Glycosylation of immunoglobulins is crucial for their function. For instance, N-glycans attached to the Fc domain of immunoglobulin G affect the interaction with Fc gamma and lectin receptors present on the cells of the immune system shaping the immune response triggered by these antibodies. Changes in antibody glycosylation status accompany many physiological and pathologic processes, such as ageing, pregnancy, autoimmune and inflammatory responses, and infectious diseases, cancers, etc. and can thus be used as diagnostic and prognostic biomarkers. Moreover, production of therapeutic monoclonal antibodies (mAbs) requires careful control over their glycan composition to ensure proper biological action, efficacy, and safety of these drugs. Understanding the regulation and functional consequences of heterogeneity of antibody glycosylation is essential for the field of immunology and necessary to develop new therapeutic and diagnostic markers.
Recently, great progress has been made in the field of glycobiology by the introduction of a wide spectrum of methods for glycoprofiling: from studying glycans of a single protein in high throughput to mass spectrometry imaging of tissue glycosylation. Recent work continues to investigate regulatory and functional aspects of the glycomes of IgG, IgA, and other antibody classes, including the glycosylation of antigen-specific antibodies. At the same time the importance of glycosylation of Ig receptors and complement proteins is widely recognized. Development of high-throughput glycosylation profiling has opened the road to the multi omics approach to study the biological pathways involved in glycan synthesis. All these studies help to elucidate the ways in which immunity works and to develop new therapeutic strategies.
The current Research Topic will cover studies that investigate the structural and functional implications of glycan micro- and macroheterogeneity on immunoglobulins and immunoglobulin receptors in health and disease. It will additionally address the role of glycans in receptor recognition and effector functions of antibodies, their biomarker potential, and the regulation of glycosylation.
We welcome research that elucidates the role of glycans in humoral immune responses performed in the fields of glycoproteomics and/or glycomics, genetics of antibody glycosylation, structural biology of immunoglobulins, their receptors and complement system.
• Glycosylation of antibodies in health and disease
• Isotype- and subclass-specific glycosylation of antibodies
• Role of glycans in antibody effector functions, receptor recognition, complement activation and immune response
• Antibody glycosylation and disease prediction / therapy, glycan biomarkers
• Regulation of antibody glycosylation at different cellular levels
• Importance and changes of antibody glycosylation of therapeutic antibodies in vivo
• Glycosylation of antibody receptors
Glycosylation of immunoglobulins is crucial for their function. For instance, N-glycans attached to the Fc domain of immunoglobulin G affect the interaction with Fc gamma and lectin receptors present on the cells of the immune system shaping the immune response triggered by these antibodies. Changes in antibody glycosylation status accompany many physiological and pathologic processes, such as ageing, pregnancy, autoimmune and inflammatory responses, and infectious diseases, cancers, etc. and can thus be used as diagnostic and prognostic biomarkers. Moreover, production of therapeutic monoclonal antibodies (mAbs) requires careful control over their glycan composition to ensure proper biological action, efficacy, and safety of these drugs. Understanding the regulation and functional consequences of heterogeneity of antibody glycosylation is essential for the field of immunology and necessary to develop new therapeutic and diagnostic markers.
Recently, great progress has been made in the field of glycobiology by the introduction of a wide spectrum of methods for glycoprofiling: from studying glycans of a single protein in high throughput to mass spectrometry imaging of tissue glycosylation. Recent work continues to investigate regulatory and functional aspects of the glycomes of IgG, IgA, and other antibody classes, including the glycosylation of antigen-specific antibodies. At the same time the importance of glycosylation of Ig receptors and complement proteins is widely recognized. Development of high-throughput glycosylation profiling has opened the road to the multi omics approach to study the biological pathways involved in glycan synthesis. All these studies help to elucidate the ways in which immunity works and to develop new therapeutic strategies.
The current Research Topic will cover studies that investigate the structural and functional implications of glycan micro- and macroheterogeneity on immunoglobulins and immunoglobulin receptors in health and disease. It will additionally address the role of glycans in receptor recognition and effector functions of antibodies, their biomarker potential, and the regulation of glycosylation.
We welcome research that elucidates the role of glycans in humoral immune responses performed in the fields of glycoproteomics and/or glycomics, genetics of antibody glycosylation, structural biology of immunoglobulins, their receptors and complement system.
• Glycosylation of antibodies in health and disease
• Isotype- and subclass-specific glycosylation of antibodies
• Role of glycans in antibody effector functions, receptor recognition, complement activation and immune response
• Antibody glycosylation and disease prediction / therapy, glycan biomarkers
• Regulation of antibody glycosylation at different cellular levels
• Importance and changes of antibody glycosylation of therapeutic antibodies in vivo
• Glycosylation of antibody receptors
