Conformational flexibility is a key determinant of the lytic activity of the pore forming protein, Cytolysin A

Abstract

Bacterial pore-forming toxins (PFTs) bind and oligomerize on mammalian cell membranes to form nanopores spanning the lipid bilayer, which causes cell lysis and promotes further infections. Cytolysin A (ClyA), an alpha (α)-PFT, is known to undergo one of the largest conformational changes during its transition from a water-soluble monomeric form to a membrane-embedded dodecameric pore complex. Despite extensive work on ClyA structure and assembly, what features of the protein drive this transformation is poorly understood.