Multiple O-and an N-glycosylation of the stalk region of the NK cell activation receptor NKp46 mediates its interaction with the Candida glabrata epithelial adhesin 1
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F25%3A00619611" target="_blank" >RIV/86652036:_____/25:00619611 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/25:10500804
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0141813025035895?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813025035895?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.ijbiomac.2025.143037" target="_blank" >10.1016/j.ijbiomac.2025.143037</a>
Alternative languages
Result language
angličtina
Original language name
Multiple O-and an N-glycosylation of the stalk region of the NK cell activation receptor NKp46 mediates its interaction with the Candida glabrata epithelial adhesin 1
Original language description
Natural killer (NK) cells are critical components of the innate immune system. Their primary role is to induce apoptosis in target cells, such as cancerous or virally infected cells. These targets are recognized through interactions between activating or inhibitory receptors on the NK cell surface. Among the activating receptors is the natural cytotoxicity receptor NKp46. Several ligands for this receptor have been identified, including the epithelial adhesin Epa1 from the yeast Candida glabrata. Invasive candidiasis caused by this yeast is a significant complication for patients with hematological diseases. The interaction between NKp46 and Epa1 is thought to depend specifically on an O-glycan at threonine 225 of NKp46. To elucidate the molecular details of this interaction, we optimized the recombinant production of soluble NKp46 and Epa1, generated glycosylation variants of multiple NKp46 mutants, and evaluated the role of NKp46 glycosylation in Epa1 binding using microscale thermophoresis and isothermal titration calorimetry. Additionally, for the first time, we provide a comprehensive glycosylation profile of NKp46, determined through mass spectrometry of intact glycopeptides obtained by O-glycoprotease and trypsin proteolysis. Our findings demonstrate that the NKp46 stalk is glycosylated at multiple sites, involving both an N-glycan and more than one O-glycan. These glycans are critical for the interaction with Epa1, providing NK cells with enhanced sensitivity to Candida glabrata epitopes.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10404 - Polymer science
Result continuities
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
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International Journal of Biological Macromolecules
ISSN
0141-8130
e-ISSN
1879-0003
Volume of the periodical
310
Issue of the periodical within the volume
MAY 2025
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
13
Pages from-to
143037
UT code for WoS article
001477216100001
EID of the result in the Scopus database
2-s2.0-105002904761