Mutations in an avian IgY-Fc fragment reveal the locations of monocyte Fc receptor binding sites

Alexander I. Taylor; Brian J. Sutton; Rosaleen A. Calvert

doi:10.1016/j.dci.2009.08.012

Mutations in an avian IgY-Fc fragment reveal the locations of monocyte Fc receptor binding sites

Alexander I. Taylor, Brian J. Sutton, Rosaleen A. Calvert

King's College London

Research output: Contribution to journal › Article › peer-review

20 Citations (Scopus)

Abstract

The avian IgY antibody isotype shares a common ancestor with both mammalian IgG and IgE and so provides a means to study the evolution of their structural and functional specialisations. Although both IgG and IgE bind to their leukocyte Fc receptors with 1:1 stoichiometry, IgY binds to CHIR-AB1, a receptor expressed in avian monocytes, with 2:1 stoichiometry. The mutagenesis data reported here explain the structural basis for this difference, mapping the CHIR-AB1 binding site to the C upsilon 3/C upsilon 4 interface and not the N-terminal region of C upsilon 3 where, at equivalent locations, the IgG and IgE leukocyte Fc receptor binding sites lie. This finding, together with the phylogenetic relationship of the antibodies and their receptors, indicates that a substantial shift in the nature of Fc receptor binding occurred during the evolution of mammalian IgG and IgE. (C) 2009 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	97 - 101
Number of pages	5
Journal	Developmental and Comparative Immunology
Volume	34
Issue number	2
DOIs	https://doi.org/10.1016/j.dci.2009.08.012
Publication status	Published - Feb 2010

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title = "Mutations in an avian IgY-Fc fragment reveal the locations of monocyte Fc receptor binding sites",

abstract = "The avian IgY antibody isotype shares a common ancestor with both mammalian IgG and IgE and so provides a means to study the evolution of their structural and functional specialisations. Although both IgG and IgE bind to their leukocyte Fc receptors with 1:1 stoichiometry, IgY binds to CHIR-AB1, a receptor expressed in avian monocytes, with 2:1 stoichiometry. The mutagenesis data reported here explain the structural basis for this difference, mapping the CHIR-AB1 binding site to the C upsilon 3/C upsilon 4 interface and not the N-terminal region of C upsilon 3 where, at equivalent locations, the IgG and IgE leukocyte Fc receptor binding sites lie. This finding, together with the phylogenetic relationship of the antibodies and their receptors, indicates that a substantial shift in the nature of Fc receptor binding occurred during the evolution of mammalian IgG and IgE. (C) 2009 Elsevier Ltd. All rights reserved.",

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AU - Taylor, Alexander I.

AU - Sutton, Brian J.

AU - Calvert, Rosaleen A.

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AB - The avian IgY antibody isotype shares a common ancestor with both mammalian IgG and IgE and so provides a means to study the evolution of their structural and functional specialisations. Although both IgG and IgE bind to their leukocyte Fc receptors with 1:1 stoichiometry, IgY binds to CHIR-AB1, a receptor expressed in avian monocytes, with 2:1 stoichiometry. The mutagenesis data reported here explain the structural basis for this difference, mapping the CHIR-AB1 binding site to the C upsilon 3/C upsilon 4 interface and not the N-terminal region of C upsilon 3 where, at equivalent locations, the IgG and IgE leukocyte Fc receptor binding sites lie. This finding, together with the phylogenetic relationship of the antibodies and their receptors, indicates that a substantial shift in the nature of Fc receptor binding occurred during the evolution of mammalian IgG and IgE. (C) 2009 Elsevier Ltd. All rights reserved.

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DO - 10.1016/j.dci.2009.08.012

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EP - 101

JO - Developmental and Comparative Immunology

JF - Developmental and Comparative Immunology

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Mutations in an avian IgY-Fc fragment reveal the locations of monocyte Fc receptor binding sites

Abstract

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