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Evolution of Vertebrate Immunoglobulin Variable Gene Segments

  • Chapter
Origin and Evolution of the Vertebrate Immune System

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 248))

Abstract

Immunoglobulins (Igs), also known as antibodies, play major roles in the verte- brate humoral immune system. They recognize and bind to foreign antigens, such as viruses, bacteria and parasites, and initiate a series of immunological responses (effector function). The dual function of the Ig protein is facilitated by its unique structure consisting of two functionally distinct domains, i.e., the variable (V) domain for antigen recognition and the constant (C) domain for effector function (Frazer and Capra 1998). Ig is generally composed of two identical heavy (IgH) and two identical light (IgL) chains, both of which contribute to the formation of V and C domains.

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Authors and Affiliations

  1. Center for Human Genetics, Boston University School of Medicine, 715 Albany St., Boston, MA, 02118, USA

    T. Ota

  2. The Graduate University for Advanced Studies, Hayama, Kanagawa, Japan

    T. Ota

  3. Eisai Merrimack Valley Lab Inc., 100 Federal St., Andover, MA, 01810, USA

    T. Sitnikova

  4. Institute of Molecular Evolutionary Genetics and Department of Biology, The Pennsylvania State University, 328 Mueller, University Park, PA, 16802, USA

    M. Nei

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  2. T. Sitnikova
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  3. M. Nei
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  1. Basel Institute for Immunlogy, Grenzacherstr. 487, CH-4005, Basel, Switzerland

    Louis Du Pasquier

  2. All Children’s Hospital, University of South Florida, 801 6th Street South, 33701, St. Petersburg, FL, USA

    Gary W. Litman M.D.

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Ota, T., Sitnikova, T., Nei, M. (2000). Evolution of Vertebrate Immunoglobulin Variable Gene Segments. In: Du Pasquier, L., Litman, G.W. (eds) Origin and Evolution of the Vertebrate Immune System. Current Topics in Microbiology and Immunology, vol 248. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-59674-2_10

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