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- W4283798981 endingPage "167717" @default.
- W4283798981 startingPage "167717" @default.
- W4283798981 abstract "Allosteric proteins transition between 'inactive' and 'active' states. In general, such proteins assume distinct conformational states at the level of secondary, tertiary and/or quaternary structure. Different conformers of an allosteric protein can be antigenically dissimilar and induce antibodies with a highly distinctive specificities and neutralizing functional effects. Here we summarize studies on various functional types of monoclonal antibodies obtained against different allosteric conformers of the mannose-specific bacterial adhesin FimH - the most common cell attachment protein of Escherichia coli and other enterobacterial pathogens. Included are types of antibodies that activate the FimH function via interaction with ligand-induced binding sites or by wedging between domains as well as antibodies that inhibit FimH through orthosteric, parasteric, or novel dynasteric mechanisms. Understanding the molecular mechanism of antibody action against allosteric proteins provides insights on how to design antibodies with a desired functional effect, including those with neutralizing activity against bacterial and viral cell attachment proteins." @default.
- W4283798981 created "2022-07-05" @default.
- W4283798981 creator A5051799220 @default.
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- W4283798981 creator A5064867080 @default.
- W4283798981 creator A5068343952 @default.
- W4283798981 creator A5089097984 @default.
- W4283798981 date "2022-09-01" @default.
- W4283798981 modified "2023-10-18" @default.
- W4283798981 title "Neutralizing Antibodies Against Allosteric Proteins: Insights From a Bacterial Adhesin" @default.
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