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Article dans une revue

Discovery of a new sialic acid binding region that regulates Siglec-7

Abstract : Siglec-7 is a human CD33-like siglec, and is localised predominantly on human natural killer (NK) cells and monocytes. Siglec-7 is considered to function as an immunoreceptor in a sialic acid-dependent manner. However, the underlying mechanisms linking sialic acid-binding and function remain unknown. Here, to gain new insights into the ligand-binding properties of Siglec-7, we carried out in silico analysis and site-directed mutagenesis, and found a new sialic acid-binding region (site 2 containing R67) in addition to the well-known primary ligand-binding region (site 1 containing R124). This was supported by equilibrium dialysis, STD-NMR experiments, and inhibition analysis of GD3-binding toward Siglec-7 using synthetic sialoglycoconjugates and a comprehensive set of ganglioside-based glycoconjugates. Our results suggest that the two ligand-binding sites are potentially controlled by each other due to the flexible conformation of the C-C′ loop of Siglec-7.
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Soumis le : mercredi 24 mars 2021 - 12:16:36
Dernière modification le : mardi 19 octobre 2021 - 11:34:39


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Nao Yamakawa, Yu Yasuda, Atsushi Yoshimura, Ami Goshima, Paul R. Crocker, et al.. Discovery of a new sialic acid binding region that regulates Siglec-7. Scientific Reports, Nature Publishing Group, 2020, Scientific Reports, 10 (1), ⟨10.1038/s41598-020-64887-4⟩. ⟨hal-03179459⟩



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