Binding of Kingella kingae RtxA Toxin Depends on Cell Surface Oligosaccharides, but Not on beta(2) Integrins

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F20%3A00536763" target="_blank" >RIV/61388971:_____/20:00536763 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/20:10421360

Result on the web

<a href="https://www.mdpi.com/1422-0067/21/23/9092" target="_blank" >https://www.mdpi.com/1422-0067/21/23/9092</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/ijms21239092" target="_blank" >10.3390/ijms21239092</a>

Result language

angličtina

Original language name

Binding of Kingella kingae RtxA Toxin Depends on Cell Surface Oligosaccharides, but Not on beta(2) Integrins

Original language description

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.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10606 - Microbiology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2020

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

International Journal of Molecular Sciences

ISSN

1422-0067

e-ISSN

—

Volume of the periodical

21

Issue of the periodical within the volume

23

Country of publishing house

CH - SWITZERLAND

Number of pages

14

Pages from-to

9092

UT code for WoS article

000597593100001

EID of the result in the Scopus database

2-s2.0-85097035918