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Molecular cloning of chicken interleukin-5 receptor α-chain and analysis of its binding specificity.

Abstract：

:Interaction between interleukin (IL)-5 and its receptor (IL-5R) is important for the regulation of immunity against worm infections, allergic reactions and B cell response in mammals. In this study, we identified a full-length cDNA encoding chicken IL-5R α-chain (chIL-5Rα). The deduced amino acid sequence showed 41-43% identity to mammalian homologues. It has four well-conserved cysteines and a WSXWS motif in the extracellular region, and a PPXP motif in the cytoplasmic region. Quantitative RT-PCR analysis revealed that chIL-5Rα mRNA expression was markedly high in bone marrow and relatively high in spleen and lung. Recombinant proteins of soluble chIL-5Rα and cytokines (artificially produced chIL-5 (achIL-5) and another IL-5-like molecule KK34) were expressed by 293F cells to examine the cytokine-receptor interactions. Interaction assay using a Biacore biosensor showed that chIL-5Rα has the capability to bind with monomeric achIL-5, but not with KK34. In conclusion, chicken has an IL-5Rα homologue but KK34 does not complement the IL-5/IL-5R system.

journal_name

Dev Comp Immunol

journal_title

Developmental and comparative immunology

authors

Fukushima Y,Miyai T,Kumagae M,Horiuchi H,Furusawa S

doi

10.1016/j.dci.2012.02.013

subject

Has Abstract

pub_date

2012-07-01 00:00:00

pages

354-62

issue

3-4

eissn

0145-305X

issn

1879-0089

pii

S0145-305X(12)00036-5

journal_volume

37

pub_type

杂志文章

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