Journal
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
Volume 34, Issue 2, Pages 97-101Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.dci.2009.08.012
Keywords
Antibodies; Birds; Evolution; Fc receptors; Immunity; Immunoglobulins
Categories
Funding
- Wellcome Trust VIP
- Biotechnology and Biological Sciences Research Council (UK)
- Biotechnology and Biological Sciences Research Council [BB/D011418/1] Funding Source: researchfish
- Medical Research Council [G0400503B, G0501494] Funding Source: researchfish
- BBSRC [BB/D011418/1] Funding Source: UKRI
- MRC [G0501494] Funding Source: UKRI
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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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