ChloroquineV1, France, Analysis, bibRecord, 000004

Regulation of endo-lysosomal pathway and autophagic flux by broad-spectrum anti-pathogen inhibitor ABMA

Identifieur interne : 000004 ( France/Analysis ); précédent : 000003; suivant : 000005

Regulation of endo-lysosomal pathway and autophagic flux by broad-spectrum anti-pathogen inhibitor ABMA

Auteurs : Yu Wu ; Claire Boulogne [France] ; Stefan Carle ; Maria Podinovskaia ; Holger Barth ; Anne Spang ; Jean-Christophe Cintrat ; Daniel Gillet ; Julien Barbier

Source :

RBID : Hal:hal-02445466

English descriptors

mix :
- Autophagy, Broad-spectrum inhibitor, Endo-lysosomal pathway, Toxins.

Abstract

The endo-lysosome system is involved in endocytosis, protein sorting and degradation as well as autophagy. Numerous toxins and pathogens exploit this system to enter host cells and exert their deleterious effects. Modulation of host endo-lysosome pathway may restrict multiple toxins intoxication as well as pathogen infection. ABMA, selected from a high-throughput screening against the cytotoxicity of ricin toxin, exhibits a broad-spectrum anti-toxin and anti-pathogen activity. Here, we show that ABMA selectively retains endocytosed protein and toxin to late endosomes, and thus delaying their intracellular trafficking. It also impairs the autophagic flux by excessive fusion of late endosomes and autophagosomes. Its exclusive action on late endosomes and corresponding consequences on the endo-lysosomal pathway and autophagic flux are distinct from known inhibitors such as bafilomycin A1, EGA or chloroquine. Hence, besides being a broad-spectrum inhibitor of endocytosed toxins and pathogens, ABMA may serve as a molecular tool to dissect endo-lysosome system-related cellular physiology and mechanisms of pathogenesis.

Url:

https://hal.archives-ouvertes.fr/hal-02445466

DOI: 10.1111/febs.15201

Affiliations:

France

Links toward previous steps (curation, corpus...)

to stream Hal, to step Corpus: 000205
to stream Hal, to step Curation: 000205
to stream Hal, to step Checkpoint: 000004
to stream Main, to step Merge: 000004
to stream Main, to step Curation: 000004
to stream Main, to step Exploration: 000004
to stream France, to step Extraction: 000004

Links to Exploration step

Hal:hal-02445466

Le document en format XML

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<front><div type="abstract" xml:lang="en">              <p>The endo-lysosome system is involved in endocytosis, protein sorting and degradation as well as autophagy. Numerous toxins and pathogens exploit this system to enter host cells and exert their deleterious effects. Modulation of host endo-lysosome pathway may restrict multiple toxins intoxication as well as pathogen infection. ABMA, selected from a high-throughput screening against the cytotoxicity of ricin toxin, exhibits a broad-spectrum anti-toxin and anti-pathogen activity. Here, we show that ABMA selectively retains endocytosed protein and toxin to late endosomes, and thus delaying their intracellular trafficking. It also impairs the autophagic flux by excessive fusion of late endosomes and autophagosomes. Its exclusive action on late endosomes and corresponding consequences on the endo-lysosomal pathway and autophagic flux are distinct from known inhibitors such as bafilomycin A1, EGA or chloroquine. Hence, besides being a broad-spectrum inhibitor of endocytosed toxins and pathogens, ABMA may serve as a molecular tool to dissect endo-lysosome system-related cellular physiology and mechanisms of pathogenesis.</p>
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   |wiki=    Sante
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   |texte=   Regulation of endo-lysosomal pathway and autophagic flux by broad-spectrum anti-pathogen inhibitor ABMA
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Regulation of endo-lysosomal pathway and autophagic flux by broad-spectrum anti-pathogen inhibitor ABMA

Regulation of endo-lysosomal pathway and autophagic flux by broad-spectrum anti-pathogen inhibitor ABMA

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri