasing numbers of substitutions in the flanking regions of the V3 tip sequence Gly Pro Gly Arg. Immobilization of the cyclic peptide on the sensor chip via a thiol group added near the end of the loop structure preserved the conformation of the peptide. In view of the good correlation between the BIAcore and ELISA results, biosensor data should be useful for selecting peptides to be used in diagnostic solid phase assays.</description><identifier>ISSN: 0022-1759</identifier><identifier>EISSN: 1872-7905</identifier><identifier>DOI: 10.1016/0022-1759(94)90316-6</identifier><identifier>PMID: 7983380</identifier><identifier>CODEN: JIMMBG</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>AIDS/HIV ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal - biosynthesis ; Antibodies, Monoclonal - immunology ; Binding, Competitive - immunology ; Biological and medical sciences ; Biosensing Techniques ; Biosensor assay ; Cross Reactions - immunology ; ELISA ; Enzyme-Linked Immunosorbent Assay - methods ; Female ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; HIV Antibodies - biosynthesis ; HIV Antibodies - immunology ; HIV Envelope Protein gp120 - immunology ; HIV-1 ; Humans ; Mice ; Mice, Inbred BALB C ; Molecular immunology ; Molecular Sequence Data ; Monoclonal antibody ; Peptide Fragments - immunology ; Recombinant Fusion Proteins - immunology ; Techniques ; Virology</subject><ispartof>Journal of immunological methods, 1994-12, Vol.176 (2), p.221-234</ispartof><rights>1994</rights><rights>1995 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-e144c6c83955e2d124fce9324a5bc979e78d516c2b9db466cc3f62b1db8304bc3</citedby><cites>FETCH-LOGICAL-c386t-e144c6c83955e2d124fce9324a5bc979e78d516c2b9db466cc3f62b1db8304bc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0022-1759(94)90316-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3337549$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7983380$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Richalet-Sécordel, Pascale M.</creatorcontrib><creatorcontrib>Zeder-Lutz, Gabrielle</creatorcontrib><creatorcontrib>Plaue, Serge</creatorcontrib><creatorcontrib>Sommermeyer-Leroux, Ghislaine</creatorcontrib><creatorcontrib>Van Regenmortel, Marc H.V.</creatorcontrib><title>Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technology and ELISA</title><title>Journal of immunological methods</title><addtitle>J Immunol Methods</addtitle><description>The reactivity of monoclonal antibodies (Mabs) raised against a cyclic peptide representing a chimeric V3 loop of HIV-1 gp120 with different peptide analogues was studied with a biosensor system (BIAcore) and by ELISA. In both assays, the Mabs cross-reacted extensively with the V3 regions of different HIV-1 strains and recognized the cyclic form of the peptide immunogen better than its linear form. The highest degree of cross-reactivity was observed with peptides that shared a Lys
312 with the chimeric sequence. Dissociation rate constants of ten Mabs measured with the BIAcore with respect to different peptides increased with increasing numbers of substitutions in the flanking regions of the V3 tip sequence Gly Pro Gly Arg. Immobilization of the cyclic peptide on the sensor chip via a thiol group added near the end of the loop structure preserved the conformation of the peptide. In view of the good correlation between the BIAcore and ELISA results, biosensor data should be useful for selecting peptides to be used in diagnostic solid phase assays.</description><subject>AIDS/HIV</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - biosynthesis</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Binding, Competitive - immunology</subject><subject>Biological and medical sciences</subject><subject>Biosensing Techniques</subject><subject>Biosensor assay</subject><subject>Cross Reactions - immunology</subject><subject>ELISA</subject><subject>Enzyme-Linked Immunosorbent Assay - methods</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>HIV Antibodies - biosynthesis</subject><subject>HIV Antibodies - immunology</subject><subject>HIV Envelope Protein gp120 - immunology</subject><subject>HIV-1</subject><subject>Humans</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Molecular immunology</subject><subject>Molecular Sequence Data</subject><subject>Monoclonal antibody</subject><subject>Peptide Fragments - immunology</subject><subject>Recombinant Fusion Proteins - immunology</subject><subject>Techniques</subject><subject>Virology</subject><issn>0022-1759</issn><issn>1872-7905</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcGKFDEQhhtR1nH1DRRyENFDa9JJpzsXYRlWd2DAg7rXkFSqnUh3Z0wyK_MOPrRpZ5ijp0Dq-3-Kr6rqJaPvGWXyA6VNU7OuVW-VeKcoZ7KWj6oV67um7hRtH1erC_K0epbST0opo5JeVVed6jnv6ar6s44hpTqigewffD6SMJApzAHGMJuRmDl7G5zHRHIghsDOTxg9kHtO9rjP3uGSuNvc14z89nl3-TUlHn4cSjDlQylwxB6J9SHhnEIkGWE3h0IcC-nI7Xbz9eZ59WQwY8IX5_e6-v7p9tv6rt5--bxZ32xr4L3MNTIhQELPVdti41gjBkDFG2FaC6pT2PWuZRIaq5wVUgLwQTaWOdtzKizw6-rNqXcfw6-yYdaTT4DjaGYMh6Q72ctS0BZQnEBYLEUc9D76ycSjZlQvR9CLYb0Y1krof0fQssRenfsPdkJ3CZ2tl_nr89wkMOMQzQw-XTDOedcKVbCPJwyLiwePUSfwOAM6HxGydsH_f4-_DaOkHw</recordid><startdate>19941202</startdate><enddate>19941202</enddate><creator>Richalet-Sécordel, Pascale M.</creator><creator>Zeder-Lutz, Gabrielle</creator><creator>Plaue, Serge</creator><creator>Sommermeyer-Leroux, Ghislaine</creator><creator>Van Regenmortel, Marc H.V.</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>19941202</creationdate><title>Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technology and ELISA</title><author>Richalet-Sécordel, Pascale M. ; Zeder-Lutz, Gabrielle ; Plaue, Serge ; Sommermeyer-Leroux, Ghislaine ; Van Regenmortel, Marc H.V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-e144c6c83955e2d124fce9324a5bc979e78d516c2b9db466cc3f62b1db8304bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>AIDS/HIV</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - biosynthesis</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Binding, Competitive - immunology</topic><topic>Biological and medical sciences</topic><topic>Biosensing Techniques</topic><topic>Biosensor assay</topic><topic>Cross Reactions - immunology</topic><topic>ELISA</topic><topic>Enzyme-Linked Immunosorbent Assay - methods</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>HIV Antibodies - biosynthesis</topic><topic>HIV Antibodies - immunology</topic><topic>HIV Envelope Protein gp120 - immunology</topic><topic>HIV-1</topic><topic>Humans</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Molecular immunology</topic><topic>Molecular Sequence Data</topic><topic>Monoclonal antibody</topic><topic>Peptide Fragments - immunology</topic><topic>Recombinant Fusion Proteins - immunology</topic><topic>Techniques</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Richalet-Sécordel, Pascale M.</creatorcontrib><creatorcontrib>Zeder-Lutz, Gabrielle</creatorcontrib><creatorcontrib>Plaue, Serge</creatorcontrib><creatorcontrib>Sommermeyer-Leroux, Ghislaine</creatorcontrib><creatorcontrib>Van Regenmortel, Marc H.V.</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 immunological methods</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Richalet-Sécordel, Pascale M.</au><au>Zeder-Lutz, Gabrielle</au><au>Plaue, Serge</au><au>Sommermeyer-Leroux, Ghislaine</au><au>Van Regenmortel, Marc H.V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technology and ELISA</atitle><jtitle>Journal of immunological methods</jtitle><addtitle>J Immunol Methods</addtitle><date>1994-12-02</date><risdate>1994</risdate><volume>176</volume><issue>2</issue><spage>221</spage><epage>234</epage><pages>221-234</pages><issn>0022-1759</issn><eissn>1872-7905</eissn><coden>JIMMBG</coden><abstract>The reactivity of monoclonal antibodies (Mabs) raised against a cyclic peptide representing a chimeric V3 loop of HIV-1 gp120 with different peptide analogues was studied with a biosensor system (BIAcore) and by ELISA. In both assays, the Mabs cross-reacted extensively with the V3 regions of different HIV-1 strains and recognized the cyclic form of the peptide immunogen better than its linear form. The highest degree of cross-reactivity was observed with peptides that shared a Lys
312 with the chimeric sequence. Dissociation rate constants of ten Mabs measured with the BIAcore with respect to different peptides increased with increasing numbers of substitutions in the flanking regions of the V3 tip sequence Gly Pro Gly Arg. Immobilization of the cyclic peptide on the sensor chip via a thiol group added near the end of the loop structure preserved the conformation of the peptide. In view of the good correlation between the BIAcore and ELISA results, biosensor data should be useful for selecting peptides to be used in diagnostic solid phase assays.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>7983380</pmid><doi>10.1016/0022-1759(94)90316-6</doi><tpages>14</tpages></addata></record> |
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| ispartof | Journal of immunological methods, 1994-12, Vol.176 (2), p.221-234 |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | AIDS/HIV Amino Acid Sequence Animals Antibodies, Monoclonal - biosynthesis Antibodies, Monoclonal - immunology Binding, Competitive - immunology Biological and medical sciences Biosensing Techniques Biosensor assay Cross Reactions - immunology ELISA Enzyme-Linked Immunosorbent Assay - methods Female Fundamental and applied biological sciences. Psychology Fundamental immunology HIV Antibodies - biosynthesis HIV Antibodies - immunology HIV Envelope Protein gp120 - immunology HIV-1 Humans Mice Mice, Inbred BALB C Molecular immunology Molecular Sequence Data Monoclonal antibody Peptide Fragments - immunology Recombinant Fusion Proteins - immunology Techniques Virology |
| title | Cross-reactivity of monoclonal antibodies to a chimeric V3 peptide of HIV-1 with peptide analogues studied by biosensor technology and ELISA |
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