Matthias Theobald - Current Immunotherapeutic Strategies in Cancer

This book series presents comprehensive, high-quality updates on areas of current interest in basic, clinical, and translational cancer research. The scope of the series is broad, encompassing epidemiology, etiology, pathophysiology, prevention, diagnosis, and treatment. Each volume is devoted to a specific topic with the aim of providing readers with a thorough overview by acclaimed experts. While advances in understanding of the cellular, genetic, and molecular mechanisms of cancer and progress toward personalized cancer care are a particular focus, subjects such as the lifestyle, psychological, and social aspects of cancer and public policy are also covered. Recent Results in Cancer Research is accordingly of interest to a wide spectrum of researchers, clinicians, other health care professionals, and stakeholders. The series is listed in PubMed/Index Medicus.

More information about this series at http://www.springer.com/series/392

This Springer imprint is published by the registered company Springer Nature Switzerland AG

The registered company address is: Gewerbestrasse 11, 6330 Cham, Switzerland

Functionally, antibodies are divided into two parts; the two arms in the Y-shaped structure contain the antigen-binding sites and are named as the fragment antigen-binding (Fab) region, along with the base of the Y-shaped structure which mediates immunological signalling by antibodies and is called the fragment crystallizable (Fc) region. The Fab arm of an IgG antibody contains the full light chains and part of the heavy chain, each with their own constant and variable domains. Antigen specificity in the Fab region is determined by complementarity-determining regions (CDRs) within the variable domains. These CDRs have the greatest sequence variation within antibodies, and this feature gives rise to the diverse range of antigen specificities. There are three CDRs for each variable region, which means six CDRs (heavy and light) for each Fab arm and twelve in total for a single antibody molecule. The six CDRs on each Fab arm fold together to form the antigen-binding pocket, and this allows an antibody to be able to simultaneously bind two epitopes. When antibodies recognize a soluble antigen, this simultaneous binding can produce large multimeric structures called immune complexes.

Within the immune system, a principle function of antibodies is to neutralize pathogens such as bacteria and viruses. The CDRs within the variable regions of an antibody recognize a specific molecular structure of an antigen, called the epitope, present on the pathogen. Because of the random nature of antibody generation in the development of each individual B cell, there are millions of B cells circulating at any given time that each recognize a different antigen. Once a B cell encounters an invading pathogen with its unique epitope, it undergoes maturation with the help of specific T cells and produces large amounts of soluble antibody. Multiple B cells will recognize different epitopes present on the pathogen, and so many different antibodies will be produced. Once produced, these antibodies bind their antigen on the surface of the bacteria or virus to neutralize the pathogen and mark it for destruction by innate immune effector cells.