Huang T1, Wu K2, Yuan X1, Shao S1, Wang W1, Wei S1, Cao G3. 2016. Dev Comp Immunol. 60:160-6. doi: 10.1016/j.dci.2016.02.024. Epub 2016 Feb 24.
1School of Life Science, Henan University, Kaifeng 475004, PR China; Institute of Bioengineering, Henan University, Kaifeng 475004, PR China.
2Institute of Bioengineering, Henan University, Kaifeng 475004, PR China.
3School of Life Science, Henan University, Kaifeng 475004, PR China; Institute of Bioengineering, Henan University, Kaifeng 475004, PR China. Electronic address: email@example.com.
Immunoglobulins play an important role in adaptive immune system as defense molecules against pathogens. However, our knowledge on avian immunoglobulin genes has been limited to a few species. In this study, we analyzed goose (Anser cygnoides orientalis) immunoglobulin genes. Three IgH classes including IgM, IgA, IgY and λ light chain were identified. The IgM and IgA heavy chain constant regions are characteristically similar to their counterparts described in other vertebrates. In addition to the classic Ig isotypes, we also detected a transcript that encoded a truncated form of IgY (IgY(ΔFc)) in goose. Similar to duck, the IgY(ΔFc) in goose was generated by using different transcriptional termination signal of the same υ gene. Limited variability and only one leader peptide were observed in VH and VL domains, which suggested that gene conversion was the primary mechanism involved in goose antibody diversity. Our study provides more insights into the immunoglobulin genes in goose that had not been fully explored before.
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Evolution; Goose; Immunoglobulin gene