Binding of Kingella kingae RtxA Toxin Depends on Cell Surface Oligosaccharides, but Not on β2 Integrins
| Autor: | Nela Klimova, Adriana Osickova, Jinery Lora, Radim Osicka, Nataliya V. Balashova, Waheed Ur Rahman |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Glycosylation β2 integrins Cell Oligosaccharides Kingella kingae RtxA lcsh:Chemistry Mice Cytotoxic T cell lcsh:QH301-705.5 Spectroscopy biology Cell Death Chemistry RTX toxin Hemolysin General Medicine Computer Science Applications medicine.anatomical_structure Female Protein Binding Cell type Glycoside Hydrolases 030106 microbiology Integrin Bacterial Toxins Catalysis Article Microbiology Cell Line Inorganic Chemistry 03 medical and health sciences medicine Animals Humans Physical and Theoretical Chemistry Molecular Biology Macrophages Organic Chemistry Cell Membrane biology.organism_classification Cytolysis 030104 developmental biology lcsh:Biology (General) lcsh:QD1-999 CD18 Antigens biology.protein |
| Zdroj: | International Journal of Molecular Sciences International Journal of Molecular Sciences, Vol 21, Iss 9092, p 9092 (2020) Volume 21 Issue 23 |
| ISSN: | 1422-0067 |
| Popis: | The Gram-negative coccobacillus Kingella kingae is increasingly recognized as an important invasive pediatric pathogen that causes mostly bacteremia and skeletal system infections. K. kingae secretes an RtxA toxin that belongs to a broad family of the RTX (Repeats in ToXin) cytotoxins produced by bacterial pathogens. Recently, we demonstrated that membrane cholesterol facilitates interaction of RtxA with target cells, but other cell surface structures potentially involved in toxin binding to cells remain unknown. We show that deglycosylation of cell surface structures by glycosidase treatment, or inhibition of protein N- and O-glycosylation by chemical inhibitors substantially reduces RtxA binding to target cells. Consequently, the deglycosylated cells were more resistant to cytotoxic activity of RtxA. Moreover, experiments on cells expressing or lacking cell surface integrins of the &beta 2 family revealed that, unlike some other cytotoxins of the RTX family, K. kingae RtxA does not bind target cells via the &beta 2 integrins. Our results, hence, show that RtxA binds cell surface oligosaccharides present on all mammalian cells but not the leukocyte-restricted &beta 2 integrins. This explains the previously observed interaction of the toxin with a broad range of cell types of various mammalian species and reveals that RtxA belongs to the group of broadly cytolytic RTX hemolysins. |
| Databáze: | OpenAIRE |
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