A Guide to Monoclonal Antibodies Directed to Glycotopes

Kannagi, Reiji; Hakomori, Sen‐itiroh

doi:10.1007/978-1-4615-1267-7_38

Cited by 34 publications

(28 citation statements)

References 211 publications

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“…The problem is particularly important in view of the potential immunogenicity of pharmaceutical recombinant glycoproteins produced in transgenic plants [36]. Many monoclonal anti-carbohydrate antibodies have been obtained, and most of which are directed against oligosaccharide structures typical for glycosphingolipids [37]. Several 'glycotopes' are typical for glycoproteins and some epitopes are present in N-and O-glycans as well, and also in glycosphingolipids.…”

Section: Glycosidic and Glycopeptidic Epitopes Of Glycoproteinsmentioning

confidence: 99%

“…Therefore, anticarbohydrate antibodies are not specific for a defined glycoprotein, because they usually recognize their target epitopes in different antigens, irrespective of the glycan core structure and its carrier. However, anti-carbohydrate antibodies specific for the same structure may differ in fine specificity, since they recognize different fragments or sides of the target structure [37]. Another type of carbohydrate epitopes are ThomsenFriedenreich (TF) and Tn antigens (table 1) which represent core structures of O-glycans present in erythrocyte glycophorins and other mucin-type glycoproteins.…”

Section: Glycosidic and Glycopeptidic Epitopes Of Glycoproteinsmentioning

confidence: 99%

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The role of glycosylation in protein antigenic properties

Lisowska¹

2002

Cellular and Molecular Life Sciences (CMLS)

101

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Glycosylation of proteins is a common event and contributes to protein antigenic properties. Most data have been obtained from model studies on glycoprotens with well-defined structure or synthetic glycopeptides and their respective monoclonal antibodies. Antibodies raised against glycoprotein antigens may be specific for their carbohydrate units which are recognized irrespective of the protein carrier (carbohydrate epitopes), or in the context of the adjacent amino acid residues (glycopeptidic epitopes). Conformation or proper exposure of peptidic epitopes of glycoproteins is also frequently modulated by glycosylation due to intramolecular carbohydrate-protein interactions. The effects of glycosylation are broad: glycosylation may 'inactivate' the peptidic epitope or may be required for its reactivity with the antibody, depending on the structure of the antigenic site and antibody fine specificity. Evidence is increasing that similar effects of glycosylation pertain to T cell-dependent cellular immune responses. Glycosylated peptides can be bound and presented by MHC class I or II molecules and elicit glycopeptide-specific T cell clones.

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Section: Glycosidic and Glycopeptidic Epitopes Of Glycoproteinsmentioning

confidence: 99%

Section: Glycosidic and Glycopeptidic Epitopes Of Glycoproteinsmentioning

confidence: 99%

The role of glycosylation in protein antigenic properties

Lisowska¹

2002

Cellular and Molecular Life Sciences (CMLS)

101

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“…Human immunoglobulin (Ig) G1 isotype is commonly used, because it can mediate multiple effector functions, including antibody-dependent cellular cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), and direct killing activity, including apoptosis. 11,12) Thus far, a number of anti-Tn IgG and IgM antibodies have been generated, [13][14][15][16][17] and the anti-tumor activities of some already reported. 14,16,18) However, viability of anti-Tn monoclonal antibody for cancer immunotherapy has not been well validated, since data are mainly limited to in vitro assays with murine antibodies.…”

mentioning

confidence: 99%

Mouse-Human Chimeric Anti-Tn IgG1 Induced Anti-tumor Activity against Jurkat Cells in Vitro and in Vivo

Ando¹,

Matsushita²,

Wakitani³

et al. 2008

Biological & Pharmaceutical Bulletin

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“…Note that binding of CD22-Fc to B-lymphocytes is significantly reduced by the KN343 antibody, but not by the GL7 antibody. Adopted from reference [12] comprehensive listing of anti-oligosaccharide antibodies may be found in reference [15].…”

Section: Remarks and Conclusionmentioning

confidence: 99%

Anti-oligosaccharide antibodies as tools for studying sulfated sialoglycoconjugate ligands for siglecs and selectins

2008

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Several sulfated sialoglycoconjugates have recently been shown to serve as ligands for selectins and siglecs. For instance, alpha2-->3 sialylated 6-sulfo-Lewis x was found to serve as a ligand for selectins on skin-homing helper memory T cells, and alpha2-->6 sialylated 6-sulfo-LacNAc to be a preferred ligand for CD22/siglec-2 on human naïve B cells. Monoclonal antibodies specific to sulfated sialoglycoconjugates are effective tools to dissect these ligands on minor subsets of human leukocytes.

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A Guide to Monoclonal Antibodies Directed to Glycotopes

Cited by 34 publications

References 211 publications

The role of glycosylation in protein antigenic properties

The role of glycosylation in protein antigenic properties

Mouse-Human Chimeric Anti-Tn IgG1 Induced Anti-tumor Activity against Jurkat Cells in Vitro and in Vivo

Anti-oligosaccharide antibodies as tools for studying sulfated sialoglycoconjugate ligands for siglecs and selectins

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