Literature Seminar

Listeriolysin O (LLO) is a toxic protein secreted by the pathogen, Listeria monocytogenes, which has spurred several food-borne outbreaks in recent years. LLO mediates the entryway of Listeria into host tissues by assembling transmembrane pores and therefore, LLO is an important target for the development of antimicrobial defenses to combat the spread of Listeria. Although studies upon homologous pore-forming toxins have aided in identifying the mechanism by which LLO forms these pores, the nature of the structural change that induces the pre-pore to pore transition in the oligomeric LLO assembly is not currently known. Furthermore, it is thought that the cell membrane plays an integral role in pore formation, but further investigation is needed to understand how the properties of membranes enable or hinder the development of pores and how LLO binding impacts the membrane lipid dynamics. This talk will focus on a recent publication that aimed to uncover the conformational states of the LLO protein and the impact of pore development on lipid diffusion within an artificial membrane surface using a combination of experimental and computational methods.