Antibody Glycosylation

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, suchas 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.

Autorentext

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.

Inhalt

Preface - Marija Pezer, Genos Glycoscience Research Laboratory, Croatia
Analytical methods1.(UP)LC based methods for Ig(G) glycosylation analysis Irena Trbojevic Akmacic, Genos Glycoscience Research Laboratory, Croatia2.MS based methods for Ig(G) glycosylation analysis Mislav Novokmet, Genos Glycoscience Research Laboratory, Croatia3.CE based methods for Ig glycosylation analysis Rene Hennig, Erdmann Rapp, GlyXera, Germany4.Automation of Ig glycosylation analysis Daniel Spencer, Richard Gardner, Ludger, UK5.Bioinformatics in IgG glycosylation analysis Bas Jansen, Omina Technologies, UK
Biosynthesis & Regulation6.Ig(G) glycan biosynthesis - Sahari Kelokumpu, University of Oulu, Finland7.Genetics of IgG glycosylation Lucija Klaric, University of Edinburgh, UK; Olga Zaytseva, Genos Glycoscience Research Laboratory, Croatia8.Epigenetics of IgG glycosylation Vlatka Zoldos, University of Zagreb, Croatia9.IgG glycosylation changes (role) in ageing, or inflammageing Fabio dall'Olio, University of Bologna, Italy10.IgG glycosylation and sex hormones Peter Nigrovic, Boston's Children Hospital, Harvard Medical School, USA
Effector functions & Diseases11.Sweet rules linking IgG glycosylation and antibody function - Falk Nimmerjahn, University of Erlangen, Germany12.IgG glycosylation in diseases - Marija Pezer, Genos Glycoscience Research Laboratory, Croatia13.IgA/E/M/D glycosylation/modifications
Applications14.Importance and monitoring of therapeutic antibody modifications Yusuke Mimura, NHO Yamaguchi Ube Medical Center, Japan; Roy Jefferis, University of Birmingham15.Biomarker potential of IgG glycosylation Alyce Russell, Wei Wang, Edith Cowan University, Australia16.Perspectives on IgG glycosylation in vaccination and immunotherapy