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This book summarizes recent advances in antibody glycosylation research. Covering major topics relevant for immunoglobulin glycosylation - analytical methods, biosynthesis and regulation, modulation of effector functions - it provides new perspectives for research and development in the field of therapeutic antibodies, biomarkers, vaccinations, and immunotherapy.
Glycans attached to both variable and constant regions of antibodies are known to affect the antibody conformation, stability, and effector functions. Although it focuses on immunoglobulin G (IgG), the most explored antibody in this context, and unravels the natural phenomena resulting from the mixture of IgG glycovariants present in the human body, the book also discusses other classes of human immunoglobulins, as well as immunoglobulins produced in other species and production systems. Further, it reviews the glycoanalytical methods applied to antibodies and addresses a range of less commonly explored topics, such as automatization and bioinformatics aspects of high-throughput antibody glycosylation analysis. Lastly, the book highlights application areas ranging from the ones already benefitting from antibody glycoengineering (such as monoclonal antibody production), to those still in the research stages (such as exploration of antibody glycosylation as a clinical or biological age biomarker), and the potential use of antibody glycosylation in the optimization of vaccine production and immunization protocols.
Summarizing the current knowledge on the broad topic of antibody glycosylation and its therapeutic and biomarker potential, this book will appeal to a wide biomedical readership in academia and industry alike.
Chapter 4 is available open access under a Creative Commons Attribution 4.0 International License via link.springer.com.
List of contents
Microheterogeneity of antibody molecules.- Part I: Analytical Methods.- Lectin and LC based methods for immunoglobulin (G) glycosylation analysis.- Mass spectrometry-based methods for immunoglobulin G N-glycosylation analysis.- CE based methods for Ig(G) glycosylation analysis.- Automation of Ig glycosylation analysis.- Bioinformatics in immunoglobulin glycosylation analysis.- Part II: Biosynthesis & Regulation.- N-glycan biosynthesis: Basic principles and factors affecting its outcome.- Genetic regulation of immunoglobulin G glycosylation.- Epigenetics of immunoglobulin G glycosylation.- IgG changes in aging and other inflammatory conditions.- Estrogen-driven changes in immunoglobulin G Fc glycosylation.- Part III: Effector Functions & Diseases.- Sweet rules - linking glycosylation to antibody function.- Immunoglobulin G glycosylation in diseases.- Immunoglobulin A glycosylation and its role in diseases.- Part IV: Applications.- Importance and monitoring of therapeutic immunoglobulin G glycosylation.- Glycosylation of plant-produced immunoglobulins.- The rapidly expanding nexus of immunoglobulin G N-glycomics, suboptimal health status, and precision medicine.- Glycosylation of antigen-specific antibodies - Perspectives on immunoglobulin G glycosylation in vaccination and immunotherapy.
About the author
Marija Pezer received her PhD in Molecular Biology from the University of Zagreb, Croatia, in 2013. She currently works at Genos Glycoscience Research Laboratory, Croatia, where she is investigating the biomarker potential of immunoglobulin G glycosylation patterns in different pathological and physiological states. The Genos lab has performed over 150,000 total plasma and IgG N-glycome analyses (world’s No. 1). She is also the Head of product development for GlycanAge – the first glycan-based test for biological age.
Summary
This book summarizes recent advances in antibody glycosylation research. Covering major topics relevant for immunoglobulin glycosylation - analytical methods, biosynthesis and regulation, modulation of effector functions - it provides new perspectives for research and development in the field of therapeutic antibodies, biomarkers, vaccinations, and immunotherapy.
Glycans attached to both variable and constant regions of antibodies are known to affect the antibody conformation, stability, and effector functions. Although it focuses on immunoglobulin G (IgG), the most explored antibody in this context, and unravels the natural phenomena resulting from the mixture of IgG glycovariants present in the human body, the book also discusses other classes of human immunoglobulins, as well as immunoglobulins produced in other species and production systems. Further, it reviews the glycoanalytical methods applied to antibodies and addresses a range of less commonly explored topics, such as automatization and bioinformatics aspects of high-throughput antibody glycosylation analysis. Lastly, the book highlights application areas ranging from the ones already benefitting from antibody glycoengineering (such as monoclonal antibody production), to those still in the research stages (such as exploration of antibody glycosylation as a clinical or biological age biomarker), and the potential use of antibody glycosylation in the optimization of vaccine production and immunization protocols.
Summarizing the current knowledge on the broad topic of antibody glycosylation and its therapeutic and biomarker potential, this book will appeal to a wide biomedical readership in academia and industry alike.
Chapter 4 is available open access under a Creative Commons Attribution 4.0 International License via link.springer.com.
