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IgY: a key isotype in antibody evolution.

Xiaoying Zhang1, Rosaleen A Calvert2, Brian J Sutton2

  • 1Department of Basic Veterinary, College of Veterinary Medicine, Northwest A&F University, Yangling, 712100, China.

Biological Reviews of the Cambridge Philosophical Society
|March 17, 2017
PubMed
Summary
This summary is machine-generated.

Immunoglobulin Y (IgY) is an abundant antibody in reptiles and birds, evolutionarily linked to mammalian IgG. Its unique structure and lack of reactivity with mammalian receptors offer significant potential for biotechnological applications.

Keywords:
Fc receptorsIgAIgEIgGIgMIgYantibody evolutionhinge region

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Area of Science:

  • Immunology
  • Evolutionary Biology
  • Biotechnology

Background:

  • Immunoglobulin Y (IgY) is the primary serum antibody in non-mammalian vertebrates like birds and reptiles.
  • IgY shares evolutionary links with mammalian immunoglobulins, including Immunoglobulin G (IgG), Immunoglobulin A (IgA), Immunoglobulin M (IgM), and Immunoglobulin E (IgE).
  • Despite being orthologous to IgG, IgY possesses a domain architecture similar to IgM and IgE, lacking a hinge region.

Purpose of the Study:

  • To explore the evolutionary relationships of IgY with other immunoglobulin classes.
  • To investigate the structural features of IgY, including its hinge region and Fc fragment.
  • To examine the interactions of IgY with its known Fc receptors and compare them to mammalian counterparts.
  • To highlight the biotechnological and therapeutic potential of IgY.

Main Methods:

  • Comparative analysis of immunoglobulin structures and evolutionary pathways.
  • Review of existing literature on IgY structure, function, and receptor interactions.
  • Examination of Fc receptor binding sites and their homology to mammalian systems.

Main Results:

  • IgY is evolutionarily linked to ancestral IgM and mucosal IgA, as well as mammalian IgG and IgE.
  • The absence of a hinge region in IgY, contrasted with its presence in related amphibian and mammalian antibodies, suggests independent evolution of this feature.
  • IgY binds to specific Fc receptors (CHIR-AB1, FcRY, ggFcR) with sites homologous to mammalian IgA, IgG, and IgE receptors.
  • IgY does not react with mammalian Fc receptors.

Conclusions:

  • IgY's evolutionary trajectory involves connections to both ancestral and mammalian immunoglobulin classes.
  • The independent evolution of the hinge region in various immunoglobulin lineages is supported.
  • Structural homologies in Fc receptor binding sites underscore the evolutionary relatedness of IgY to mammalian antibodies.
  • IgY's distinct properties, including lack of mammalian Fc receptor cross-reactivity and ease of production, present significant advantages for medical and biotechnological applications.