Determination of the Rituximab Binding Site to the CD20 Epitope Using SPOT Synthesis and Surface Plasmon Resonance Analyses
Antibodies not only play a major role in clinical diagnostics and biopharmaceutical analysis but also are a class of drugs that are regularly used to treat numerous diseases. The identification of antibody–epitope binding sites is then of great interest to many emerging medical and bioanalytical app...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2021-05, Vol.93 (17), p.6865-6872 |
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| creator | Bar, Laure Nguyen, Christophe Galibert, Mathieu Santos-Schneider, Francisco Aldrian, Gudrun Dejeu, Jérôme Lartia, Rémy Coche-Guérente, Liliane Molina, Franck Boturyn, Didier |
| description | Antibodies not only play a major role in clinical diagnostics and biopharmaceutical analysis but also are a class of drugs that are regularly used to treat numerous diseases. The identification of antibody–epitope binding sites is then of great interest to many emerging medical and bioanalytical applications, particularly to design monoclonal antibodies (mAb) mimics taking advantage of amino acid residues involved in the binding. Among relevant antibodies, the monoclonal antibody rituximab has received significant attention as it is exploited to treat several cancers including non-Hodgkin’s lymphoma and chronic lymphocytic leukemia, as well as some autoimmune disorders such as rheumatoid arthritis. The binding of rituximab to the targeted cells occurs via the recognition of the CD20 epitope. A crystallographic study has shown that the binding area, named paratope, is located at the surface of rituximab. Combining the SPOT method and the complementary surface plasmon resonance technique allowed us to detect an extended recognition domain buried in the pocket of the rituximab Fab formed by four β-sheets. More generally, the present study offers a comprehensive approach to identify antibody–epitope binding sites. |
| doi_str_mv | 10.1021/acs.analchem.1c00960 |
| format | Article |
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Chem</addtitle><description>Antibodies not only play a major role in clinical diagnostics and biopharmaceutical analysis but also are a class of drugs that are regularly used to treat numerous diseases. The identification of antibody–epitope binding sites is then of great interest to many emerging medical and bioanalytical applications, particularly to design monoclonal antibodies (mAb) mimics taking advantage of amino acid residues involved in the binding. Among relevant antibodies, the monoclonal antibody rituximab has received significant attention as it is exploited to treat several cancers including non-Hodgkin’s lymphoma and chronic lymphocytic leukemia, as well as some autoimmune disorders such as rheumatoid arthritis. The binding of rituximab to the targeted cells occurs via the recognition of the CD20 epitope. A crystallographic study has shown that the binding area, named paratope, is located at the surface of rituximab. Combining the SPOT method and the complementary surface plasmon resonance technique allowed us to detect an extended recognition domain buried in the pocket of the rituximab Fab formed by four β-sheets. 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Chem</addtitle><date>2021-05-04</date><risdate>2021</risdate><volume>93</volume><issue>17</issue><spage>6865</spage><epage>6872</epage><pages>6865-6872</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><abstract>Antibodies not only play a major role in clinical diagnostics and biopharmaceutical analysis but also are a class of drugs that are regularly used to treat numerous diseases. The identification of antibody–epitope binding sites is then of great interest to many emerging medical and bioanalytical applications, particularly to design monoclonal antibodies (mAb) mimics taking advantage of amino acid residues involved in the binding. Among relevant antibodies, the monoclonal antibody rituximab has received significant attention as it is exploited to treat several cancers including non-Hodgkin’s lymphoma and chronic lymphocytic leukemia, as well as some autoimmune disorders such as rheumatoid arthritis. The binding of rituximab to the targeted cells occurs via the recognition of the CD20 epitope. A crystallographic study has shown that the binding area, named paratope, is located at the surface of rituximab. Combining the SPOT method and the complementary surface plasmon resonance technique allowed us to detect an extended recognition domain buried in the pocket of the rituximab Fab formed by four β-sheets. 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| subjects | Amino acids Analytical chemistry Antibodies Arthritis Autoimmune diseases Binding sites Biopharmaceuticals CD20 antigen Chemical Sciences Chemistry Chemistry, Analytical Chronic lymphocytic leukemia Crystallography Epitopes Immunotherapy Leukemia Lymphatic leukemia Lymphoma Monoclonal antibodies Non-Hodgkin's lymphoma Physical Sciences Recognition Resonance Rheumatoid arthritis Rituximab Science & Technology Surface plasmon resonance Targeted cancer therapy |
| title | Determination of the Rituximab Binding Site to the CD20 Epitope Using SPOT Synthesis and Surface Plasmon Resonance Analyses |
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