Abstract
Perfringolysin O (PFO) is the archetypical pore-forming toxin in the cholesterol-dependent cytolysin (CDC) family, which is implicated in major infections ranging from food poisoning to pneumonia and meningitis. Like other CDCs, transmembrane pores are formed when PFO monomers bind to cholesterol-containing membranes and oligomerize into larger (30-50 subunit) structures.Previous structural studies have shown evidence for intermediate arc- and ring-shaped pre-pores. Here we combine in vitro single-molecule imaging and electrical recordings to track the kinetics of PFO assembly within individual pores formed on droplet-interface bilayers. We observe kinetics consistent with irreversible pore assembly. We also characterize the heterogeneity in pore formation kinetics and observe a range of plasticity events during pore formation. Our data give new insights into the dynamics of the pore formation mechanism of PFO.
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