Epidermolytic toxin binds to components in the epidermis of a resistant species.

Ferritin-labeled epidermolytic toxin selectively bound to resin-impregnated sections of toxin-resistant rat skin. Binding was confined to the keratohyalin granules of the stratum granulosum and to the cytoplasm of cells in the stratum corneum. Single granules, and equivalent regions in composite granules, failed to bind the conjugate. Preferential binding of the ferritin-toxin probe created anastomosed arrays in the large granules. The scoring density within corneal cells varied with the position of the cell in the stratum corneum. It reached a maximum in the fourth cell from the granular-corneal junction, then decreased to a negligible value in the outermost corneal layers. Three groups of toxin-binding polypeptides were identified in epidermal extracts. These include profilaggrin, a group of three histone H1 polypeptides and histone H3. Filaggrin did not react with toxin on Western blots. The findings demonstrate that sensitivity to epidermolytic toxin is not solely dependent on the presence of target material. It is suggested that species-specific differences in the morphology of keratohyalin granules and in metabolism of profilaggrin may be important factors in intoxication.