Visualizing the Domino-Like Prepore-to-Pore Transition of Streptolysin O by High-Speed AFM.

ABSTRACT: Pore-forming proteins (PFPs) are produced by various organisms, including pathogenic bacteria, and form pores within the target cell membrane. Streptolysin O (SLO) is a PFP produced by Streptococcus pyogenes and forms high-order oligomers on the membrane surface. In this prepore state, multiple α-helices in domain 3 of each subunit exist as unfolded structures and transiently interact with each other. They subsequently transition into transmembrane β-hairpins (TMHs) and form pores with diameters of 20-30 nm. However, in this pore formation process, the trigger of the transition in a subunit and collaboration between subunits remains elusive. Here, I observed the dynamic pore formation process using high-speed atomic force microscopy. During the oligomer transition process, each subunit was

SUBMITTER: Ariyama H 

PROVIDER: S-EPMC9884259 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature