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CD22 (Siglec-2) is a B-cell surface inhibitory protein capable of selectively recognising sialylated glycans, thus dampening autoimmune responses against self-antigens. Here we have characterised the dynamic recognition of complex-type N-glycans by human CD22 by means of orthogonal approaches including NMR spectroscopy, computational methods and biophysical assays. We provide new molecular insights into the binding mode of sialoglycans in complex with h-CD22, highlighting the role of the sialic acid galactose moieties in the recognition process, elucidating the conformational behaviour of complex-type N-glycans bound to Siglec-2 and dissecting the formation of CD22 homo-oligomers on the B-cell surface. Our results could enable the development of additional therapeutics capable of modulating the activity of h-CD22 in autoimmune diseases and malignancies derived from B-cells. © 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Citation

Cristina Di Carluccio, Enrique Crisman, Yoshiyuki Manabe, Rosa Ester Forgione, Alessandra Lacetera, Jussara Amato, Bruno Pagano, Antonio Randazzo, Angela Zampella, Rosa Lanzetta, Koichi Fukase, Antonio Molinaro, Paul R Crocker, Sonsoles Martín-Santamaría, Roberta Marchetti, Alba Silipo. Characterisation of the Dynamic Interactions between Complex N-Glycans and Human CD22. Chembiochem : a European journal of chemical biology. 2020 Jan 15;21(1-2):129-140

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PMID: 31095840

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