Efficient CD4 binding and immunosuppressive properties of the 13B8.2 monoclonal antibody are displayed by its CDR-H1-derived peptide CB1
A systematic exploration of the V H2/V κ12–13 variable domains of the anti-CD4 monoclonal antibody (mAb) 13B8.2 was performed by the Spot method to screen for paratope-derived peptides (PDPs) demonstrating CD4 binding ability. Nine peptides, named CB1 to CB9, were identified, synthesized in a cyclic...
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| Veröffentlicht in: | FEBS letters 2001-11, Vol.508 (1), p.67-74 |
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| creator | Bès, Cédric Briant-Longuet, Laurence Cerruti, Martine DeBerardinis, Piergiuseppe Devauchelle, Gérard Devaux, Christian Granier, Claude Chardès, Thierry |
| description | A systematic exploration of the V
H2/V
κ12–13 variable domains of the anti-CD4 monoclonal antibody (mAb) 13B8.2 was performed by the Spot method to screen for paratope-derived peptides (PDPs) demonstrating CD4 binding ability. Nine peptides, named CB1 to CB9, were identified, synthesized in a cyclic and soluble form and tested for binding to recombinant soluble CD4. Among them, CB1, CB2 and CB8 showed high anti-CD4 activity. Competition studies for CD4 binding indicated that PDPs CB1, CB8, and the parental mAb 13B8.2 recognized the same complementarity determining region (CDR)3-
like loop region. PDP CB1 was shown to mimic the biological properties of 13B8.2 mAb in two independent cellular assays, demonstrating inhibitory activities in the micromolar range on antigen presentation and human immunodeficiency virus promoter activation. Our results indicate that the bioactive CDR-H1 PDP CB1 has retained a significant part of the parental 13B8.2 mAb properties and might be a lead for the design of anti-CD4 peptidomimetics of clinical interest. |
| doi_str_mv | 10.1016/S0014-5793(01)03036-8 |
| format | Article |
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H2/V
κ12–13 variable domains of the anti-CD4 monoclonal antibody (mAb) 13B8.2 was performed by the Spot method to screen for paratope-derived peptides (PDPs) demonstrating CD4 binding ability. Nine peptides, named CB1 to CB9, were identified, synthesized in a cyclic and soluble form and tested for binding to recombinant soluble CD4. Among them, CB1, CB2 and CB8 showed high anti-CD4 activity. Competition studies for CD4 binding indicated that PDPs CB1, CB8, and the parental mAb 13B8.2 recognized the same complementarity determining region (CDR)3-
like loop region. PDP CB1 was shown to mimic the biological properties of 13B8.2 mAb in two independent cellular assays, demonstrating inhibitory activities in the micromolar range on antigen presentation and human immunodeficiency virus promoter activation. Our results indicate that the bioactive CDR-H1 PDP CB1 has retained a significant part of the parental 13B8.2 mAb properties and might be a lead for the design of anti-CD4 peptidomimetics of clinical interest.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(01)03036-8</identifier><identifier>PMID: 11707270</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Anti-HIV Agents - immunology ; Anti-HIV Agents - metabolism ; Anti-HIV Agents - pharmacology ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal - metabolism ; Antibodies, Monoclonal - pharmacology ; Antibody ; Antigen Presentation ; CD4 ; CD4 Antigens - immunology ; CD4 Antigens - metabolism ; Cell Line ; Cellular Biology ; Complementarity determining region 3- like loop ; Enzyme-Linked Immunosorbent Assay ; Epitopes ; Gene Expression Regulation ; Genes, Reporter ; HIV-1 - metabolism ; Human immunodeficiency virus ; Humans ; Immunoglobulin Variable Region ; Immunosuppressive Agents - metabolism ; Immunosuppressive Agents - pharmacology ; Interleukin-2 - metabolism ; Life Sciences ; Mice ; Molecular Mimicry ; Molecular Sequence Data ; Paratope-derived peptide ; Peptide Fragments - immunology ; Peptide Fragments - metabolism ; Promoter Regions, Genetic ; Protein Binding ; Recombinant Fusion Proteins - metabolism ; T cell activation</subject><ispartof>FEBS letters, 2001-11, Vol.508 (1), p.67-74</ispartof><rights>2001 Federation of European Biochemical Societies</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0002-1886-7409 ; 0000-0002-1995-3501</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(01)03036-8$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,777,781,882,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11707270$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02671665$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Bès, Cédric</creatorcontrib><creatorcontrib>Briant-Longuet, Laurence</creatorcontrib><creatorcontrib>Cerruti, Martine</creatorcontrib><creatorcontrib>DeBerardinis, Piergiuseppe</creatorcontrib><creatorcontrib>Devauchelle, Gérard</creatorcontrib><creatorcontrib>Devaux, Christian</creatorcontrib><creatorcontrib>Granier, Claude</creatorcontrib><creatorcontrib>Chardès, Thierry</creatorcontrib><title>Efficient CD4 binding and immunosuppressive properties of the 13B8.2 monoclonal antibody are displayed by its CDR-H1-derived peptide CB1</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>A systematic exploration of the V
H2/V
κ12–13 variable domains of the anti-CD4 monoclonal antibody (mAb) 13B8.2 was performed by the Spot method to screen for paratope-derived peptides (PDPs) demonstrating CD4 binding ability. Nine peptides, named CB1 to CB9, were identified, synthesized in a cyclic and soluble form and tested for binding to recombinant soluble CD4. Among them, CB1, CB2 and CB8 showed high anti-CD4 activity. Competition studies for CD4 binding indicated that PDPs CB1, CB8, and the parental mAb 13B8.2 recognized the same complementarity determining region (CDR)3-
like loop region. PDP CB1 was shown to mimic the biological properties of 13B8.2 mAb in two independent cellular assays, demonstrating inhibitory activities in the micromolar range on antigen presentation and human immunodeficiency virus promoter activation. Our results indicate that the bioactive CDR-H1 PDP CB1 has retained a significant part of the parental 13B8.2 mAb properties and might be a lead for the design of anti-CD4 peptidomimetics of clinical interest.</description><subject>Animals</subject><subject>Anti-HIV Agents - immunology</subject><subject>Anti-HIV Agents - metabolism</subject><subject>Anti-HIV Agents - pharmacology</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Antibodies, Monoclonal - pharmacology</subject><subject>Antibody</subject><subject>Antigen Presentation</subject><subject>CD4</subject><subject>CD4 Antigens - immunology</subject><subject>CD4 Antigens - metabolism</subject><subject>Cell Line</subject><subject>Cellular Biology</subject><subject>Complementarity determining region 3- like loop</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Epitopes</subject><subject>Gene Expression Regulation</subject><subject>Genes, Reporter</subject><subject>HIV-1 - metabolism</subject><subject>Human immunodeficiency virus</subject><subject>Humans</subject><subject>Immunoglobulin Variable Region</subject><subject>Immunosuppressive Agents - metabolism</subject><subject>Immunosuppressive Agents - pharmacology</subject><subject>Interleukin-2 - metabolism</subject><subject>Life Sciences</subject><subject>Mice</subject><subject>Molecular Mimicry</subject><subject>Molecular Sequence Data</subject><subject>Paratope-derived peptide</subject><subject>Peptide Fragments - immunology</subject><subject>Peptide Fragments - metabolism</subject><subject>Promoter Regions, Genetic</subject><subject>Protein Binding</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>T cell activation</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kcFu1DAQhi0EotvCI4B8QvSQ4rGdODmhdtuySCsh0XK2nHhMjZI42MlK-wY8Nt5u29NoRt_8o39-Qj4AuwAG1Zc7xkAWpWrEZwbnTDBRFfUrsoJaiULIqn5NVi_ICTlN6Q_LfQ3NW3ICoJjiiq3IvxvnfOdxnOn6WtLWj9aPv6kZLfXDsIwhLdMUMSW_QzrFMGGcPSYaHJ0fkIK4qi84HcIYuj6Mps-bs2-D3VMTkVqfpt7s0dJ2T_2c8o2fxQYKizHrWTrhNHuLdH0F78gbZ_qE75_qGfl1e3O_3hTbH9--ry-3BfJGzYV0TtrGcqhUxWq0jZBl1xhloC7bEiw6JSx2KFlbtlwZJ5kDJ2RnZcmrloszcn7UfTC9nqIfTNzrYLzeXG71YcZ4paCqyh1k9tORzcb_LphmPfjUYd-bEcOStOJcCaZUBj8-gUs7oH3Rff5zBr4eAczWdh6jToend2h9xG7WNngNTB-S1Y_J6kNsmoF-TFbX4j-kFpO6</recordid><startdate>20011109</startdate><enddate>20011109</enddate><creator>Bès, Cédric</creator><creator>Briant-Longuet, Laurence</creator><creator>Cerruti, Martine</creator><creator>DeBerardinis, Piergiuseppe</creator><creator>Devauchelle, Gérard</creator><creator>Devaux, Christian</creator><creator>Granier, Claude</creator><creator>Chardès, Thierry</creator><general>Elsevier B.V</general><general>Wiley</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-1886-7409</orcidid><orcidid>https://orcid.org/0000-0002-1995-3501</orcidid></search><sort><creationdate>20011109</creationdate><title>Efficient CD4 binding and immunosuppressive properties of the 13B8.2 monoclonal antibody are displayed by its CDR-H1-derived peptide CB1</title><author>Bès, Cédric ; Briant-Longuet, Laurence ; Cerruti, Martine ; DeBerardinis, Piergiuseppe ; Devauchelle, Gérard ; Devaux, Christian ; Granier, Claude ; Chardès, Thierry</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e297t-4ff4d9d2167608ed9345c9a7a185b51def73dece40b5b27af40f1f34cd4526b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Animals</topic><topic>Anti-HIV Agents - immunology</topic><topic>Anti-HIV Agents - metabolism</topic><topic>Anti-HIV Agents - pharmacology</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Monoclonal - metabolism</topic><topic>Antibodies, Monoclonal - pharmacology</topic><topic>Antibody</topic><topic>Antigen Presentation</topic><topic>CD4</topic><topic>CD4 Antigens - immunology</topic><topic>CD4 Antigens - metabolism</topic><topic>Cell Line</topic><topic>Cellular Biology</topic><topic>Complementarity determining region 3- like loop</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Epitopes</topic><topic>Gene Expression Regulation</topic><topic>Genes, Reporter</topic><topic>HIV-1 - metabolism</topic><topic>Human immunodeficiency virus</topic><topic>Humans</topic><topic>Immunoglobulin Variable Region</topic><topic>Immunosuppressive Agents - metabolism</topic><topic>Immunosuppressive Agents - pharmacology</topic><topic>Interleukin-2 - metabolism</topic><topic>Life Sciences</topic><topic>Mice</topic><topic>Molecular Mimicry</topic><topic>Molecular Sequence Data</topic><topic>Paratope-derived peptide</topic><topic>Peptide Fragments - immunology</topic><topic>Peptide Fragments - metabolism</topic><topic>Promoter Regions, Genetic</topic><topic>Protein Binding</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>T cell activation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bès, Cédric</creatorcontrib><creatorcontrib>Briant-Longuet, Laurence</creatorcontrib><creatorcontrib>Cerruti, Martine</creatorcontrib><creatorcontrib>DeBerardinis, Piergiuseppe</creatorcontrib><creatorcontrib>Devauchelle, Gérard</creatorcontrib><creatorcontrib>Devaux, Christian</creatorcontrib><creatorcontrib>Granier, Claude</creatorcontrib><creatorcontrib>Chardès, Thierry</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bès, Cédric</au><au>Briant-Longuet, Laurence</au><au>Cerruti, Martine</au><au>DeBerardinis, Piergiuseppe</au><au>Devauchelle, Gérard</au><au>Devaux, Christian</au><au>Granier, Claude</au><au>Chardès, Thierry</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Efficient CD4 binding and immunosuppressive properties of the 13B8.2 monoclonal antibody are displayed by its CDR-H1-derived peptide CB1</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2001-11-09</date><risdate>2001</risdate><volume>508</volume><issue>1</issue><spage>67</spage><epage>74</epage><pages>67-74</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>A systematic exploration of the V
H2/V
κ12–13 variable domains of the anti-CD4 monoclonal antibody (mAb) 13B8.2 was performed by the Spot method to screen for paratope-derived peptides (PDPs) demonstrating CD4 binding ability. Nine peptides, named CB1 to CB9, were identified, synthesized in a cyclic and soluble form and tested for binding to recombinant soluble CD4. Among them, CB1, CB2 and CB8 showed high anti-CD4 activity. Competition studies for CD4 binding indicated that PDPs CB1, CB8, and the parental mAb 13B8.2 recognized the same complementarity determining region (CDR)3-
like loop region. PDP CB1 was shown to mimic the biological properties of 13B8.2 mAb in two independent cellular assays, demonstrating inhibitory activities in the micromolar range on antigen presentation and human immunodeficiency virus promoter activation. Our results indicate that the bioactive CDR-H1 PDP CB1 has retained a significant part of the parental 13B8.2 mAb properties and might be a lead for the design of anti-CD4 peptidomimetics of clinical interest.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>11707270</pmid><doi>10.1016/S0014-5793(01)03036-8</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-1886-7409</orcidid><orcidid>https://orcid.org/0000-0002-1995-3501</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 2001-11, Vol.508 (1), p.67-74 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Anti-HIV Agents - immunology Anti-HIV Agents - metabolism Anti-HIV Agents - pharmacology Antibodies, Monoclonal - immunology Antibodies, Monoclonal - metabolism Antibodies, Monoclonal - pharmacology Antibody Antigen Presentation CD4 CD4 Antigens - immunology CD4 Antigens - metabolism Cell Line Cellular Biology Complementarity determining region 3- like loop Enzyme-Linked Immunosorbent Assay Epitopes Gene Expression Regulation Genes, Reporter HIV-1 - metabolism Human immunodeficiency virus Humans Immunoglobulin Variable Region Immunosuppressive Agents - metabolism Immunosuppressive Agents - pharmacology Interleukin-2 - metabolism Life Sciences Mice Molecular Mimicry Molecular Sequence Data Paratope-derived peptide Peptide Fragments - immunology Peptide Fragments - metabolism Promoter Regions, Genetic Protein Binding Recombinant Fusion Proteins - metabolism T cell activation |
| title | Efficient CD4 binding and immunosuppressive properties of the 13B8.2 monoclonal antibody are displayed by its CDR-H1-derived peptide CB1 |
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