chicken leukocyte receptor complex encodes a primordial, activating, high-affinity IgY Fc receptor

Fc receptors are key players of the immune system that link the fine specificity of immunoglobulins and innate effector responses. Here, we describe a nonmammalian Fcγ receptor, CHIR-AB1, a member of the leukocyte receptor complex, that binds IgY with high affinity with its single Ig domain. It is e...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2007-07, Vol.104 (28), p.11718-11723
Main Authors: Viertlboeck, Birgit C, Schweinsberg, Sonja, Hanczaruk, Matthias A, Schmitt, Ramona, Du Pasquier, Louis, Herberg, Friedrich W, Göbel, Thomas W
Format: Article
Language:English
Subjects:
Animals
Antibody Affinity - immunology
B lymphocytes
Biological Sciences
Calcium
Cell Line
Cell lines
Chickens
Chickens - immunology
Fc receptors
Genes
Immune system
Immunoglobulins
Immunoglobulins - metabolism
Immunology
Leukocytes
Leukocytes - immunology
Leukocytes - metabolism
Ligands
Macrophages
Molecular Sequence Data
Natural killer cells
Poultry
Protein Binding - immunology
Receptors
Receptors, Fc - genetics
Receptors, Fc - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Fc receptors are key players of the immune system that link the fine specificity of immunoglobulins and innate effector responses. Here, we describe a nonmammalian Fcγ receptor, CHIR-AB1, a member of the leukocyte receptor complex, that binds IgY with high affinity with its single Ig domain. It is expressed on immature and mature B lymphocytes, monocytes, macrophages, and natural killer cells and harbors motifs of activating and inhibitory Fc receptors. In the absence of FcεRIγ, CHIR-AB1 can be expressed on B cells but cross-linking does not induce intracellular calcium release. In contrast, cells expressing CHIR-AB1 and FcεRIγ are triggered to release intracellular calcium upon stimulation with heat-aggregated IgY. CHIR-AB1 thus represents a primordial Fc receptor that combines features of different mammalian counterparts.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0702011104