The parasitic mushroom Laetiporus sulphureus produces a family of lectins (LSL's) sharing 80-90% sequence identity that possesses a low but significant sequence similarity to the bacterial pore-forming toxins mosquitocidal toxin Mtx-2 from Bacillus sphaericus and α toxin from Clostridium septicum. The crystal structure of one member of the L. sulphureus lectins family (LSLa) reveals unexpected structural similarities to the β-pore-forming toxins from the aerolysin family, namely, aerolysin from the Gram-negative bacterium Aeromonas hydrophila, ε-toxin from Clostridium perfringens and parasporin from B. thuringiensis. This similarity presumably indicates that the hemolytic activity of LSLa proceeds through a molecular mechanism that involves the formation of oligomeric transmembrane β-barrels. Comparison of the crystal structures of the above mentioned proteins reveals common pore-forming modules, which are then distributed both in bacteria and fungi. Currently, it can be stated that the above three dimensional structures have been key in revealing structural similarities that were elusive at the sequence level. A potential corollary from this is that structural studies aimed at determining high resolution structures of aerolysin-like pore-forming toxins, whose biological activity involves large conformational changes, are mandatory to define protein domains or structural motifs with membrane-binding properties.