Insights into stability, dimerisation, and ligand binding properties of Siglec-7: Isotope labelling in HEK293 cells for protein characterisation by NMR spectroscopy

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F25%3A10499042" target="_blank" >RIV/00216208:11310/25:10499042 - isvavai.cz</a>

Alternative codes found

RIV/00216224:90242/25:00144088

Result on the web

<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=G7xTbBOkgG" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=G7xTbBOkgG</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ijbiomac.2025.142672" target="_blank" >10.1016/j.ijbiomac.2025.142672</a>

Result language

angličtina

Original language name

Insights into stability, dimerisation, and ligand binding properties of Siglec-7: Isotope labelling in HEK293 cells for protein characterisation by NMR spectroscopy

Original language description

Siglec-7, an immune checkpoint receptor, has emerged as a promising target for cancer immunotherapy due to its involvement in the regulation of immune and inflammatory responses. However, while its participation in immunoediting and immune evasion is well established, understanding its biological context, relevant ligands, and associated signalling pathways remains limited. Understanding these aspects is crucial for the development of effective immunotherapies targeting Siglec-7.In this study, three expression constructs of Siglec-7 were designed, expressed, and characterised, including an analysis of the oligomeric state of its extracellular domain. The N-terminal V-set Ig carbohydrate recognition domain was also produced in an isotopically double-labelled ((13)C,(15)N) mammalian cell growth medium. Two stable constructs suitable for biophysical and structural studies were identified. These findings reveal the noncovalent dimerisation of Siglec-7, offering new insights into its possible ligand interactions, signal transduction mechanisms, or receptor/ligand clustering. The dimerisation of Siglec-7 may be essential to achieve multivalent, high-avidity interactions with glycoconjugates, which may result in enhanced or alternative signalling processes within the NK cell immune synapse. In addition, a detailed protocol for generating double-labelled Siglec-7 in HEK293 cells, which may apply to other proteins under similar conditions, was described. These findings contribute to a better understanding of the biophysical and structural properties of Siglec-7 and are key to the design of more precise and effective cancer immunotherapies targeting Siglec-7.

Czech name

—

Czech description

—

Type

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

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

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

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2025

Confidentiality

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

Name of the periodical

International Journal of Biological Macromolecules

ISSN

0141-8130

e-ISSN

1879-0003

Volume of the periodical

309

Issue of the periodical within the volume

Part 1

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

14

Pages from-to

142672

UT code for WoS article

001468747500001

EID of the result in the Scopus database

2-s2.0-105001822220