Altering the mechanical properties of self-assembled filaments through engineering of EspA bacterial protein.

Protein-based biomaterials are in high demand due to their high biocompatibility, non-toxicity, and biodegradability. In this study, we explore the bacterial secreted protein A (EspA), which self-assembles into long extracellular filaments, as a potential building block for new protein-based biomaterials. We investigated the morphological and mechanical properties of EspA filaments and how protein engineering can modify them.

The sequence of events of enteropathogenic . 's type III secretion system translocon assembly.

Many bacterial pathogens employ the type III secretion system (T3SS), a specialized complex that transports effector proteins that manipulate various cellular processes. The T3SS forms a translocon pore within the host-cell membrane consisting of two secreted proteins that transition from a soluble state into a transmembrane complex. Still, the exact sequence of events leading to the formation of a membranous functional pore remains uncertain.