Vibrio cholerae cytolysin: structure–function mechanism of an atypical β-barrel pore- forming toxin

Abstract

β-Barrel pore-forming toxins (β-PFTs) represent a unique class of bacterial protein toxins. β-PFTs act by punching holes in the membrane lipid bilayer of their target host cells. Generalized mechanism of β-PFT mode of action shows unique structural paradigm that involves formation of transmembrane oligomeric β-barrel pores in the target cells. Vibrio cholerae cytolysin (VCC) is a prominent member in the bacterial β-PFT family, and it exhibits common features of the β-PFT mode of action in general. Structure–function mechanism of VCC, however, highlights distinct features that are not commonly documented in the archetypical β-PFT family members. In this review, we present a brief description of our current understanding regarding the mode of action of VCC, in the context of its β-barrel membrane pore formation mechanism.