A Dynamic Characterization of the Interaction Between Complex-Type N-Glycans and Siglec-2

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A Dynamic Characterization of the Interaction Between Complex-Type N-Glycans and Siglec-2

Cristina Di Carluccio 1 , Antonio Molinaro 1 , Roberta Marchetti 1 , Alba Silipo 1

1 University of Naples “Federico II”, Naples, Italy

Siglecs (Sialic acid-binding Immunoglobulin (Ig)-like lectins) constitute a family of transmembrane glycan-binding receptors that decorate immune cells surfaces and are implicated in both innate and adaptive immunity. [1,2,3] These lectins recognize and bind sialic acids containing glycans, which represent a common structural motif exposed on all mammalian cells. Siglecs perform many regulatory roles and are involved in events like cell-cell communication, inhibition or regulation of immune tolerance and host-pathogen interactions. [4,5]

We deeply characterized, at atomic level, the recognition of complex-type N-glycans by human and murine Siglec-2, also known as CD22, a B-cell surface inhibitory protein [1,5,6] able to dampen autoimmune responses against self-antigens. [7] A combination of different techniques, including advanced NMR approaches [8,9,10,11] (Saturation transfer difference, transferred-NOESY), computational methods [12,13] (Molecular Dynamic, Docking, CORCEMA-ST) and biophysical assays (Surface Plasmon Resonance, Alpha Assay) allowed to achieve key information on the epitope mapping and conformation of complex glycans interacting with human/murine Siglec-2.

Our results may have implication in the design of novel glycomimetics able to modulate the activity of Siglec-2 in autoimmune diseases and various B-cell derived malignancies.

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