Chloroquine-analogues block anthrax protective antigen channels in steady-state and kinetic studies.
Anthrax-toxin
Binding components
Binding kinetics
Black lipid bilayer
Chloroquine
Quinoline analogues
Journal
Toxicology
ISSN: 1879-3185
Titre abrégé: Toxicology
Pays: Ireland
ID NLM: 0361055
Informations de publication
Date de publication:
15 06 2023
15 06 2023
Historique:
received:
30
03
2023
revised:
11
05
2023
accepted:
15
05
2023
medline:
1
6
2023
pubmed:
19
5
2023
entrez:
18
5
2023
Statut:
ppublish
Résumé
The tripartite anthrax toxin from Bacillus anthracis represents the prototype of A-B type of toxins, where the effector A (an enzymatic subunit) is transported with the help of a binding component B into a target cell. Anthrax toxin consists of three different molecules, two effectors, lethal factor (LF) and edema factor (EF) and the binding component also known as protective antigen (PA). PA forms heptamers or octamers following binding to host cell's receptors and mediates the translocation of the effectors into the cytosol via the endosomal pathway. The cation-selective PA
Identifiants
pubmed: 37201861
pii: S0300-483X(23)00133-6
doi: 10.1016/j.tox.2023.153547
pii:
doi:
Substances chimiques
anthrax toxin
0
Chloroquine
886U3H6UFF
Ligands
0
Bacterial Toxins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
153547Informations de copyright
Copyright © 2023 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Roland Benz reports financial support was provided by Deutsche Forschungsgemeinschaft. Roland Benz reports a relationship with Constructor University Bremen gGmbH that includes: employment. No additional relationships or activities to declare.