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Article ; Online: Impact of Siglecs on autoimmune diseases.

Brzezicka, Katarzyna Alicja / Paulson, James C

2022 Volume 90, Page(s) 101140

Abstract: Autoimmune diseases affect tens of millions of people just in the United States alone. Most of the available treatment options are aimed at reducing symptoms but do not lead to cures. Individuals affected with autoimmune diseases suffer from the ... ...

Abstract	Autoimmune diseases affect tens of millions of people just in the United States alone. Most of the available treatment options are aimed at reducing symptoms but do not lead to cures. Individuals affected with autoimmune diseases suffer from the imbalance between tolerogenic and immunogenic functions of their immune system. Often pathogenesis is mediated by autoreactive B and T cells that escape central tolerance and react against self-antigens attacking healthy tissues in the body. In recent years Siglecs, sialic-acid-binding immunoglobulin (Ig)-like lectins, have gained attention as immune checkpoints for therapeutic interventions to dampen excessive immune responses and to restore immune tolerance in autoimmune diseases. Many Siglecs function as inhibitory receptors suppressing activation signals in various immune cells through binding to sialic acid ligands as signatures of self. In this review, we highlight potential of Siglecs in suppressing immune responses causing autoimmune diseases. In particular, we cover the roles of CD22 and Siglec-G/Siglec-10 in regulating autoreactive B cell responses. We discuss several functions of Siglec-10 in the immune modulation of other immune cells, and the potential of therapeutic strategies for restoring immune tolerance by targeting Siglecs and expanding regulatory T cells. Finally, we briefly review efforts evaluating Siglec-based biomarkers to monitor autoimmune diseases.
MeSH term(s)	Humans ; Sialic Acid Binding Immunoglobulin-like Lectins/genetics ; Sialic Acid Binding Immunoglobulin-like Lectins/metabolism ; Sialic Acid Binding Ig-like Lectin 2/metabolism ; B-Lymphocytes/metabolism ; Autoimmune Diseases/therapy ; Autoimmune Diseases/metabolism ; N-Acetylneuraminic Acid/metabolism
Chemical Substances	Sialic Acid Binding Immunoglobulin-like Lectins ; Sialic Acid Binding Ig-like Lectin 2 ; N-Acetylneuraminic Acid (GZP2782OP0)
Language	English
Publishing date	2022-08-30
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	197640-0
ISSN	1872-9452 ; 0098-2997
ISSN (online)	1872-9452
ISSN	0098-2997
DOI	10.1016/j.mam.2022.101140
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Article ; Online: Targeting inhibitory Siglec-3 to suppress IgE-mediated human basophil degranulation.

Barshow, Suzanne M / Islam, Maidul / Commins, Scott / Macauley, Matthew S / Paulson, James C / Kulis, Michael D

The Journal of allergy and clinical immunology

2024

Abstract: Background: Sialic acid-binding immunoglobulin-like lectin-3 (Siglec-3 [CD33]) is a major Siglec expressed on human mast cells and basophils; engagement of CD33 leads to inhibition of cellular signaling via immunoreceptor tyrosine-based inhibitory ... ...

Abstract	Background: Sialic acid-binding immunoglobulin-like lectin-3 (Siglec-3 [CD33]) is a major Siglec expressed on human mast cells and basophils; engagement of CD33 leads to inhibition of cellular signaling via immunoreceptor tyrosine-based inhibitory motifs. Objective: We sought to inhibit human basophil degranulation by simultaneously recruiting inhibitory CD33 to the IgE-FcεRI complex by using monoclonal anti-IgE directly conjugated to CD33 ligand (CD33L). Methods: Direct and indirect basophil activation tests (BATs) were used to assess both antigen-specific (peanut) and antigen-nonspecific (polyclonal anti-IgE) stimulation. Whole blood from donors with allergy was used for direct BAT, whereas blood from donors with nonfood allergy was passively sensitized with plasma from donors with peanut allergy in the indirect BAT. Blood was incubated with anti-IgE-CD33L or controls for 1 hour or overnight and then stimulated with peanut, polyclonal anti-IgE, or N-formylmethionyl-leucyl-phenylalanine for 30 minutes. Degranulation was determined by measuring CD63 expression on the basophil surface by flow cytometry. Results: Incubation for 1 hour with anti-IgE-CD33L significantly reduced basophil degranulation after both allergen-induced (peanut) and polyclonal anti-IgE stimulation, with further suppression after overnight incubation with anti-IgE-CD33L. As expected, anti-IgE-CD33L did not block basophil degranulation due to N-formylmethionyl-leucyl-phenylalanine, providing evidence that this inhibition is IgE pathway-specific. Finally, CD33L is necessary for this suppression, as monoclonal anti-IgE without CD33L was unable to reduce basophil degranulation. Conclusions: Pretreating human basophils with anti-IgE-CD33L significantly suppressed basophil degranulation through the IgE-FcεRI complex. The ability to abrogate IgE-mediated basophil degranulation is of particular interest, as treatment with anti-IgE-CD33L before antigen exposure could have broad implications for the treatment of food, drug, and environmental allergies.
Language	English
Publishing date	2024-04-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	121011-7
ISSN	1097-6825 ; 1085-8725 ; 0091-6749
ISSN (online)	1097-6825 ; 1085-8725
ISSN	0091-6749
DOI	10.1016/j.jaci.2024.03.020
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Article ; Online: Siglecs as Immune Cell Checkpoints in Disease.

Duan, Shiteng / Paulson, James C

Annual review of immunology

2020 Volume 38, Page(s) 365–395

Abstract: Sialic acid-binding immunoglobulin-type lectins (Siglecs) are expressed on the majority of white blood cells of the immune system and play critical roles in immune cell signaling. Through recognition of sialic acid-containing glycans as ligands, they ... ...

Abstract	Sialic acid-binding immunoglobulin-type lectins (Siglecs) are expressed on the majority of white blood cells of the immune system and play critical roles in immune cell signaling. Through recognition of sialic acid-containing glycans as ligands, they help the immune system distinguish between self and nonself. Because of their restricted cell type expression and roles as checkpoints in immune cell responses in human diseases such as cancer, asthma, allergy, neurodegeneration, and autoimmune diseases they have gained attention as targets for therapeutic interventions. In this review we describe the Siglec family, its roles in regulation of immune cell signaling, current efforts to define its roles in disease processes, and approaches to target Siglecs for treatment of human disease.
MeSH term(s)	Animals ; Biomarkers ; Disease Susceptibility ; Humans ; Immune Checkpoint Proteins/genetics ; Immune Checkpoint Proteins/metabolism ; Immune System/immunology ; Immune System/metabolism ; Immunomodulation ; Lymphocytes/immunology ; Lymphocytes/metabolism ; Sialic Acid Binding Immunoglobulin-like Lectins/genetics ; Sialic Acid Binding Immunoglobulin-like Lectins/metabolism ; Signal Transduction
Chemical Substances	Biomarkers ; Immune Checkpoint Proteins ; Sialic Acid Binding Immunoglobulin-like Lectins
Language	English
Publishing date	2020-01-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	604953-9
ISSN	1545-3278 ; 0732-0582
ISSN (online)	1545-3278
ISSN	0732-0582
DOI	10.1146/annurev-immunol-102419-035900
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Article ; Online: Adaptation of influenza viruses to human airway receptors.

Thompson, Andrew J / Paulson, James C

The Journal of biological chemistry

2020 Volume 296, Page(s) 100017

Abstract: Through annual epidemics and global pandemics, influenza A viruses (IAVs) remain a significant threat to human health as the leading cause of severe respiratory disease. Within the last century, four global pandemics have resulted from the introduction ... ...

Abstract	Through annual epidemics and global pandemics, influenza A viruses (IAVs) remain a significant threat to human health as the leading cause of severe respiratory disease. Within the last century, four global pandemics have resulted from the introduction of novel IAVs into humans, with components of each originating from avian viruses. IAVs infect many avian species wherein they maintain a diverse natural reservoir, posing a risk to humans through the occasional emergence of novel strains with enhanced zoonotic potential. One natural barrier for transmission of avian IAVs into humans is the specificity of the receptor-binding protein, hemagglutinin (HA), which recognizes sialic-acid-containing glycans on host cells. HAs from human IAVs exhibit "human-type" receptor specificity, binding exclusively to glycans on cells lining the human airway where terminal sialic acids are attached in the α2-6 configuration (NeuAcα2-6Gal). In contrast, HAs from avian viruses exhibit specificity for "avian-type" α2-3-linked (NeuAcα2-3Gal) receptors and thus require adaptive mutations to bind human-type receptors. Since all human IAV pandemics can be traced to avian origins, there remains ever-present concern over emerging IAVs with human-adaptive potential that might lead to the next pandemic. This concern has been brought into focus through emergence of SARS-CoV-2, aligning both scientific and public attention to the threat of novel respiratory viruses from animal sources. In this review, we summarize receptor-binding adaptations underlying the emergence of all prior IAV pandemics in humans, maintenance and evolution of human-type receptor specificity in subsequent seasonal IAVs, and potential for future human-type receptor adaptation in novel avian HAs.
MeSH term(s)	Adaptation, Physiological ; Animals ; Binding Sites ; Biological Coevolution ; Birds/virology ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Hemagglutinin Glycoproteins, Influenza Virus/metabolism ; Humans ; Influenza A virus/chemistry ; Influenza A virus/genetics ; Influenza A virus/metabolism ; Influenza in Birds/epidemiology ; Influenza in Birds/transmission ; Influenza in Birds/virology ; Influenza, Human/epidemiology ; Influenza, Human/transmission ; Influenza, Human/virology ; Models, Molecular ; Pandemics ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Protein Binding ; Receptors, Virus/chemistry ; Receptors, Virus/genetics ; Receptors, Virus/metabolism ; Respiratory System/virology ; Sialic Acids/chemistry ; Sialic Acids/metabolism ; Species Specificity
Chemical Substances	Hemagglutinin Glycoproteins, Influenza Virus ; Polysaccharides ; Receptors, Virus ; Sialic Acids
Keywords	covid19
Language	English
Publishing date	2020-11-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.REV120.013309
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Article ; Conference proceedings ; Online: REGULATION OF TERMINAL GLYCOSYLATION

Svensson, Eric C. / Lee, Eryn Ujita / Livingston, Brian / Wen, Xiao-Hong / Weinstein, Jasminder / Paulson, James C.

2024

Abstract: Mammalian cell lines used for production of recombinant glycoproteins elaborate terminal glycosylation structures on N-linked and O-linked carbohydrate groupsthat are determined by the glycosyltransferases expressed by these cells. As many as twelve ... ...

Abstract	Mammalian cell lines used for production of recombinant glycoproteins elaborate terminal glycosylation structures on N-linked and O-linked carbohydrate groupsthat are determined by the glycosyltransferases expressed by these cells. As many as twelve glycosyltransferase cDNAs have now been cloned by a variety of strategies (1). By expressing these glycosyltransferase cDNAs incells not normally expressing them, it is now possible to alter the cellular glycosylation machinery to produce new terminal glycosylation sequences (2,3). This principle was demonstrated by expressing the rat B-galactoside 02,6 sialyltransferase (a2,6ST) cDNA in CHOcells, which are known notto express the product of this sialyltransferase. After selection for stable expression, these cells were shown to produce Nlinked carbohydrate groups with terminal 02,6 linked sialic acid, demonstrating an altered glycosylation machinery (2).
Language	English
Publishing date	2024-02-28
Publisher	GBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweig
Publishing country	de
Document type	Article ; Conference proceedings ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Adaptation of Influenza Viruses to Human Airway Receptors

Thompson, Andrew J / Paulson, James C

J. biol. chem

Abstract	Through annual epidemics and global pandemics, influenza A viruses (IAVs) remain a significant threat to human health as the leading cause of severe respiratory disease. Within the last century, four global pandemics have resulted from the introduction of novel IAVs into humans, with components of each originating from avian viruses. IAVs infect many avian species wherein they maintain a diverse natural reservoir, posing a risk to humans through the occasional emergence of novel strains with enhanced zoonotic potential. One natural barrier for transmission of avian IAVs into humans is the specificity of the receptor-binding protein, hemagglutinin (HA), that recognizes sialic acid-containing glycans on host cells. HAs from human IAVs exhibit "human-type" receptor specificity, binding exclusively to glycans on cells lining the human airway where terminal sialic acids are attached in the α2-6 configuration (NeuAcα2-6Gal). In contrast, HAs from avian viruses exhibit specificity for "avian-type" α2-3-linked (NeuAcα2-3Gal) receptors, and thus require adaptive mutations to bind human-type receptors. Since all human IAV pandemics can be traced to avian origins, there remains ever-present concern over emerging IAVs with human-adaptive potential that might lead to the next pandemic. This concern has been brought into focus through emergence of SARS-CoV-2, aligning both scientific and public attention to the threat of novel respiratory viruses from animal sources. In this review we summarize receptor-binding adaptations underlying the emergence of all prior IAV pandemics in humans, maintenance and evolution of human-type receptor specificity in subsequent seasonal IAVs, and potential for future human-type receptor adaptation in novel avian HAs.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #910220
Database	COVID19

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Article ; Online: Suppressing Immune Responses Using Siglec Ligand-Decorated Anti-receptor Antibodies.

Islam, Maidul / Arlian, Britni M / Pfrengle, Fabian / Duan, Shiteng / Smith, Scott A / Paulson, James C

Journal of the American Chemical Society

2022 Volume 144, Issue 21, Page(s) 9302–9311

Abstract: The sialic acid-binding immunoglobulin-type lectins (Siglecs) are expressed predominantly on white blood cells and participate in immune cell recognition of self. Most Siglecs contain cytoplasmic inhibitory immunoreceptor tyrosine-based inhibitory motifs ...

Abstract	The sialic acid-binding immunoglobulin-type lectins (Siglecs) are expressed predominantly on white blood cells and participate in immune cell recognition of self. Most Siglecs contain cytoplasmic inhibitory immunoreceptor tyrosine-based inhibitory motifs characteristic of inhibitory checkpoint co-receptors that suppress cell signaling when they are recruited to the immunological synapse of an activating receptor. Antibodies to activatory receptors typically activate immune cells by ligating the receptors on the cell surface. Here, we report that the conjugation of high affinity ligands of Siglecs to antibodies targeting activatory immune receptors can suppress receptor-mediated activation of immune cells. Indeed, B-cell activation by antibodies to the B-cell receptor IgD is dramatically suppressed by conjugation of anti-IgD with high affinity ligands of a B-cell Siglec CD22/Siglec-2. Similarly, degranulation of mast cells induced by antibodies to IgE, which ligate the IgE/FcεR1 receptor complex, is suppressed by conjugation of anti-IgE to high affinity ligands of a mast cell Siglec, CD33/Siglec-3 (CD33L). Moreover, the anti-IgE-CD33L suppresses anti-IgE-mediated systemic anaphylaxis of sensitized humanized mice and prevents anaphylaxis upon subsequent challenge with anti-IgE. The results demonstrate that attachment of ligands of inhibitory Siglecs to anti-receptor antibodies can suppress the activation of immune cells and modulate unwanted immune responses.
MeSH term(s)	Anaphylaxis ; Animals ; Immunoglobulin E ; Ligands ; Lymphocyte Activation ; Mice ; Sialic Acid Binding Immunoglobulin-like Lectins
Chemical Substances	Ligands ; Sialic Acid Binding Immunoglobulin-like Lectins ; Immunoglobulin E (37341-29-0)
Language	English
Publishing date	2022-05-20
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.2c00922
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Article ; Online: Suppression of Autoimmune Rheumatoid Arthritis with Hybrid Nanoparticles That Induce B and T Cell Tolerance to Self-Antigen.

Brzezicka, Katarzyna A / Arlian, Britni M / Wang, Shengyang / Olmer, Merissa / Lotz, Martin / Paulson, James C

ACS nano

2022 Volume 16, Issue 12, Page(s) 20206–20221

Abstract: Autoimmune diseases affect over 4% of the world's population. Treatments are generally palliative or use broad spectrum immunosuppressants to reduce symptoms and disease progression. In some diseases, antibodies generated to a single autoantigen are the ... ...

Abstract	Autoimmune diseases affect over 4% of the world's population. Treatments are generally palliative or use broad spectrum immunosuppressants to reduce symptoms and disease progression. In some diseases, antibodies generated to a single autoantigen are the major cause of pathogenic inflammation, suggesting that treatments to induce tolerance to the autoantigen could be therapeutic. Here we report the development of hybrid nanoparticles (NPs) that induce tolerance in both T cells and B cells. The NPs comprise a lipid monolayer encapsulating a PLGA core loaded with rapamycin that promotes development of regulatory T cells (Tregs). The lipid monolayer displays the protein antigen and a ligand of the B cell inhibitory co-receptor CD22 (CD22L) that act together to suppress activation of B cells recognizing the antigen. We demonstrate that the hybrid NPs decorated with ovalbumin (OVA) elicit tolerance to OVA in naı̈ve mice, as judged by low OVA-specific antibody titers after the challenge. In the K/BxN mouse model of rheumatoid arthritis caused by B and T cell-dependent responses to the self-antigen glucose-6-phosphate-isomerase (GPI), we show that GPI hybrid NPs delay development of disease, with some treated mice remaining arthritis-free for 300 days. We provide evidence that the mechanism of rheumatoid arthritis suppression involves induction of B cell tolerance, as measured by low anti-GPI antibodies and decreased plasma cell populations, and T cell tolerance, as measured by increased Tregs. The results show the potential of this versatile NP platform for inducing immune tolerance to a self-antigen and suppressing autoimmune disease.
MeSH term(s)	Mice ; Animals ; Autoantigens ; Polylactic Acid-Polyglycolic Acid Copolymer ; Autoimmune Diseases ; Immune Tolerance ; Arthritis, Rheumatoid/drug therapy ; Nanoparticles ; Lipids ; Ovalbumin
Chemical Substances	Autoantigens ; Polylactic Acid-Polyglycolic Acid Copolymer (1SIA8062RS) ; Lipids ; Ovalbumin (9006-59-1)
Language	English
Publishing date	2022-11-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1936-086X
ISSN (online)	1936-086X
DOI	10.1021/acsnano.2c05643
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: CD22 Ligands on a Natural N-Glycan Scaffold Efficiently Deliver Toxins to B-Lymphoma Cells.

Peng, Wenjie / Paulson, James C

Journal of the American Chemical Society

2017 Volume 139, Issue 36, Page(s) 12450–12458

Abstract: CD22 is a sialic acid-binding immunoglobulin-like lectin (Siglec) that is highly expressed on B-cells and B cell lymphomas, and is a validated target for antibody and nanoparticle based therapeutics. However, cell targeted therapeutics are limited by ... ...

Abstract	CD22 is a sialic acid-binding immunoglobulin-like lectin (Siglec) that is highly expressed on B-cells and B cell lymphomas, and is a validated target for antibody and nanoparticle based therapeutics. However, cell targeted therapeutics are limited by their complexity, heterogeneity, and difficulties in production. We describe here a chemically defined natural N-linked glycan scaffold that displays high affinity CD22 glycan ligands and outcompetes the natural ligand for the receptor, resulting in single molecule binding to CD22 and endocytosis into cells. Binding affinity is increased by up to 1500-fold compared to the monovalent ligand, while maintaining the selectivity for hCD22 over other Siglecs. Conjugates of these multivalent ligands with auristatin and saporin toxins are efficiently internalized via hCD22 resulting in killing of B-cell lymphoma cells. This single molecule ligand targeting strategy represents an alternative to antibody- and nanoparticle-mediated approaches for delivery of agents to cells expressing CD22 and other Siglecs.
MeSH term(s)	Animals ; Antineoplastic Agents/administration & dosage ; CHO Cells ; Cell Line, Tumor ; Cricetulus ; Endocytosis ; Humans ; Ligands ; Lymphoma, B-Cell/drug therapy ; Lymphoma, B-Cell/metabolism ; Lymphoma, B-Cell/pathology ; Mice ; Polysaccharides/metabolism ; Sialic Acid Binding Ig-like Lectin 2/metabolism
Chemical Substances	Antineoplastic Agents ; CD22 protein, human ; Ligands ; Polysaccharides ; Sialic Acid Binding Ig-like Lectin 2
Language	English
Publishing date	2017-08-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.7b03208
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Article ; Online: Unraveling Molecular Recognition of Glycan Ligands by Siglec-9 via NMR Spectroscopy and Molecular Dynamics Modeling.

Atxabal, Unai / Nycholat, Corwin / Pröpster, Johannes M / Fernández, Andrea / Oyenarte, Iker / Lenza, Maria Pia / Franconetti, Antonio / Soares, Cátia O / Coelho, Helena / Marcelo, Filipa / Schubert, Mario / Paulson, James C / Jiménez-Barbero, Jesús / Ereño-Orbea, June

ACS chemical biology

2024 Volume 19, Issue 2, Page(s) 483–496

Abstract: Human sialic-acid-binding immunoglobulin-like lectin-9 (Siglec-9) is a glycoimmune checkpoint receptor expressed on several immune cells. Binding of Siglec-9 to sialic acid containing glycans (sialoglycans) is well documented to modulate its functions as ...

Abstract	Human sialic-acid-binding immunoglobulin-like lectin-9 (Siglec-9) is a glycoimmune checkpoint receptor expressed on several immune cells. Binding of Siglec-9 to sialic acid containing glycans (sialoglycans) is well documented to modulate its functions as an inhibitory receptor. Here, we first assigned the amino acid backbone of the Siglec-9 V-set domain (Siglec-9
MeSH term(s)	Humans ; Molecular Dynamics Simulation ; N-Acetylneuraminic Acid ; Antigens, Differentiation, Myelomonocytic/metabolism ; Sialic Acid Binding Immunoglobulin-like Lectins/metabolism ; Polysaccharides/metabolism ; Magnetic Resonance Spectroscopy ; Ligands
Chemical Substances	N-Acetylneuraminic Acid (GZP2782OP0) ; Antigens, Differentiation, Myelomonocytic ; Sialic Acid Binding Immunoglobulin-like Lectins ; Polysaccharides ; Ligands
Language	English
Publishing date	2024-02-07
Publishing country	United States
Document type	Journal Article
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.3c00664
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