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Characterisation of the Dynamic Interactions between Complex N ‐Glycans and Human CD22
Author(s) -
Di Carluccio Cristina,
Crisman Enrique,
Manabe Yoshiyuki,
Forgione Rosa Ester,
Lacetera Alessandra,
Amato Jussara,
Pagano Bruno,
Randazzo Antonio,
Zampella Angela,
Lanzetta Rosa,
Fukase Koichi,
Molinaro Antonio,
Crocker Paul R.,
MartínSantamaría Sonsoles,
Marchetti Roberta,
Silipo Alba
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900295
Subject(s) - cd22 , glycan , siglec , sialic acid , chemistry , biochemistry , cell , computational biology , microbiology and biotechnology , biophysics , biology , glycoprotein , cd19
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.