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Antigen–Antibody Complexes

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Vertebrate and Invertebrate Respiratory Proteins, Lipoproteins and other Body Fluid Proteins

Part of the book series: Subcellular Biochemistry ((SCBI,volume 94))

Abstract

In vertebrates, immunoglobulins (Igs), commonly known as antibodies, play an integral role in the armamentarium of immune defense against various pathogens. After an antigenic challenge, antibodies are secreted by differentiated B cells called plasma cells. Antibodies have two predominant roles that involve specific binding to antigens to launch an immune response, along with activation of other components of the immune system to fight pathogens. The ability of immunoglobulins to fight against innumerable and diverse pathogens lies in their intrinsic ability to discriminate between different antigens. Due to this specificity and high affinity for their antigens, antibodies have been a valuable and indispensable tool in research, diagnostics and therapy. Although seemingly a simple maneuver, the association between an antibody and its antigen, to make an antigen–antibody complex, is comprised of myriads of non-covalent interactions. Amino acid residues on the antigen binding site, the epitope, and on the antibody binding site, the paratope, intimately contribute to the energetics needed for the antigen–antibody complex stability. Structural biology methods to study antigen–antibody complexes are extremely valuable tools to visualize antigen–antibody interactions in detail; this helps to elucidate the basis of molecular recognition between an antibody and its specific antigen. The main scope of this chapter is to discuss the structure and function of different classes of antibodies and the various aspects of antigen–antibody interactions including antigen–antibody interfaces—with a special focus on paratopes, complementarity determining regions (CDRs) and other non-CDR residues important for antigen binding and recognition. Herein, we also discuss methods used to study antigen–antibody complexes, antigen recognition by antibodies, types of antigens in complexes, and how antigen–antibody complexes play a role in modern day medicine and human health. Understanding the molecular basis of antigen binding and recognition by antibodies helps to facilitate the production of better and more potent antibodies for immunotherapy, vaccines and various other applications.

Maksymilian Chruszcz—To whom correspondence should be addressed: Maksymilian Chruszcz, Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA

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Acknowledgements

The authors would like to thank Dr. Tapiwa Pekoyo for insightful comments and discussions. This work was supported by grant R01AI077653 from National Institute of Allergy and Infectious Diseases. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, 29208, USA

    A. Brenda Kapingidza & Maksymilian Chruszcz

  2. Department of Allergology and Internal Medicine, Medical University of Bialystok, Bialystok, Poland

    Krzysztof Kowal

  3. Department of Experimental Allergology and Immunology, Medical University of Bialystok, Bialystok, Poland

    Krzysztof Kowal

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  1. A. Brenda Kapingidza
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Correspondence to Maksymilian Chruszcz .

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  1. Institute of Molecular Physiology, Johannes Gutenberg University, Mainz, Rheinland-Pfalz, Germany

    Ulrich Hoeger

  2. Institute of Molecular Physiology, Johannes Gutenberg University, Mainz, Rheinland-Pfalz, Germany

    J. Robin Harris

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Kapingidza, A.B., Kowal, K., Chruszcz, M. (2020). Antigen–Antibody Complexes. In: Hoeger, U., Harris, J. (eds) Vertebrate and Invertebrate Respiratory Proteins, Lipoproteins and other Body Fluid Proteins. Subcellular Biochemistry, vol 94. Springer, Cham. https://doi.org/10.1007/978-3-030-41769-7_19

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