Ubiquitins play an important role in bacterial infections because they are important regulators of the immune response. Could these proteins be a new approach for therapies? Prof. Schlüter is investigating this question. In his RESIST project B12, he and his team are investigating the structures and functions of deubiquitinases – the enzymes that attach ubiquitins to proteins or cleave them from proteins. “A therapeutic influence on ubiquitination may make it possible to treat infections beyond antibiotics,” says Prof. Schlüter. Therapeutics could alter ubiquitination and thus strengthen the antibacterial immune response.
Prof. Schlüter’s team, in collaboration with Prof. Werfel and PD Dr. Rösner, also investigated the role of ubiquitin in patients with atopic dermatitis and a Staphylococcus aureus infection. In atopic dermatitis (AD), the skin is often colonized by these bacteria, which contributes to the severity of the disease. The researchers found that the deubiquitinating enzyme CYLD is produced at higher levels in the macrophages of patients. This affects the macrophages to such an extent that they are less able to control the bacteria. The research team published the results Ablation of the deubiquitinating enzyme cylindromatosis (CYLD) augments STAT1-mediated M1 macrophage polarization and fosters Staphylococcus aureus control in the journal Frontiers in Immunology.
The figure shows Staphylococcus aureus (ultrathin section in a transmission electron microscope).
Source: : P. Kaiser. Coloring: A. Schnartendorff/RKI