1.C.38.1.14
Pore-forming toxin, Nigrelysin of 214 aas. The toxin lacks Cys and readily permeabilizes erythrocytes, as well as L1210 cells. CD spectroscopy revealed that its secondary structure is dominated by beta structure (58.5%) with 5.5% α-helix, and 35% random structure. Binding experiments to lipidic monolayers and to liposomes, as well as permeabilization studies in vesicles, revealed that the affinity of this toxin for sphingomyelin-containing membranes is quite similar to sticholysin II (StII) (Alvarado-Mesén et al. 2019).