Protein aggregation is a consequence of the dormancy-inducing membrane toxin TisB in Escherichia coli

Protein aggregates occur in all living cells due to misfolding of proteins. In bacteria, protein aggregation is associated with cellular inactivity, which is related to dormancy and tolerance to stressful conditions, including the exposure to antibiotics. In Escherichia coli, the membrane toxin TisB is an important factor for dormancy and antibiotic tolerance upon DNA damage mediated by the fluoroquinolone antibiotic ciprofloxacin. Here, we show that TisB provokes protein aggregation in response to ciprofloxacin. The stress response and TisB-dependent protein aggregates are analyzed by LC-MS.