Cathepsin Release from Lysosomes Promotes Endocytosis of Clostridium perfringens Iota-Toxin.
Toxins (Basel)
; 13(10)2021 10 12.
Article
en En
| MEDLINE
| ID: mdl-34679014
Iota-toxin from Clostridium perfringens type E is a binary toxin composed of two independent proteins: actin-ADP-ribosylating enzyme component, iota-a (Ia), and binding component, iota-b (Ib). Ib binds to target cell receptors and mediates the internalization of Ia into the cytoplasm. Extracellular lysosomal enzyme acid sphingomyelinase (ASMase) was previously shown to facilitate the internalization of iota-toxin. In this study, we investigated how lysosomal cathepsin promotes the internalization of iota-toxin into target cells. Cysteine protease inhibitor E64 prevented the cytotoxicity caused by iota-toxin, but aspartate protease inhibitor pepstatin-A and serine protease inhibitor AEBSF did not. Knockdown of lysosomal cysteine protease cathepsins B and L decreased the toxin-induced cytotoxicity. E64 suppressed the Ib-induced ASMase activity in extracellular fluid, showing that the proteases play a role in ASMase activation. These results indicate that cathepsin B and L facilitate entry of iota-toxin via activation of ASMase.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Esfingomielina Fosfodiesterasa
/
Toxinas Bacterianas
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ADP Ribosa Transferasas
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Endocitosis
Límite:
Animals
Idioma:
En
Revista:
Toxins (Basel)
Año:
2021
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Suiza