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Article ; Online: Flow Cytometry-Based Detection of Siglec Ligands.

Schmidt, Edward N / Jung, Jaesoo / Macauley, Matthew S

Methods in molecular biology (Clifton, N.J.)

2023 Volume 2657, Page(s) 181–193

Abstract: Siglecs are a family of immunomodulatory cell surface receptors present on white blood cells. Binding to cell surface sialic acid-containing glycans modulates the proximity of Siglecs to other receptors that they regulate. This proximity is key to ... ...

Abstract	Siglecs are a family of immunomodulatory cell surface receptors present on white blood cells. Binding to cell surface sialic acid-containing glycans modulates the proximity of Siglecs to other receptors that they regulate. This proximity is key to enabling signaling motifs on the cytosolic domain of Siglecs to modulate immune responses. Given the important roles that Siglecs play in helping to maintain immune homeostasis, a better understanding of their glycan ligands is needed to elucidate their roles in health and disease. A common approach for probing Siglec ligands on cells is to use soluble versions of the recombinant Siglecs in conjunction with flow cytometry. Flow cytometry has many advantages in enabling the relative levels of Siglec ligands between cell types to be rapidly quantified. Here, a step-by-step protocol is described on how to detect Siglec ligands most sensitively and accurately on cells by flow cytometry.
MeSH term(s)	Sialic Acid Binding Immunoglobulin-like Lectins ; Flow Cytometry ; Ligands ; Polysaccharides ; N-Acetylneuraminic Acid/metabolism
Chemical Substances	Sialic Acid Binding Immunoglobulin-like Lectins ; Ligands ; Polysaccharides ; N-Acetylneuraminic Acid (GZP2782OP0)
Language	English
Publishing date	2023-05-06
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-3151-5_13
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Article ; Online: CD33 isoforms in microglia and Alzheimer's disease: Friend and foe.

Eskandari-Sedighi, Ghazaleh / Jung, Jaesoo / Macauley, Matthew S

Molecular aspects of medicine

2022 Volume 90, Page(s) 101111

Abstract: Alzheimer's disease (AD) is the most common form of neurodegenerative disease and is considered the main cause of dementia worldwide. Genome-wide association studies combined with integrated analysis of functional datasets support a critical role for ... ...

Abstract	Alzheimer's disease (AD) is the most common form of neurodegenerative disease and is considered the main cause of dementia worldwide. Genome-wide association studies combined with integrated analysis of functional datasets support a critical role for microglia in AD pathogenesis, identifying them as important potential therapeutic targets. The ability of immunomodulatory receptors on microglia to control the response to pathogenic amyloid-β aggregates has gained significant interest. Siglec-3, also known as CD33, is one of these immunomodulatory receptors expressed on microglia that has been identified as an AD susceptibility factor. Here, we review recent advances made in understanding the multifaceted roles that CD33 plays in microglia with emphasis on two human-specific CD33 isoforms that differentially correlate with AD susceptibility. We also describe several different therapeutic approaches for targeting CD33 that have been advanced for the purpose of skewing microglial cell responses.
MeSH term(s)	Humans ; Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Microglia/pathology ; Neurodegenerative Diseases/pathology ; Genome-Wide Association Study ; Protein Isoforms/genetics ; Sialic Acid Binding Ig-like Lectin 3/genetics
Chemical Substances	Protein Isoforms ; CD33 protein, human ; Sialic Acid Binding Ig-like Lectin 3
Language	English
Publishing date	2022-08-05
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	197640-0
ISSN	1872-9452 ; 0098-2997
ISSN (online)	1872-9452
ISSN	0098-2997
DOI	10.1016/j.mam.2022.101111
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Article ; Online: Coordinated roles for glycans in regulating the inhibitory function of CD22 on B cells.

Enterina, Jhon R / Jung, Jaesoo / Macauley, Matthew S

Biomedical journal

2019 Volume 42, Issue 4, Page(s) 218–232

Abstract: CD22 is an inhibitory B cell co-receptor that recognizes sialic acid-containing glycoconjugates as ligands. Interactions with its glycan ligands are key to regulating the ability of CD22 to modulate B cell function, the most widely explored of which is ... ...

Abstract	CD22 is an inhibitory B cell co-receptor that recognizes sialic acid-containing glycoconjugates as ligands. Interactions with its glycan ligands are key to regulating the ability of CD22 to modulate B cell function, the most widely explored of which is antagonizing B cell receptor (BCR) signaling. Most importantly, interactions of CD22 with ligands on the same cell (cis) control the organization of CD22 on the cell surface, which minimizes co-localization with the BCR. In contrast with the modest ability of CD22 to intrinsically dampen BCR signaling, glycan ligands presented on another cell (trans) along with an antigen drawn CD22 and the BCR together within an immunological synapse, strongly inhibiting BCR signaling. New concepts are emerging for how CD22 controls B cell function, such as changes in glycosylation at different stages of B cell differentiation, specifically on GC B cells. Related to these changes, new players, such galectin-9, have been discovered that regulate cell surface nanoclusters of CD22. Roles of glycan ligands in controlling CD22 are the primary focus of this review as we highlight the ability of CD22 to modulate B cell function.
MeSH term(s)	Animals ; B-Lymphocytes/immunology ; Humans ; Ligands ; Lymphocyte Activation/immunology ; Polysaccharides/immunology ; Receptors, Antigen, B-Cell/immunology ; Sialic Acid Binding Ig-like Lectin 2/immunology
Chemical Substances	Ligands ; Polysaccharides ; Receptors, Antigen, B-Cell ; Sialic Acid Binding Ig-like Lectin 2
Language	English
Publishing date	2019-09-16
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2698541-X
ISSN	2320-2890 ; 2319-4170
ISSN (online)	2320-2890
ISSN	2319-4170
DOI	10.1016/j.bj.2019.07.010
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Article ; Online: Mass Spectrometry-Based Shotgun Glycomics for Discovery of Natural Ligands of Glycan-Binding Proteins.

Park, Heajin / Jung, Jaesoo / Rodrigues, Emily / Kitova, Elena N / Macauley, Matthew S / Klassen, John S

Analytical chemistry

2020 Volume 92, Issue 20, Page(s) 14012–14020

Abstract: Glycans attached to lipids and membrane-bound and secreted proteins and peptides mediate many important physiological and pathophysiological processes through interactions with glycan-binding proteins (GBPs). However, uncovering functional glycan ligands ...

Abstract	Glycans attached to lipids and membrane-bound and secreted proteins and peptides mediate many important physiological and pathophysiological processes through interactions with glycan-binding proteins (GBPs). However, uncovering functional glycan ligands is challenging due to the large number of naturally occurring glycan structures, the limited availability of glycans in their purified form, the low affinities of GBP-glycan interactions, and limitations in existing binding assays. This work explores the application of catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS) for screening libraries of
MeSH term(s)	Agglutinins/chemistry ; Agglutinins/metabolism ; Chromatography, High Pressure Liquid ; Glycomics/methods ; Humans ; Ligands ; Plant Lectins/chemistry ; Plant Lectins/metabolism ; Polysaccharides/analysis ; Polysaccharides/metabolism ; Protein Binding ; Sambucus nigra/metabolism ; Sialic Acid Binding Ig-like Lectin 2/chemistry ; Sialic Acid Binding Ig-like Lectin 2/metabolism ; Spectrometry, Mass, Electrospray Ionization
Chemical Substances	Agglutinins ; CD22 protein, human ; Ligands ; Plant Lectins ; Polysaccharides ; Sialic Acid Binding Ig-like Lectin 2
Language	English
Publishing date	2020-10-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.0c02931
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Article: Mass Spectrometry-Based Shotgun Glycomics for Discovery of Natural Ligands of Glycan-Binding Proteins

Park, Heajin / Jung, Jaesoo / Rodrigues, Emily / Kitova, Elena N / Macauley, Matthew S / Klassen, John S

Analytical chemistry. 2020 Sept. 16, v. 92, no. 20

2020

Abstract	Glycans attached to lipids and membrane-bound and secreted proteins and peptides mediate many important physiological and pathophysiological processes through interactions with glycan-binding proteins (GBPs). However, uncovering functional glycan ligands is challenging due to the large number of naturally occurring glycan structures, the limited availability of glycans in their purified form, the low affinities of GBP–glycan interactions, and limitations in existing binding assays. This work explores the application of catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS) for screening libraries of N-glycans derived from natural sources. The assay was tested by screening a small-defined library of complex N-glycans at equimolar concentrations against plant and human GBPs with known specificities for either α2-3- or α2-6-linked sialosides, with affinities in the millimolar to micromolar range. Validation experiments, performed in negative ion mode, revealed that bound N-glycan ligands are readily released, as intact deprotonated ions, from GBPs in the gas phase using collision-induced dissociation. Moreover, the relative abundances of the released ligands closely match their solution affinities. The results obtained for a natural N-glycan library produced from cultured immune cells serve to highlight the ease with which CaR-ESI-MS can screen complex mixtures of N-glycans for interactions. Additionally, scaling the relative abundances of released glycan ligands according to their relative abundances in solution, as determined by hydrophilic interaction–ultrahigh-performance liquid chromatography of the fluorescently labeled library, allows the relative affinities of glycan ligands to be ranked.
Keywords	analytical chemistry ; dissociation ; electrospray ionization mass spectrometry ; glycomics ; humans ; hydrophilicity ; ligands ; liquid chromatography ; peptides ; polysaccharides
Language	English
Dates of publication	2020-0916
Size	p. 14012-14020.
Publishing place	American Chemical Society
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.0c02931
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Article ; Online: Coordinated changes in glycosylation regulate the germinal center through CD22.

Enterina, Jhon R / Sarkar, Susmita / Streith, Laura / Jung, Jaesoo / Arlian, Britni M / Meyer, Sarah J / Takematsu, Hiromu / Xiao, Changchun / Baldwin, Troy A / Nitschke, Lars / Shlomchick, Mark J / Paulson, James C / Macauley, Matthew S

Cell reports

2022 Volume 38, Issue 11, Page(s) 110512

Abstract: Germinal centers (GCs) are essential for antibody affinity maturation. GC B cells have a unique repertoire of cell surface glycans compared with naive B cells, yet functional roles for changes in glycosylation in the GC have yet to be ascribed. Detection ...

Abstract	Germinal centers (GCs) are essential for antibody affinity maturation. GC B cells have a unique repertoire of cell surface glycans compared with naive B cells, yet functional roles for changes in glycosylation in the GC have yet to be ascribed. Detection of GCs by the antibody GL7 reflects a downregulation in ligands for CD22, an inhibitory co-receptor of the B cell receptor. To test a functional role for downregulation of CD22 ligands in the GC, we generate a mouse model that maintains CD22 ligands on GC B cells. With this model, we demonstrate that glycan remodeling plays a critical role in the maintenance of B cells in the GC. Sustained expression of CD22 ligands induces higher levels of apoptosis in GC B cells, reduces memory B cell and plasma cell output, and delays affinity maturation of antibodies. These defects are CD22 dependent, demonstrating that downregulation of CD22 ligands on B cells plays a critical function in the GC.
MeSH term(s)	Animals ; B-Lymphocytes ; Germinal Center ; Glycosylation ; Ligands ; Mice ; Polysaccharides/metabolism ; Receptors, Antigen, B-Cell/metabolism
Chemical Substances	Ligands ; Polysaccharides ; Receptors, Antigen, B-Cell
Language	English
Publishing date	2022-03-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.110512
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Article ; Online: Mass Spectrometry-Based Shotgun Glycomics Using Labeled Glycan Libraries.

Bui, Duong T / Jung, Jaesoo / Kitova, Elena N / Li, Zhixiong / Willows, Steven D / Boddington, Marie E / Kitov, Pavel I / Mason, Andrew L / Capicciotti, Chantelle J / Mahal, Lara K / Macauley, Matthew S / Klassen, John S

Analytical chemistry

2022 Volume 94, Issue 12, Page(s) 4997–5005

Abstract: Mass spectrometry-based shotgun glycomics (MS-SG) is a rapid, sensitive, label-, and immobilization-free approach for the discovery of natural ligands of glycan-binding proteins (GBPs). To perform MS-SG, natural libraries of glycans derived from ... ...

Abstract	Mass spectrometry-based shotgun glycomics (MS-SG) is a rapid, sensitive, label-, and immobilization-free approach for the discovery of natural ligands of glycan-binding proteins (GBPs). To perform MS-SG, natural libraries of glycans derived from glycoconjugates in cells or tissues are screened against a target GBP using catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS). Because glycan concentrations are challenging to determine, ligand affinities cannot be directly measured. In principle, relative affinities can be ranked by combining CaR-ESI-MS data with relative concentrations established by hydrophilic interaction liquid chromatography (HILIC) performed on the fluorophore-labeled glycan library. To validate this approach, as well as the feasibility of performing CaR-ESI-MS directly on labeled glycans, libraries of labeled
MeSH term(s)	Carrier Proteins/metabolism ; Chromatography, Liquid ; Fluorescent Dyes/chemistry ; Glycomics/methods ; Humans ; Ligands ; Polysaccharides/chemistry ; Proteins/metabolism ; Spectrometry, Mass, Electrospray Ionization/methods
Chemical Substances	Carrier Proteins ; Fluorescent Dyes ; Ligands ; Polysaccharides ; Proteins
Language	English
Publishing date	2022-03-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.1c04779
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Article: Mass Spectrometry-Based Shotgun Glycomics Using Labeled Glycan Libraries

Bui, Duong T. / Jung, Jaesoo / Kitova, Elena N. / Li, Zhixiong / Willows, Steven D. / Boddington, Marie E. / Kitov, Pavel I. / Mason, Andrew L. / Capicciotti, Chantelle J. / Mahal, Lara K. / Macauley, Matthew S. / Klassen, John S.

Analytical chemistry. 2022 Mar. 18, v. 94, no. 12

2022

Abstract	Mass spectrometry-based shotgun glycomics (MS-SG) is a rapid, sensitive, label-, and immobilization-free approach for the discovery of natural ligands of glycan-binding proteins (GBPs). To perform MS-SG, natural libraries of glycans derived from glycoconjugates in cells or tissues are screened against a target GBP using catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS). Because glycan concentrations are challenging to determine, ligand affinities cannot be directly measured. In principle, relative affinities can be ranked by combining CaR-ESI-MS data with relative concentrations established by hydrophilic interaction liquid chromatography (HILIC) performed on the fluorophore-labeled glycan library. To validate this approach, as well as the feasibility of performing CaR-ESI-MS directly on labeled glycans, libraries of labeled N-glycans extracted from the human monocytic U937 cells or intestinal tissues were labeled with 2-aminobenzamide (2-AB), 2-aminobenzoic acid (2-AA), or procainamide (proA). The libraries were screened against plant and human GBPs with known specificities for α2-3- and α2-6-linked sialosides and quantified by HILIC. Dramatic differences, in some cases, were found for affinity rankings obtained with libraries labeled with different fluorophores, as well as those produced using the combined unlabeled/labeled library approach. The origin of these differences could be explained by differential glycan labeling efficiencies, the impact of specific labels on glycan affinities for the GBPs, and the relative efficiency of release of ligands from GBPs in CaR-ESI-MS. Overall, the results of this study suggest that the 2-AB(CaR-ESI-MS)/2-AB(HILIC) combination provides the most reliable description of the binding specificities of GBPs for N-glycans and is recommended for MS-SG applications.
Keywords	analytical chemistry ; electrospray ionization mass spectrometry ; fluorescent dyes ; glycoconjugates ; glycomics ; humans ; hydrophilic interaction chromatography ; intestines ; ligands ; polysaccharides
Language	English
Dates of publication	2022-0318
Size	p. 4997-5005.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.1c04779
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Article ; Online: The CD33 short isoform is a gain-of-function variant that enhances Aβ

Bhattacherjee, Abhishek / Jung, Jaesoo / Zia, Sameera / Ho, Madelene / Eskandari-Sedighi, Ghazaleh / St Laurent, Chris D / McCord, Kelli A / Bains, Arjun / Sidhu, Gaurav / Sarkar, Susmita / Plemel, Jason R / Macauley, Matthew S

Molecular neurodegeneration

2021 Volume 16, Issue 1, Page(s) 19

Abstract: Background: CD33 is genetically linked to Alzheimer's disease (AD) susceptibility through differential expression of isoforms in microglia. The role of the human CD33 short isoform (hCD33m), preferentially encoded by an AD-protective CD33 allele ( ... ...

Abstract	Background: CD33 is genetically linked to Alzheimer's disease (AD) susceptibility through differential expression of isoforms in microglia. The role of the human CD33 short isoform (hCD33m), preferentially encoded by an AD-protective CD33 allele (rs12459419T), is unknown. Here, we test whether hCD33m represents a loss-of-function or gain-of-function variant. Methods: We have developed two models to test the role of hCD33m. The first is a new strain of transgenic mice expressing hCD33m in the microglial cell lineage. The second is U937 cells where the CD33 gene was disrupted by CRISPR/Cas9 and complemented with different variants of hCD33. Primary microglia and U937 cells were tested in phagocytosis assays and single cell RNA sequencing (scRNAseq) was carried out on the primary microglia. Furthermore, a new monoclonal antibody was developed to detect hCD33m more efficiently. Results: In both primary microglia and U937 cells, we find that hCD33m enhances phagocytosis. This contrasts with the human CD33 long isoform (hCD33M) that represses phagocytosis, as previously demonstrated. As revealed by scRNAseq, hCD33m Conclusions: These results provide strong support that hCD33m represents a gain-of-function isoform and offers insight into what it may take to therapeutically capture the AD-protective CD33 allele.
MeSH term(s)	Alleles ; Amyloid beta-Peptides/metabolism ; Animals ; CRISPR-Cas Systems ; Crosses, Genetic ; Female ; Gain of Function Mutation ; Gene Editing ; Gene Regulatory Networks ; Genes, Immediate-Early ; Humans ; Male ; Mice, Inbred C57BL ; Mice, Transgenic ; Microglia/physiology ; Peptide Fragments/metabolism ; Phagocytosis/genetics ; Polysaccharides/metabolism ; Protein Isoforms/genetics ; Protein Isoforms/physiology ; RNA-Seq ; Sialic Acid Binding Ig-like Lectin 3/antagonists & inhibitors ; Sialic Acid Binding Ig-like Lectin 3/genetics ; Sialic Acid Binding Ig-like Lectin 3/physiology ; Single-Cell Analysis ; U937 Cells ; Mice
Chemical Substances	Amyloid beta-Peptides ; CD33 protein, human ; Peptide Fragments ; Polysaccharides ; Protein Isoforms ; Sialic Acid Binding Ig-like Lectin 3 ; amyloid beta-protein (1-42)
Language	English
Publishing date	2021-03-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2244557-2
ISSN	1750-1326 ; 1750-1326
ISSN (online)	1750-1326
ISSN	1750-1326
DOI	10.1186/s13024-021-00443-6
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Article ; Online: Carbohydrate Sulfation As a Mechanism for Fine-Tuning Siglec Ligands.

Jung, Jaesoo / Enterina, Jhon R / Bui, Duong T / Mozaneh, Fahima / Lin, Po-Han / Nitin / Kuo, Chu-Wei / Rodrigues, Emily / Bhattacherjee, Abhishek / Raeisimakiani, Parisa / Daskhan, Gour C / St Laurent, Chris D / Khoo, Kay-Hooi / Mahal, Lara K / Zandberg, Wesley F / Huang, Xuefei / Klassen, John S / Macauley, Matthew S

ACS chemical biology

2021 Volume 16, Issue 11, Page(s) 2673–2689

Abstract: The immunomodulatory family of Siglecs recognizes sialic acid-containing glycans as " ...

Abstract	The immunomodulatory family of Siglecs recognizes sialic acid-containing glycans as "
MeSH term(s)	Carbohydrate Metabolism ; Cell Line ; Down-Regulation ; Humans ; Ligands ; Mass Spectrometry ; N-Acetylneuraminic Acid/metabolism ; Neoplasms/metabolism ; Protein Binding ; Protein Processing, Post-Translational ; Sialic Acid Binding Immunoglobulin-like Lectins/metabolism ; Sulfates/metabolism ; Up-Regulation
Chemical Substances	Ligands ; Sialic Acid Binding Immunoglobulin-like Lectins ; Sulfates ; N-Acetylneuraminic Acid (GZP2782OP0)
Language	English
Publishing date	2021-10-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.1c00501
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