Neutralizing Antibodies Against Allosteric Proteins: Insights From a Bacterial Adhesin.

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 w

SUBMITTER: Sokurenko EV 

PROVIDER: S-EPMC9398984 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature