Anti-glycan monoclonal antibodies: Basic research and clinical applications

Gillmann, Kara M.; Temme, J. Sebastian; Marglous, Samantha; Brown, Clark E.; Gildersleeve, Jeffrey C.

doi:10.1016/j.cbpa.2023.102281

Cited by 4 publications

(4 citation statements)

References 95 publications

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“…Although there are some cases where the functional significance of a glycan structure for human health has been revealed, there remains a need to decipher the "glycocode" (or sugar code, as has been repeatedly proposed by H. Gabius since 1998) [125][126][127] for detecting several pathological processes. Figure 8 shows various analytical configurations for in situ detection of glycans (i.e., without the glycan being released from a protein backbone prior to the analysis) using lectins or glycan-binding proteins, such as antibodies which, unfortunately, are still in limited supply [128]. Without using an antibody monolayer during the glycoprofiling process, no tissue specificity can be guaranteed.…”

Section: Glycosylation Of Immunoglobulins In Diagnostics and Therapymentioning

confidence: 99%

Medical Relevance, State-of-the-Art and Perspectives of “Sweet Metacode” in Liquid Biopsy Approaches

Pinkeova,

Kosutova,

Jane

et al. 2024

Diagnostics

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This review briefly introduces readers to an area where glycomics meets modern oncodiagnostics with a focus on the analysis of sialic acid (Neu5Ac)-terminated structures. We present the biochemical perspective of aberrant sialylation during tumourigenesis and its significance, as well as an analytical perspective on the detection of these structures using different approaches for diagnostic and therapeutic purposes. We also provide a comparison to other established liquid biopsy approaches, and we mathematically define an early-stage cancer based on the overall prognosis and effect of these approaches on the patient’s quality of life. Finally, some barriers including regulations and quality of clinical validations data are discussed, and a perspective and major challenges in this area are summarised.

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Section: Glycosylation Of Immunoglobulins In Diagnostics and Therapymentioning

confidence: 99%

Medical Relevance, State-of-the-Art and Perspectives of “Sweet Metacode” in Liquid Biopsy Approaches

Pinkeova,

Kosutova,

Jane

et al. 2024

Diagnostics

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“…Moving beyond lectins, some efforts have focused on identifying or creating proteins that bind bacterial carbohydrate motifs [ 49 ]. Toward this end, Eddenden et al recently reported a catalytically-dead glycoside hydrolase probe that binds to the prominent biofilm polysaccharide poly-β−1,6- N -acetylglucosmine (PNAG) [ 50 ].…”

Section: Introductionmentioning

confidence: 99%

“…This probe allowed for monitoring of PNAG production during biofilm formation. Newly developed screens for anti-glycan antibodies [ 49 ] offer promise for identifying antibodies that bind distinctive bacterial glycan epitopes. Increasing the suite of bacterial glycan-binding proteins will provide an expanded toolkit for probing bacterial glycans and their functions in situ .…”

Section: Introductionmentioning

confidence: 99%

Chemical biology tools to probe bacterial glycans

Calles-Garcia,

Dube

2024

Current Opinion in Chemical Biology

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“…It has also been reported that various glycan antigens reflect the progression of the cellular pathology of human diseases, such as cancer, and infectious and inflammatory diseases 2,6,7 . As antibodies that specifically react with specific glycan structures on the cell surface are useful for the diagnosis and treatment of these diseases, we have been developing technology for efficiently obtaining anti-glycan monoclonal antibodies [7][8][9][10] .…”

mentioning

confidence: 99%

Serum components influence antibody reactivity to glycan and DNA antigens

Okuda,

Kato

2023

Sci Rep

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We previously generated three types of anti-glycan monoclonal IgM antibodies that react with certain structures on the glycans of glycosphingolipids and glycoproteins. As the nucleotide sequences for the variable regions of these IgM antibodies showed homology with those of anti-DNA antibodies deposited in public databases, we analyzed the reactivity of the anti-glycan IgM antibodies to DNA by ELISA. We found that anti-α2,6-sialyl LacNAc IgM in the supernatant of a hybridoma culture cross-reacted with DNA, and after purification of the IgM by zirconia column chromatography, the highly purified IgM showed increased cross-reactivity to DNA. As most of the contaminating bovine serum proteins in the culture supernatant were removed by the purification process, it is likely that a part of the removed components influences antibody reactivity to DNA. Purified anti-DNA antibodies prepared from lupus model NZB/W F1 and MRL/lpr mouse sera and normal human serum were then analyzed, and similar results showing increased reactivity to DNA were obtained. Furthermore, ELISA using these purified antibodies and various carbohydrate antigens showed that the antigen-binding specificity of these antibodies was altered by the purification process from serum-containing antibody preparations. Our results indicate that mammalian serum contains components that strongly influence antibody reactivity to carbohydrate antigens, including DNA.

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Anti-glycan monoclonal antibodies: Basic research and clinical applications

Cited by 4 publications

References 95 publications

Medical Relevance, State-of-the-Art and Perspectives of “Sweet Metacode” in Liquid Biopsy Approaches

Medical Relevance, State-of-the-Art and Perspectives of “Sweet Metacode” in Liquid Biopsy Approaches

Chemical biology tools to probe bacterial glycans

Serum components influence antibody reactivity to glycan and DNA antigens

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