Characterisation of the Dynamic Interactions between Complex N-Glycans and Human CD22

Cristina Di Carluccio; Enrique Crisman; Yoshiyuki Manabe; Rosa Ester Forgione; Alessandra Lacetera; Jussara Amato; Bruno Pagano; Antonio Randazzo; Angela Zampella; Rosa Lanzetta; Koichi Fukase; Antonio Molinaro; Paul R. Crocker; Sonsoles Martín-Santamaría; Roberta Marchetti; Alba Silipo

doi:10.1002/cbic.201900295

Characterisation of the Dynamic Interactions between Complex N-Glycans and Human CD22

Cristina Di Carluccio, Enrique Crisman, Yoshiyuki Manabe, Rosa Ester Forgione, Alessandra Lacetera, Jussara Amato, Bruno Pagano, Antonio Randazzo, Angela Zampella, Rosa Lanzetta, Koichi Fukase, Antonio Molinaro, Paul R. Crocker, Sonsoles Martín-Santamaría (Lead / Corresponding author), Roberta Marchetti (Lead / Corresponding author), Alba Silipo (Lead / Corresponding author)

Cell Signalling and Immunology

Research output: Contribution to journal › Article › peer-review

16 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	129-140
Number of pages	12
Journal	ChemBioChem
Volume	21
Issue number	1-2
Early online date	16 May 2019
DOIs	https://doi.org/10.1002/cbic.201900295
Publication status	Published - 15 Jan 2020

Keywords

molecular recognition
N-glycans
NMR spectroscopy
sialic acids
Siglecs

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Organic Chemistry

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/cbic.201900295

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Di Carluccio, C., Crisman, E., Manabe, Y., Forgione, R. E., Lacetera, A., Amato, J., Pagano, B., Randazzo, A., Zampella, A., Lanzetta, R., Fukase, K., Molinaro, A., Crocker, P. R., Martín-Santamaría, S., Marchetti, R., & Silipo, A. (2020). Characterisation of the Dynamic Interactions between Complex N-Glycans and Human CD22. ChemBioChem, 21(1-2), 129-140. https://doi.org/10.1002/cbic.201900295

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title = "Characterisation of the Dynamic Interactions between Complex N-Glycans and Human CD22",

abstract = "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.",

keywords = "molecular recognition, N-glycans, NMR spectroscopy, sialic acids, Siglecs",

author = "{Di Carluccio}, Cristina and Enrique Crisman and Yoshiyuki Manabe and Forgione, {Rosa Ester} and Alessandra Lacetera and Jussara Amato and Bruno Pagano and Antonio Randazzo and Angela Zampella and Rosa Lanzetta and Koichi Fukase and Antonio Molinaro and Crocker, {Paul R.} and Sonsoles Mart{\'i}n-Santamar{\'i}a and Roberta Marchetti and Alba Silipo",

note = "Funding Information: H2020 Marie Sk{\l}odowska-Curie Actions. Grant Numbers: 642157, 814102; Mizutani Foundation for Glycoscience. Grant Number: 2014-2015",

year = "2020",

month = jan,

day = "15",

doi = "10.1002/cbic.201900295",

language = "English",

volume = "21",

pages = "129--140",

journal = "ChemBioChem",

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Di Carluccio, C, Crisman, E, Manabe, Y, Forgione, RE, Lacetera, A, Amato, J, Pagano, B, Randazzo, A, Zampella, A, Lanzetta, R, Fukase, K, Molinaro, A, Crocker, PR, Martín-Santamaría, S, Marchetti, R & Silipo, A 2020, 'Characterisation of the Dynamic Interactions between Complex N-Glycans and Human CD22', ChemBioChem, vol. 21, no. 1-2, pp. 129-140. https://doi.org/10.1002/cbic.201900295

TY - JOUR

T1 - Characterisation of the Dynamic Interactions between Complex N-Glycans and Human CD22

AU - Di Carluccio, Cristina

AU - Crisman, Enrique

AU - Manabe, Yoshiyuki

AU - Forgione, Rosa Ester

AU - Lacetera, Alessandra

AU - Amato, Jussara

AU - Pagano, Bruno

AU - Randazzo, Antonio

AU - Zampella, Angela

AU - Lanzetta, Rosa

AU - Fukase, Koichi

AU - Molinaro, Antonio

AU - Crocker, Paul R.

AU - Martín-Santamaría, Sonsoles

AU - Marchetti, Roberta

AU - Silipo, Alba

N1 - Funding Information: H2020 Marie Skłodowska-Curie Actions. Grant Numbers: 642157, 814102; Mizutani Foundation for Glycoscience. Grant Number: 2014-2015

PY - 2020/1/15

Y1 - 2020/1/15

N2 - 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.

AB - 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.

KW - molecular recognition

KW - N-glycans

KW - NMR spectroscopy

KW - sialic acids

KW - Siglecs

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DO - 10.1002/cbic.201900295

M3 - Article

C2 - 31095840

AN - SCOPUS:85074393287

SN - 1439-4227

VL - 21

SP - 129

EP - 140

JO - ChemBioChem

JF - ChemBioChem

IS - 1-2

ER -

Characterisation of the Dynamic Interactions between Complex N-Glycans and Human CD22

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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