Number of the records: 1
Kingella kingae RtxA toxin interacts with sialylated gangliosides
- 1.0575316 - MBÚ 2024 RIV NL eng J - Journal Article
Rahman, Waheed Ur - Fišer, Radovan - Osička, Radim
Kingella kingae RtxA toxin interacts with sialylated gangliosides.
Microbial Pathogenesis. Roč. 181, AUG (2023), č. článku 106200. ISSN 0882-4010. E-ISSN 1096-1208
R&D Projects: GA ČR(CZ) GA22-15825S; GA MŠMT(CZ) LM2023053
Institutional support: RVO:61388971
Keywords : Gangliosides * Kingella kingae * RtxA * RTX toxins * Sialic acid * Vesicles
OECD category: Microbiology
Impact factor: 3.8, year: 2022
Method of publishing: Limited access
https://www.sciencedirect.com/science/article/pii/S0882401023002334?via%3Dihub
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.
Permanent Link: https://hdl.handle.net/11104/0345099
Number of the records: 1