Bacterial intracellularly active toxins: Membrane localisation of the active domain.
Animals
Bacterial Proteins
Bacterial Toxins
/ metabolism
Botulinum Toxins
Catalytic Domain
Cell Membrane
/ drug effects
Cytoplasm
/ metabolism
Humans
Legionella pneumophila
Metalloendopeptidases
Neurotoxins
Phosphatidic Acids
Phosphatidylserines
/ metabolism
Tetanus Toxin
Virulence Factors
/ metabolism
rho GTP-Binding Proteins
/ metabolism
Pasteurella multocida toxin
Bacterial virulence factors
MARTX toxins
Rho/Ras-GTPases
cell membrane
large clostridial glucosylating toxins
phospholipids
Journal
Cellular microbiology
ISSN: 1462-5822
Titre abrégé: Cell Microbiol
Pays: India
ID NLM: 100883691
Informations de publication
Date de publication:
07 2020
07 2020
Historique:
received:
03
12
2019
revised:
06
04
2020
accepted:
17
04
2020
pubmed:
1
5
2020
medline:
2
6
2021
entrez:
1
5
2020
Statut:
ppublish
Résumé
Numerous bacterial toxins exert their activity by inactivating or modulating a specific intracellular host target. For this purpose, these toxins have developed efficient strategies to overcome the different host cell defences including specific binding to cell surface, internalisation, passage through the endosome or plasma membrane, exploiting intracellular trafficking and addressing to intracellular targets. Several intracellularly active toxins deliver an active domain into the cytosol that interacts with a target localised to the inner face of the plasma membrane. Thus, the large clostridial glucosylating toxins (LCGTs) target Rho/Ras-GTPases, certain virulence factors of Gram negative bacteria, Rho-GTPases, while Pasteurella multocida toxin (PMT) targets trimeric G-proteins. Others such as botulinum neurotoxins and tetanus neurotoxin have their substrate on synaptic vesicle membrane. LCGTs, PMT, and certain virulence factors from Vibrio sp. show a particular structure constituted of a four-helix bundle membrane (4HBM) protruding from the catalytic site that specifically binds to the membrane phospholipids and then trap the catalytic domain at the proximity of the membrane anchored substrate. Structural and functional analysis indicate that the 4HBM tip of the Clostridium sordellii lethal toxin (TcsL) from the LCGT family contain two loops forming a cavity that mediates the binding to phospholipids and more specifically to phosphatidylserine.
Substances chimiques
Bacterial Proteins
0
Bacterial Toxins
0
Neurotoxins
0
Pasteurella multocida toxin
0
Phosphatidic Acids
0
Phosphatidylserines
0
Tetanus Toxin
0
Virulence Factors
0
lethal toxin LT, Clostridium sordellii
0
tetanospasmin
11032-48-7
Metalloendopeptidases
EC 3.4.24.-
Botulinum Toxins
EC 3.4.24.69
rho GTP-Binding Proteins
EC 3.6.5.2
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e13213Informations de copyright
© 2020 John Wiley & Sons Ltd.
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