Advanced glycation end products reduce macrophage-mediated killing of Staphylococcus aureus by ARL8 upregulation and inhibition of autolysosome formation.
ARL8
Advanced glycation end products (AGEs)
Autophagy
Macrophage
Staphylococcus aureus
Journal
European journal of immunology
ISSN: 1521-4141
Titre abrégé: Eur J Immunol
Pays: Germany
ID NLM: 1273201
Informations de publication
Date de publication:
08 2020
08 2020
Historique:
received:
19
11
2019
revised:
25
02
2020
accepted:
31
03
2020
pubmed:
7
4
2020
medline:
16
12
2020
entrez:
7
4
2020
Statut:
ppublish
Résumé
Staphylococcus aureus, a pathogen most frequently found in diabetic foot ulcer infection, was recently suggested as an intracellular pathogen. Autophagy in professional phagocytes like macrophages allows selective destruction of intracellular pathogens, and its dysfunction can increase the survival of internalized pathogens, causing infections to worsen and spread. Previous works have shown that S. aureus infections in diabetes appeared more severe and invasive, and coincided with the suppressed autophagy in dermal tissues of diabetic rat, but the exact mechanisms are unclear. Here, we demonstrated that accumulation of advanced glycation end products (AGEs) contributed to the diminished autophagy-mediated clearance of S. aureus in the macrophages differentiated from PMA-treated human monocytic cell line THP-1. Importantly, infected macrophages showed increased S. aureus containing autophagosome, but the subsequent fusion of S. aureus containing autophagosome and lysosome was suppressed in AGEs-pretreated cells, suggesting AGEs blocked the autophagic flux and enabled S. aureus survival and escape. At the molecular level, elevated lysosomal ARL8 expression in AGEs-treated macrophages was required for AGEs-mediated inhibition of autophagosome-lysosome fusion. Silencing ARL8 in AGEs-treated macrophages restored autophagic flux and increased S. aureus clearance. Our results therefore demonstrate a new mechanism, in which AGEs accelerate S. aureus immune evasion in macrophages by ARL8-dependent suppression of autophagosome-lysosome fusion and bactericidal capability.
Identifiants
pubmed: 32250445
doi: 10.1002/eji.201948477
doi:
Substances chimiques
Glycation End Products, Advanced
0
ARL5B protein, human
EC 3.6.1.2
ADP-Ribosylation Factors
EC 3.6.5.2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1174-1186Subventions
Organisme : National Key R&D Program of China
ID : 2016YFC0901200
Pays : International
Organisme : National Natural Science Foundation of China
ID : 81770827
Pays : International
Organisme : National Natural Science Foundation of China
ID : 81972967
Pays : International
Organisme : Guangdong Science and Technology Department
ID : 2017B030314026
Pays : International
Organisme : Guangdong Medical Research Fund Project
ID : A2018365
Pays : International
Organisme : Guangdong Basic and Applied Basic Research Foundation
ID : 2017A020215017
Pays : International
Organisme : Guangdong Basic and Applied Basic Research Foundation
ID : 2019A1515011754
Pays : International
Informations de copyright
© 2020 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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