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Binding of Kingella kingae RtxA Toxin Depends on Cell Surface Oligosaccharides, but Not on beta(2) Integrins
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SYSNO ASEP 0536763 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Binding of Kingella kingae RtxA Toxin Depends on Cell Surface Oligosaccharides, but Not on beta(2) Integrins Author(s) Rahman, Waheed Ur (MBU-M) ORCID
Osičková, Adriana (MBU-M) RID, ORCID
Klímová, Nela (MBU-M) ORCID
Lora, J. (US)
Balashova, N. (US)
Osička, Radim (MBU-M) RID, ORCIDArticle number 9092 Source Title International Journal of Molecular Sciences. - : MDPI
Roč. 21, č. 23 (2020)Number of pages 14 s. Language eng - English Country CH - Switzerland Keywords integrins ; Kingella kingae ; oligosaccharides Subject RIV EE - Microbiology, Virology OECD category Microbiology R&D Projects GA18-18079S GA ČR - Czech Science Foundation (CSF) LM2018133 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support MBU-M - RVO:61388971 UT WOS 000597593100001 EID SCOPUS 85097035918 DOI 10.3390/ijms21239092 Annotation 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. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2021 Electronic address https://www.mdpi.com/1422-0067/21/23/9092
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