Clostridium perfringens epsilon-toxin requires acid sphingomyelinase for cellular entry.
Acid sphingomyelinase
C. perfringens epsilon-Toxin
Internalization
Journal
Anaerobe
ISSN: 1095-8274
Titre abrégé: Anaerobe
Pays: England
ID NLM: 9505216
Informations de publication
Date de publication:
Aug 2023
Aug 2023
Historique:
received:
18
04
2023
revised:
08
06
2023
accepted:
09
06
2023
medline:
4
10
2023
pubmed:
13
6
2023
entrez:
12
6
2023
Statut:
ppublish
Résumé
Clostridium perfringens epsilon-toxin is considered to be a crucial agent in enterotoxemia in domestic animals. Epsilon-toxin enters host cells via endocytosis and results in the formation of late endosome/lysosome-derived vacuoles. In the present study, we found that acid sphingomyelinase promotes the internalization of epsilon-toxin in MDCK cells. We measured the extracellular release of acid sphingomyelinase (ASMase) by epsilon-toxin. We examined the role of ASMase in epsilon-toxin-induced cytotoxicity using selective inhibitors and knockdown of ASMase. Production of ceramide after toxin treatment was determined by immunofluorescence technique. Blocking agents of ASMase and exocytosis of lysosomes inhibited this epsilon-toxin-induced vacuole formation. Lysosomal ASMase was liberated to extracellular space during treatment of the cells with epsilon-toxin in the presence of Ca Based on the present results, ASMase is required for efficient internalization of epsilon-toxin.
Identifiants
pubmed: 37308057
pii: S1075-9964(23)00062-8
doi: 10.1016/j.anaerobe.2023.102753
pii:
doi:
Substances chimiques
Clostridium perfringens epsilon-toxin
0
Sphingomyelin Phosphodiesterase
EC 3.1.4.12
Bacterial Toxins
0
Ceramides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
102753Informations de copyright
Copyright © 2023 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that there are no conflicts of interest.