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IgY : a key isotype in antibody evolution
Author(s) -
Zhang Xiaoying,
Calvert Rosaleen A.,
Sutton Brian J.,
Doré Katy A.
Publication year - 2017
Publication title -
biological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.993
H-Index - 165
eISSN - 1469-185X
pISSN - 1464-7931
DOI - 10.1111/brv.12325
Subject(s) - antibody , biology , isotype , immunoglobulin d , receptor , immunoglobulin e , fragment crystallizable region , immunoglobulin domain , neonatal fc receptor , immunoglobulin g , microbiology and biotechnology , immunology , genetics , b cell , monoclonal antibody
Immunoglobulin Y ( IgY ) is central to our understanding of immunoglobulin evolution. It has links to antibodies from the ancestral IgM to the mucosal IgX and IgA , as well as to mammalian serum IgG and IgE . IgY is found in amphibians, birds and reptiles, and as their most abundant serum antibody, is orthologous to mammalian IgG . However, IgY has the same domain architecture as IgM and IgE , lacking a hinge region and comprising four heavy‐chain constant domains. The relationship between IgY and the mucosal antibodies IgX and IgA is discussed herein, in particular the question of how IgA could have contributed to the emergence of IgY . Although IgY does not contain a hinge region, amphibian IgF and duck‐billed platypus IgY/O , which are closely related to IgY , do contain this region, as does mammalian IgG , IgA and IgD . A hinge region must therefore have evolved at least three times independently by convergent evolution. In the absence of three‐dimensional structural information for the complete F c fragment of chicken IgY ( IgY‐Fc ), it remains to be discovered whether IgY displays the same conformational properties as IgM and IgE , which exhibit substantial flexibility in their F c regions. IgY has three characterised F c receptors, chicken I g‐like receptor AB1 ( CHIR‐AB1 ), the chicken yolk sac IgY receptor ( FcRY ) and G allus gallus F c receptor ( ggFcR ). These receptors bind to IgY at sites that are structurally homologous to mammalian counterparts; IgA / FcαRI for CHIR‐AB1 , IgG / FcRn for FcRY and IgE / FcϵRI and IgG / FcγR for ggFcR . These resemblances reflect the close evolutionary relationships between IgY and IgA , IgG and IgE . However, the evolutionary distance between birds and mammals allows for the ready generation of IgY antibodies to conserved mammalian proteins for medical and biotechnological applications. Furthermore, the lack of reactivity of IgY with mammalian F c receptors, and the fact that large quantities of IgY can be made quickly and cheaply in chicken eggs, offers important advantages and considerable potential for IgY in research, diagnostics and therapeutics.