Kingella kingae RtxA toxin interacts with sialylated gangliosides.
Gangliosides
Kingella kingae
RTX toxins
RtxA
Sialic acid
Vesicles
Journal
Microbial pathogenesis
ISSN: 1096-1208
Titre abrégé: Microb Pathog
Pays: England
ID NLM: 8606191
Informations de publication
Date de publication:
Aug 2023
Aug 2023
Historique:
received:
14
04
2023
revised:
11
06
2023
accepted:
12
06
2023
medline:
10
7
2023
pubmed:
15
6
2023
entrez:
14
6
2023
Statut:
ppublish
Résumé
The membrane-damaging RTX family cytotoxin RtxA is a key virulence factor of the emerging pediatric pathogen Kingella kingae, but little is known about the mechanism of RtxA binding to host cells. While we have previously shown that RtxA binds cell surface glycoproteins, here we demonstrate that the toxin also binds different types of gangliosides. The recognition of gangliosides by RtxA depended on sialic acid side groups of ganglioside glycans. Moreover, binding of RtxA to epithelial cells was significantly decreased in the presence of free sialylated gangliosides, which inhibited cytotoxic activity of the toxin. These results suggest that RtxA utilizes sialylated gangliosides as ubiquitous cell membrane receptor molecules on host cells to exert its cytotoxic action and support K. kingae infection.
Identifiants
pubmed: 37315629
pii: S0882-4010(23)00233-4
doi: 10.1016/j.micpath.2023.106200
pii:
doi:
Substances chimiques
Bacterial Toxins
0
Virulence Factors
0
Cytotoxins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
106200Informations de copyright
Copyright © 2023 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.