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

Summary: 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...

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Main Authors: 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, Alba Silipo
Format: Article
Language:English
Published: Elsevier 2021-01-01
Series:iScience
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2589004220311950
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author 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
Alba Silipo
author_facet 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
Alba Silipo
author_sort Cristina Di Carluccio
collection DOAJ
description Summary: 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.
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spelling doaj.art-a235801d51084937ad1d3362512574e72022-12-21T22:45:16ZengElsevieriScience2589-00422021-01-01241101998Behavior of glycolylated sialoglycans in the binding pockets of murine and human CD22Cristina Di Carluccio0Rosa Ester Forgione1Marco Montefiori2Monica Civera3Sara Sattin4Giovanni Smaldone5K. Fukase6Y. Manabe7Paul R. Crocker8Antonio Molinaro9Roberta Marchetti10Alba Silipo11Dipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, ItalyDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, ItalyDipartimento di Chimica, Università Degli Studi di Milano, Via Golgi, 19, 20133 Milano, ItalyDipartimento di Chimica, Università Degli Studi di Milano, Via Golgi, 19, 20133 Milano, ItalyDipartimento di Chimica, Università Degli Studi di Milano, Via Golgi, 19, 20133 Milano, ItalyIRCCS SDN, Via E. Gianturco 113, Napoli, ItalyDepartment of Chemistry, Graduate School of Science, Osaka University, Suita, JapanDepartment of Chemistry, Graduate School of Science, Osaka University, Suita, JapanDivision of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee, United KingdomDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, ItalyDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, Italy; Corresponding authorDipartimento di Scienze Chimiche, Complesso Universitario Monte Sant’Angelo, Università di Napoli Federico II, Via Cintia 4, 80126 Napoli, Italy; Corresponding authorSummary: 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.http://www.sciencedirect.com/science/article/pii/S2589004220311950BiochemistryImmunologyStructural Biology
spellingShingle 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
Alba Silipo
Behavior of glycolylated sialoglycans in the binding pockets of murine and human CD22
iScience
Biochemistry
Immunology
Structural Biology
title Behavior of glycolylated sialoglycans in the binding pockets of murine and human CD22
title_full Behavior of glycolylated sialoglycans in the binding pockets of murine and human CD22
title_fullStr Behavior of glycolylated sialoglycans in the binding pockets of murine and human CD22
title_full_unstemmed Behavior of glycolylated sialoglycans in the binding pockets of murine and human CD22
title_short Behavior of glycolylated sialoglycans in the binding pockets of murine and human CD22
title_sort behavior of glycolylated sialoglycans in the binding pockets of murine and human cd22
topic Biochemistry
Immunology
Structural Biology
url http://www.sciencedirect.com/science/article/pii/S2589004220311950
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