Journal
ISCIENCE
Volume 23, Issue 6, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.isci.2020.101231
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Funding
- project GLYTUNES'' - MIUR Progetti di Ricerca di Rilevante Interesse Nazionale (PRIN 2017) [2017XZ2ZBK]
- progetto POR SATIN
- European Commission [H2020-MSCA-814102-SWEET CROSSTALK]
- European Research Council (ERC) under the European Union [851356]
- Spanish Ministry of Science MICINN [CTQ2017-88353-R, BES 2015-071588]
- Wellcome Trust [103744/Z/14/Z]
- Progetto POR Campania Oncoterapia
- Wellcome Trust [103744/Z/14/Z] Funding Source: Wellcome Trust
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Siglec-10 is an inhibitory I-type lectin selectively recognizing sialoglycans exposed on cell surfaces, involved in several patho-physiological processes. The key role Siglec-10 plays in the regulation of immune cell functions has made it a potential target for the development of immunotherapeutics against a broad range of diseases. However, the crystal structure of the protein has not been resolved for the time being and the atomic description of Siglec-10 interactions with complex glycans has not been previously unraveled. We present here the first insights of the molecular mechanisms regulating the interaction between Siglec-10 and naturally occurring sialoglycans. We used combined spectroscopic, computational and biophysical approaches to dissect glycans' epitope mapping and conformation upon binding in order to afford a description of the 3D complexes. Our outcomes provide a structural perspective for the rational design and development of high-affinity ligands to control the receptor functionality.
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