Chapter 4

Antibodies from Other Species

Melissa L. Vadnais

Melissa L. Vadnais

Department of Molecular Medicine, The Scripps Research Institute, 10550 N. Torrey Pines, La Jolla, CA, 92037 USA

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Michael F. Criscitiello

Michael F. Criscitiello

Texas A&M University, College of Veterinary Medicine and Biomedical Sciences, Department of Veterinary Pathobiology, 400 Raymond Stotzer Parkway, College Station, TX, 77843 USA

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Vaughn V. Smider

Vaughn V. Smider

Department of Molecular Medicine, The Scripps Research Institute, 10550 N. Torrey Pines, La Jolla, CA, 92037 USA

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First published: 14 August 2017
Citations: 1
Book Series:Methods and Principles in Medicinal Chemistry

Summary

This chapter reviews the genetic and structural features of the antibody system of several diverse species, with an emphasis on those with social or economic importance to humans, but also including unique examples of novel antibody genetics or structure that have been identified in evolutionarily important organisms. Although antibodies maintain a common structure, they exist in various isotypes, which differ in their biological function, structure, and tissue distribution. There are five major immunoglobulin isotypes in mammals: IgM, IgD, IgG, IgA, and IgE. A unique feature of mammals is the passive transfer of immunoglobulins from mother to offspring. IgG is transferred from maternal serum into the offspring by the neonatal Fc receptor (FcRn) expressed in placenta and/or the infant intestine. Antibody diversity in shark is created through V(D)J recombination of immunoglobulin genes like other jawed vertebrates, and it is one of the earliest vertebrates with this ability.

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