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 cancer and infectious disease to autoimmunity. Researchers have long understood the variable domain of antibodies, which are responsible for antigen recognition, and can provide protection by blocking the function of their target antigen. However, recent developments in our understanding of the protection mediated by antibodies have highlighted the critical nature of the antibody constant, or Fc domain, in the biological activity of antibodies. The Fc domain allows antibodies to link the adaptive and innate immune systems, providing specificity to a wide range of innate effector cells. In addition, they provide a feedback loop to regulate the character of the immune response via interactions with B cells and antigen-presenting cells. Clarifies the different mechanisms of IgG activity at the level of the different model systems used, including human genetic, mouse, and in vitro Covers the role of antibodies in cancer, infectious disease, and autoimmunity and in the setting of monoclonal antibody therapy as well as naturally raised antibodies Color illustrations enhance explanations of the immune system
This review summarizes the structural findings that formed the basis of modern antibody–Fc receptor biology and recent advances of shared Fc receptor recognition by innate pentraxins.
Carlotti E, Palumbo GA, Oldani E, et al. FCgammar IIIA and Fcgammar IIA polymorphisms do not predict clinical outcome of follicular non-Hodgkin's lymphoma patients treated with sequential CHOP and rituximab. Haematologica.
Immunoglobulins are a group of closely related glycoproteins composed of 82 to 96% protein and 4 to 18% carbohydrate.
Antibody Fc Engineering: Towards Better Therapeutics
In fact, the effector functions triggered by IgG antibodies are highly dependent on the type of Fc receptor that is bound; however, many aspects can influence Fc receptor binding by IgG antibodies, including the IgG isotype and the ...
Diversity of antigen-binding specificity may be considered the hallmark of antibodies; however, the human IgG-Fc region also exhibits binding specificity for multiple ligands.
The antibody Fc region is posttranslationally modified by N-linked glycosylation.
Antibody-dependent cellular cytotoxicity (ADCC), also called antibody-dependent cell-mediated cytotoxicity, is an immune mechanism through which Fc receptor-bearing effector cells can recognize and kill antibody-coated target cells ...
Antibody Fc: Chapter 8. FcγRs Across Species
Deleterious immune reactivity associated with FcR engagement, including immune complex diseases, allergic reactions due to IgE-mediated activation of mast cells and basophils, or facilitation of microbial infectivity, such as antibody ...