Molecular Cloning and Expression Analysis of CD127 in Pig

Abstract

CD127 (the alpha chain of the IL-7 receptor) is an 80 kDa type I membrane glycoprotein that mediates the signal for the differentiation, maturation, and survival of lymphocyte development. In this study, the full-length cDNA of pig Cd127 was cloned and sequenced. Pig CD127 cDNA contains an open reading frame (1,380 bp) encoding 459 amino acids. Phylogenetic analysis revealed that pig CD127 is most homologous to that of cow (Bos taurus) with 87% amino acid identity and less homologous to that of chicken (Gallus gallus) with 36% amino acid identity among those of species. Structurally, pig CD127 has well-conserved cytoplasmic tail that transmits a signal and little diversity of extracellular domain, compared with those of other mammalian species. Expression analysis indicates that the mRNA transcript of pig CD127 is mainly detected in lymphoid tissues, but still detected in nonlymphoid tissues. Future studies will be focused on determining a more defined expression pattern of pig CD127 and the role of CD127 during the lymphocyte development in pigs.

Influence of orally fed a select mixture of Bacillus probiotics on intestinal T-cell migration in weaned MUC4 resistant pigs following Escherichia coli challenge

“…IL-7 receptor α-chain (IL-7Rα, also known as CD127) contributes to the development of IL-22–producing cells and Treg cells, IL-7/IL-7R–dependent signaling plays a crucial role in regulating the immune response in the intestinal mucosa [ 12 , 13 ]. In swine, CD127 has been detected in the intestine, lymphoid tissues, and various nonlymphoid tissues [ 14 ].…”

Research Note: Development and characterization of monoclonal antibodies specific for chicken interleukin-7 receptor α (CD127)

“…CD127, a type I cytokine receptor ( McElroy et al, 2012 ), is expressed on most leukocytes ( Mazzucchelli and Durum, 2007 ), and has been widely used in investigation of the IL-7-mediated differentiation, maturation, and survival of lymphocytes ( Hur et al, 2009 ). Like other interleukin receptors, mammalian CD127, a glycoprotein consisting of multiple asparagine molecules, can self-associate to generate homodimers that are incapable of signaling ( Hamming et al, 2012 ).…”