Kingella kingae RtxA toxin interacts with sialylated gangliosides
Language English Country Great Britain, England Media print-electronic
Document type Journal Article
PubMed
37315629
DOI
10.1016/j.micpath.2023.106200
PII: S0882-4010(23)00233-4
Knihovny.cz E-resources
- Keywords
- Gangliosides, Kingella kingae, RTX toxins, RtxA, Sialic acid, Vesicles,
- MeSH
- Bacterial Toxins * metabolism MeSH
- Cell Membrane metabolism MeSH
- Cytotoxins metabolism MeSH
- Child MeSH
- Virulence Factors metabolism MeSH
- Kingella kingae * metabolism MeSH
- Humans MeSH
- Check Tag
- Child MeSH
- Humans MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Bacterial Toxins * MeSH
- Cytotoxins MeSH
- Virulence Factors MeSH
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.
References provided by Crossref.org
Kingella kingae cytotoxin RtxA induces an innate immune response in oral epithelial cells
