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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Elsevier
2021-01-01
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Series: | iScience |
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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. |
first_indexed | 2024-12-14T22:29:46Z |
format | Article |
id | doaj.art-a235801d51084937ad1d3362512574e7 |
institution | Directory Open Access Journal |
issn | 2589-0042 |
language | English |
last_indexed | 2024-12-14T22:29:46Z |
publishDate | 2021-01-01 |
publisher | Elsevier |
record_format | Article |
series | iScience |
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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