Cytolysin refers to the substance secreted by microorganisms, plants or animals that is specifically toxic to individual cells,[1][2] in many cases causing their dissolution through lysis.
For instance, the cytolysins responsible for the destruction of red blood cells, thereby liberating hemoglobins, are named hemolysins, and so on.
Hemolysin is also used by certain bacteria, such as Listeria monocytogenes, to disrupt the phagosome membrane of macrophages and escape into the cytoplasm of the cell.
[4] The first kind of cytolytic toxin discovered have hemolytic effects on erythrocytes of certain sensitive species, such as Human.
Rossjohn et al. present the crystal structure of perfringolysin O, a thiol-activated cytolysin, which creates membrane holes on eukaryotic cells.
[10] Shatursky et al. studied the membrane insertion mechanism of Perfringolysin O (PFO), a cholesterol-dependent pore-forming cytolysin produced by pathogenic Clostridium perfringens.
Larry et al. focused on the membrane penetrating models of RTX toxins, a family of MDT secreted by many gram-negative bacteria.
[13] The pathogenic process of PFCs normally involves forming channels or pores at the target cells' membranes.
[18] To prevent such toxicity, host cells produce immunity proteins for binding cytolysins before they do any damage inward.
The lethal effects of pore-forming cytolysins are performed by causing influx and outflux disorder in a single cell.
Pores that allow ions like Na+ to pass through created imbalance in the target cell which exceeds its ion-balancing capacity.
The pore size created by CDC is large (25–30 nm) due to the oligomeric process of cytolysins.
The water-soluble monomers oligomerize to form an intermediate product named "pre-pore" complex and then a β-barrel is penetrated into the membrane.