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
Hauptverfasser:	Bès, Cédric, Briant-Longuet, Laurence, Cerruti, Martine, DeBerardinis, Piergiuseppe, Devauchelle, Gérard, Devaux, Christian, Granier, Claude, Chardès, Thierry
Format:	Artikel
Sprache:	eng
Schlagworte:	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
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