Immunoglobulins (Igs) are co- and post-translationally modified by oligosaccharides (glycans). Ig glycans strongly impact structural and functional properties. Ig glycosylation differences may have a major impact on Fc receptor- and complement-mediated immune responses. For example, IgG Fc glycosylation is a critical element in the activation of neutrophils by autoantibodies, characteristic of anti-neutrophil cytoplasmic antibody-associated vasculitis. Furthermore, occurrence of N-glycosylation in the hypervariable domain of IgG was linked to Anti-Citrullinated Protein Antibody-positive Rheumatoid Arthritis and was suggested to increase survival of autoreactive B-cells.
Inter-individual variability of IgG glycosylation is large, but it is very stable within an individual under homeostasis. Aberrant glycosylation of Igs has shown biomarker potential in many (e.g. inflammatory, autoimmune, infectious) diseases. Glycosylation profiling in large clinical, epidemiological, and biological studies requires analytical methods that are sensitive, fast and robust. Additionally, a deep understanding of macro-, micro- and meta-heterogeneity and its functional impact is essential to aid the development of diagnostic and therapeutic tools.
Advancements in methodology are a prerequisite for addressing challenging applications, expanding our knowledge of Ig glycosylation roles and developing diagnosis and treatment leads.
The aim of the current Research Topic is to cover challenging investigations of Ig glycosylation with state-of-the-art analytical methodology/technology, resolving the functional significance of Ig glycosylation in homeostasis, therapy or pathology, or exploring aberrant glycosylation patterns in inflammatory, autoimmune, infectious diseases, and cancer. We intend to cover studies featuring in-depth and high-throughput glycomics / glycoproteomics, structural biology, molecular imaging and more for biomarker studies, as well as investigations of affinity and function with biophysical methods or in cellular assays, in vivo studies or clinical cohorts.
Specialized glycosylation analysis technologies have significantly advanced in the last decade and are currently capable to define glycosylation patterns of proteins from minute amount of starting material. With improved Ig purification techniques, glycan derivatization strategies and higher sensitivity of detection methods, we expect to see the low abundant Igs and more specialized matrices being addressed.
In addition, classical structural and functional approaches are increasingly including glycosylation, aided by the advent of glycoengineered Igs and humanized models.
We welcome the submission of Original Research, Methods, Review, and Mini-Review articles that may include, but are not limited to:
• Application of in-depth and high-throughput methods to elucidate Ig glycosylation patterns in a healthy organism and in disease state
• The role of Ig glycosylation in immunity
• Aberrant glycosylation patterns in inflammatory, autoimmune, infectious diseases, and cancer; or other diseases with an important inflammatory component
• Structural and functional approaches for studying Ig glycosylation
• Characterization of glycoengineered Igs and Igs from humanized models
Dr. Irena Trbojevic-Akmacic is an employee of Genos Ltd, a private research organization that specializes in high-throughput glycomic analysis. Dr. Erdmann Rapp is founder, CEO and CSO of glyXera GmbH, providing high-performance glycoanalytical products and services. The other Topic Editors declare no competing interests in relation to the topic theme.
Immunoglobulins (Igs) are co- and post-translationally modified by oligosaccharides (glycans). Ig glycans strongly impact structural and functional properties. Ig glycosylation differences may have a major impact on Fc receptor- and complement-mediated immune responses. For example, IgG Fc glycosylation is a critical element in the activation of neutrophils by autoantibodies, characteristic of anti-neutrophil cytoplasmic antibody-associated vasculitis. Furthermore, occurrence of N-glycosylation in the hypervariable domain of IgG was linked to Anti-Citrullinated Protein Antibody-positive Rheumatoid Arthritis and was suggested to increase survival of autoreactive B-cells.
Inter-individual variability of IgG glycosylation is large, but it is very stable within an individual under homeostasis. Aberrant glycosylation of Igs has shown biomarker potential in many (e.g. inflammatory, autoimmune, infectious) diseases. Glycosylation profiling in large clinical, epidemiological, and biological studies requires analytical methods that are sensitive, fast and robust. Additionally, a deep understanding of macro-, micro- and meta-heterogeneity and its functional impact is essential to aid the development of diagnostic and therapeutic tools.
Advancements in methodology are a prerequisite for addressing challenging applications, expanding our knowledge of Ig glycosylation roles and developing diagnosis and treatment leads.
The aim of the current Research Topic is to cover challenging investigations of Ig glycosylation with state-of-the-art analytical methodology/technology, resolving the functional significance of Ig glycosylation in homeostasis, therapy or pathology, or exploring aberrant glycosylation patterns in inflammatory, autoimmune, infectious diseases, and cancer. We intend to cover studies featuring in-depth and high-throughput glycomics / glycoproteomics, structural biology, molecular imaging and more for biomarker studies, as well as investigations of affinity and function with biophysical methods or in cellular assays, in vivo studies or clinical cohorts.
Specialized glycosylation analysis technologies have significantly advanced in the last decade and are currently capable to define glycosylation patterns of proteins from minute amount of starting material. With improved Ig purification techniques, glycan derivatization strategies and higher sensitivity of detection methods, we expect to see the low abundant Igs and more specialized matrices being addressed.
In addition, classical structural and functional approaches are increasingly including glycosylation, aided by the advent of glycoengineered Igs and humanized models.
We welcome the submission of Original Research, Methods, Review, and Mini-Review articles that may include, but are not limited to:
• Application of in-depth and high-throughput methods to elucidate Ig glycosylation patterns in a healthy organism and in disease state
• The role of Ig glycosylation in immunity
• Aberrant glycosylation patterns in inflammatory, autoimmune, infectious diseases, and cancer; or other diseases with an important inflammatory component
• Structural and functional approaches for studying Ig glycosylation
• Characterization of glycoengineered Igs and Igs from humanized models
Dr. Irena Trbojevic-Akmacic is an employee of Genos Ltd, a private research organization that specializes in high-throughput glycomic analysis. Dr. Erdmann Rapp is founder, CEO and CSO of glyXera GmbH, providing high-performance glycoanalytical products and services. The other Topic Editors declare no competing interests in relation to the topic theme.