Human α-Defensins Inhibit Hemolysis Mediated by Cholesterol-Dependent Cytolysins

The cholesterol-dependent cytolysins.

In view of the recent studies on the CDCs, a reasonable schematic of the stages leading to membrane insertion of the CDCs can be assembled. As shown in Fig. 3, we propose that the CDC first binds to the membrane as a monomer. These monomers then diffuse laterally on the membrane surface to encounter other monomers or incomplete oligomeric complexes. Presumably, once the requisite oligomer size ...

A New Model for Pore Formation by Cholesterol-Dependent Cytolysins

Cholesterol Dependent Cytolysins (CDCs) are important bacterial virulence factors that form large (200-300 Å) membrane embedded pores in target cells. Currently, insights from X-ray crystallography, biophysical and single particle cryo-Electron Microscopy (cryo-EM) experiments suggest that soluble monomers first interact with the membrane surface via a C-terminal Immunoglobulin-like domain (Ig;...

Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins.

Cholesterol-dependent cytolysins (CDCs) are a family of pore-forming toxins that punch holes in the outer membrane of eukaryotic cells. Cholesterol serves as the receptor, but a subclass of CDCs first binds to human CD59. Here we describe the crystal structures of vaginolysin and intermedilysin complexed to CD59. These studies, together with small-angle X-ray scattering, reveal that CD59 binds ...

Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins.

How cholesterol-dependent cytolysins bite holes into membranes.

In a show piece for electron microscopy (EM), Tilley at al. used single-particle cryo-EM to visualize the structural rearrangements in the bacterial toxin pneumolysin that occur when it assembles into a membrane-associated prepore and when the prepore subsequently transitions into a fully membrane-inserted pore.