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Antibody Fc
Antibody Fc is the first single text to synthesize the literature on the mechanisms underlying the dramatic variability of antibodies to influence the immune response. The book demonstrates the importance of the Fc domain, including protective mechanisms, effector cell types, genetic data, and variability in Fc domain function. This volume is a critical single-source reference for researchers in vaccine discovery, immunologists, microbiologists, oncologists and protein engineers as well as graduate students in immunology and vaccinology. Antibodies represent the correlate of protection for numerous vaccines and are the most rapidly growing class of drugs, with applications ranging from cance...
Autoantibodies
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Structure and Function of Antibodies
This book provides a detailed description of all kinds of therapeutic antibodies including IgGs, IgAs, IgEs, and IgMs, bispecific antibodies, chimeric antigen receptor antibodies, and antibody fragments. Details about how each of these antibodies interact with their ligands, the immune system, and their targets are provided. Additionally, this book delves into the details of antibody, Fc, and variable chain structures, and how subtle changes in structure, charge, flexibility, post-translational modification, and the ability to bind to natural antibody ligands can result in a significant impact on antibody activity and functionality. Finally, the book explains the critical quality attributes of modern therapeutic antibodies and how to ensure that antibodies entering development have the best possible chance of success.
IgG4 Autoantibodies in the Context of IgG4 Autoimmunity
Many autoimmune diseases are induced by pathogenic autoantibodies, that bind to self-antigen expressed in cells and tissues, and induce disease by the recruitment of immune cells, activation of the classical complement pathway or induction of antigen cross-linking and endocytosis. These pathogenic mechanisms are, however, not available to antibodies of the IgG4 subclass, as these differ structurally from the other IgG subclasses, leaving them “immunologically inert”. In general, it is thought that IgG4 is part of an anti-inflammatory immune response to an overreactive pro-inflammatory response, e.g. in the context of helminth infection and allergy.
Antibody Fc
Immunoglobulins are a group of closely related glycoproteins composed of 82 to 96% protein and 4 to 18% carbohydrate. In humans, there are five classes of immunoglobulins, which differ in heavy-chain structure. Immunoglobulin G (IgG) is the major class of immunoglobulins in blood and can be further subdivided in subclasses. The four subclasses of IgG were discovered in the 1960s following extensive studies using specific rabbit antisera against human IgG myeloma proteins.1 They are designated IgG1, IgG2, IgG3, and IgG4, in order of decreasing abundance. Several decades of research has revealed subtle but profound differences among the subclasses. Each subclass has a unique profile with respe...
