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 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

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  • Author : Margaret Ackerman
  • Publisher : Academic Press
  • Pages : 358 pages
  • ISBN : 0123948185
  • Rating : 4/5 from 21 reviews
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Antibody Fc:

Antibody Fc:
  • Author : Margaret Ackerman,Falk Nimmerjahn
  • Publisher : Academic Press
  • Release : 06 August 2013
GET THIS BOOKAntibody 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

Antibody Fc

Antibody Fc
  • Author : Theo Rispens,Gestur Vidarsson
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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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

Antibody Fc

Antibody Fc
  • Author : Victor Raúl Gómez Román,Joseph C. Murray,Louis M. Weiner
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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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 expressing tumor- or pathogen-derived antigens on their surface. Numerous associations between ADCC activity, Fc receptor polymorphisms, and clinical outcomes have been observed in both the settings of vaccination and monoclonal antibody therapy. Here, the effector cells and receptors involved in ADCC are introduced, followed by a description of the four main stages and mechanisms

Antibody Fc

Antibody Fc
  • Author : Robert M. Anthony
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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IgG antibodies are highly potent molecules, with the unique ability to link foreign particles to innate immune cells. IgG antibodies recognize antigens with high affinity and bind cellular Fc receptors with low affinity individually. These interactions occur in the form of immune complexes, resulting in high-avidity interactions. 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

Antibody Fc

Antibody Fc
  • Author : Marije B. Overdijk,Sandra Verploegen,Wim K. Bleeker,Paul W.H.I. Parren
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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Historically, lack of specificity for cancer cells has been a major problem in cancer treatment; however, the development of monoclonal antibodies (mAbs), which combine high specificity with multiple mechanisms of action (MoAs), started a revolution in anti-cancer treatment options which continues to date. As of January 2013, 15 major antibody products were being marketed for cancer treatment in various countries around the globe, 10 of which are unmodified mAbs, which generally have multiple potential MoAs and may act via direct, Fab-domain-related effects or

Antibody Fc

Antibody Fc
  • Author : Roy Jefferis
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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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. Evolution of the IgG-Fc has resulted in the generation of interaction sites for endogenous (self) ligands that recruit and activate mechanisms facilitating the removal and destruction of antibody–pathogen immune complexes. However, pathogens (bacteria and virus) have co-evolved to elaborate IgG-Fc binding proteins that seek to subvert these protective mechanisms. The four human IgG subclasses exhibit differential

Fc Mediated Activity of Antibodies

Fc Mediated Activity of Antibodies
  • Author : Jeffrey V. Ravetch,Falk Nimmerjahn
  • Publisher : Springer Nature
  • Release : 03 September 2019
GET THIS BOOKFc Mediated Activity of Antibodies

This volume explores several aspects of how antibodies mediate their activity in vivo, ranging from cancer immunotherapy to autoimmunity, infection, and vaccination. Divided into seven chapters, it provides in-depth insights into how antibodies and especially the antibody fragment crystallizable (Fc) domain modulate immune responses and antibody activity. The book begins by discussing evolutionary aspects of how the family of Fc receptors that are the key molecules for antibody activity evolved. In turn, it addresses the molecular and cellular pathways underlying

Antibody Fc

Antibody Fc
  • Author : Peter Sun
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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Molecular mechanisms of antibody-mediated Fc receptor activation have long been an interest in both Fc receptor biology and antibody therapeutics. The structural efforts to elucidate antibody recognition by Fc receptors have led to the generation of several crystal structures of antibody Fc fragments complexed with Fc receptors. Collectively, these structures revealed a conserved receptor binding mode for IgG and IgE, distinct from those for the neonatal Fc receptor (FcRn), protein A, and protein G. Fcγ receptor recognition in the lower

Antibody Fc

Antibody Fc
  • Author : Xiaojie Yu,Kavitha Baruah,Christopher N. Scanlan,Max Crispin
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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The antibody Fc region is posttranslationally modified by N-linked glycosylation. In immunoglobulin G (IgG), the processing of the glycans is restricted by the presence of extensive interaction with the protein surface. The resulting set of antibody glycoforms exhibit a range of effector functions. In this chapter, we outline the impact of glycosylation on the immune function of antibodies and discuss the implications for monoclonal antibody and intravenous immunoglobulin therapies.

Antibody Fc

Antibody Fc
  • Author : George J. Weiner
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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Monoclonal antibodies (mAbs), including rituximab, are now a mainstay in the therapy of cancer. Despite their undeniable therapeutic value, there is much we do not fully understand about the mechanisms of action responsible for their anti-tumor effects. These mechanisms are often studied in isolation. In this chapter, we will review the mechanisms of action of anti-cancer mAbs and discuss how they interact. The focus of this discussion will be on rituximab, but similar conclusions can be reached with other mAbs.

Antibody Fc

Antibody Fc
  • Author : Falk Nimmerjahn
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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Autoimmune disorders are characterized by the destruction of self-tissues by the immune system. Multiple checkpoints are in place to prevent autoreactivity under normal circumstances. Co-expression of activating and inhibitory Fc receptors (FcRs) represents such a checkpoint by establishing a threshold for immune cell activation. In many human autoimmune diseases, however, balanced FcR expression is disturbed. Analysis of murine model systems provides strong evidence that aberrant FcR expression can result in uncontrolled immune responses and the initiation of autoimmune disease. This

Antibody Fc

Antibody Fc
  • Author : Andreas Diefenbach
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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Natural killer (NK) cells are granular lymphocytes that play important roles in immunity against viruses and in the immune surveillance of tumors. In addition to being a potent innate source of IFN-γ, NK cells hold cytoplasmic granula that contain perforin and granzymes involved in cell-mediated cytotoxicity. NK cells express various types of immunoreceptors that are all designed to sense pathological changes of self cells. NK cells differ from lymphocytes of the adaptive immune system, such as T and B cells,

Antibody Fc

Antibody Fc
  • Author : Joseph U. Igietseme,Xiaoping Zhu,Carolyn M. Black
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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Fc receptor (FcR)-dependent effector functions of antibodies contribute significantly to protective immunity against microbial pathogens and tumors. Therefore, FcR-mediated immunological processes constitute a key component of the immune system’s defense armamentaria for maintaining the biological and physiological integrity of the mammalian host who is yoked with frequent encounters with infections and neoplasia. The direct effector functions that result from FcR triggering are phagocytosis, antibody-dependent cellular cytotoxicity, and induction of inflammation; also, FcR-mediated processes provide immunoregulation and immunomodulation that

Antibody Fc

Antibody Fc
  • Author : Menna R. Clatworthy
  • Publisher : Elsevier Inc. Chapters
  • Release : 06 August 2013
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Fcγ receptors (FcγR) mediate many effector functions of antibody and are critical for defense against pathogens, including bacteria, viruses, and parasites. A number of single nucleotide polymorphisms have been identified in both activating and inhibitory FcγR genes that affect either the binding affinity for IgG or receptor function. Reviewing the available evidence from murine knockout mice, in vitro studies utilizing human cells, and genetic studies in humans, the current view on the role of FcγR polymorphisms in