Structural Biology of immunoglobulin cleaving peptidase

Antibodies are crucial for pathogen recognition, with immunoglobulin A (IgA) playing a vital role in protecting mucosal surfaces from infectious microorganisms. In response, bacterial species have developed specific enzymes to cleave these antibodies and evade the immune system. Studying these enzymes is essential for understanding pathogenesis, advancing drug discovery, and developing new biomedical and biotechnological tools. We are currently investigating a large, multidomain zinc-dependent metallopeptidase that features multiple accessory domains and exhibits high specificity in cleaving IgA. Our research focuses on elucidating the recognition mechanism of this enzyme using structural biology techniques. By applying these techniques, we aim to map out the precise interactions between the enzyme and IgA, identify critical regions involved in substrate recognition and cleavage, and understand how accessory domains contribute to enzyme function.