Molecular cloning and functional characterization of porcine MyD88 essential for TLR signaling.
Molecular cloning and functional characterization of porcine MyD88 essential for TLR signaling.
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发表时间：
2007-10
影响因子：
24.1
通讯作者：
M. Tohno;T. Shimazu;H. Aso;Y. Kawai;Tadao Saito;H. Kitazawa
中科院分区：
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作者：
M. Tohno;T. Shimazu;H. Aso;Y. Kawai;Tadao Saito;H. Kitazawa
我们从GALT的Peyer‘s patches(PPS)中分离到编码猪MyD88(PoMyD88)的基因。PoMyD88的完整开放阅读框(ORF)包含879个核苷酸，编码293个氨基酸残基。PoMyD88的氨基酸序列由N端死亡、中间和C端Toll/IL-1受体(TIR)结构域组成。推测的poMyD88蛋白与人(87.2%的氨基酸同源性)比与小鼠(77.4%的氨基酸同源性)有更高的同源性。在表达猪TLR2和猪TLR4/MD-2但不表达猪RP105/MD-1的人胚胎肾(HEK)293细胞中，poMyD88的过表达参与了相应配体刺激后NF-kappaB的进一步激活。MyD88在新生猪的脾和肠系膜淋巴结中的表达水平最高，在消化组织中的表达水平较低。在成年猪中，消化组织中的表达水平低于MLN和脾组织。这些结果表明，MyD88依赖的信号通路在新生猪和成年猪中都存在，并参与了这些动物的先天免疫系统。
We isolated cDNA encoding porcine MyD88 (poMyD88) from Peyer's patches (Pps) of GALT. The complete open reading frame (ORF) of poMyD88 contains 879 bp encoding a deduced 293 aa residues. The amino acid sequence of poMyD88 was characterized by N-terminal death, intermediate and C-terminal Toll/IL-1 receptor (TIR) domains. The putative poMyD88 protein shares a higher level of homology with its human (87.2% amino acid identity) than with its mouse (77.4% amino acid identity) counterpart. Overexpression of poMyD88 participated in the further enhanced activation of NF-kappaB in human embryonic kidney (HEK) 293 cells expressing porcine TLR2 and porcine TLR4/MD-2, but not porcine RP105/MD-1 after stimulation with the corresponding ligands. The expression levels of MyD88 were highest in the spleen and mesenteric lymph nodes (MLNs), and lower in digestive tissues of newborn swine. In adult swine, the expression levels in the digestive tissues were lower than those in MLNs and the spleen. These results suggest that an MyD88-dependent signaling pathway is present in newborn as well as in adult swine and that it is involved in the innate immune system of these animals.