Behavior of glycolylated sialoglycans in the binding pockets of murine and human CD22

Cristina Di Carluccio, Rosa Ester Forgione, Marco Montefiori, Monica Civera, Sara Sattin, Giovanni Smaldone, K. Fukase, Y. Manabe, Paul R. Crocker, Antonio Molinaro, Roberta Marchetti (Lead / Corresponding author), Alba Silipo (Lead / Corresponding author)

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    Abstract

    Siglecs (sialic acid binding immunoglobulin (Ig)-like lectins) constitute a group of 15 human and 9 murine cell-surface transmembrane receptors belonging to the I-type lectin family, mostly expressed on innate immune cells and characterized by broadly similar structural features. Here, the prominent inhibitory CD22 (Siglec-2), well known in maintaining tolerance and preventing autoimmune responses on B cells, is studied in its human and murine forms in complex with sialoglycans. In detail, the role of the N-glycolyl neuraminic acid (Neu5Gc) moiety in the interaction with both orthologues was explored. The analysis of the binding mode was carried out by the combination of NMR spectroscopy, computational approaches, and CORCEMA-ST calculations. Our findings provide a first model of Neu5Gc recognition by h-CD22 and show a comparable molecular recognition profile by h- and m-CD22. These data open the way to innovative diagnostic and/or therapeutic methodologies to be used in the modulation of the immune responses.

    Original languageEnglish
    Article number101998
    Number of pages26
    JournaliScience
    Volume24
    Issue number1
    Early online date29 Dec 2020
    DOIs
    Publication statusPublished - 22 Jan 2021

    Keywords

    • Biochemistry
    • Immunology
    • Structural Biology

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