Bacterial protein listeriolysin O induces nonmonotonic dynamics because of lipid ejection and crowding.

ABSTRACT: Membrane-bound protein complexes involving pore forming toxins (PFTs) released by virulent bacteria are known to form transmembrane pores leading to host cell lysis. Developing alternative strategies against PFT mediated bacterial virulence factors requires an understanding of the cellular membrane response. However, membrane disruption and related lipid reorganization events during attack by PFTs remain largely unexplored. We report counterintuitive and nonmonotonic variations in lipid diffusion, measured using confocal fluorescence correlation spectroscopy, due to interplay of lipid ejection and crowding by membrane-bound oligomers of a prototypical cholesterol-dependent cytolysin, listeriolysin O (LLO). The observed dynamical crossover is correlated with concentration dependent transiti

SUBMITTER: Ilangumaran Ponmalar I 

PROVIDER: S-EPMC8390966 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature