Characterization of the molecular chaperone calnexin in the channel catfish, Ictalurus punctatus, and its association with MHC class II molecules
Characterization of the molecular chaperone calnexin in the channel catfish, Ictalurus punctatus, and its association with MHC class II molecules
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DOI：
10.1016/j.dci.2003.11.002
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发表时间：
2004-05-17
影响因子：
2.9
通讯作者：
McConnell, TJ
中科院分区：
文献类型：
--
作者：
Fuller, JR;Pitzer, JE;McConnell, TJ
哺乳动物MHC分子的折叠和组装发生在内质网(ER)，但在硬骨鱼中尚未被研究。Calnexin(CNX)是一种内质网伴侣蛋白，与含有单糖化N-连接寡糖侧链的糖蛋白结合。在这里，我们首次在硬骨鱼中鉴定和鉴定了CNX全长cDNA克隆，并在斑点叉尾鱼T细胞系中发现了CNX伴侣蛋白与MHC-II类分子的关系。1.8kb的CNX克隆编码607个氨基酸的蛋白质，与哺乳动物CNX的共同序列有72%的同源性。由于斑点叉尾鱼天然的MHC II类α链不含任何N-连接的寡糖共识糖基化序列，所以CNX与第II类之间的联系是特别有趣的。因此，鲶鱼中第二类分子的组装可能通过与哺乳动物不同的步骤进行。(C)2003爱思唯尔有限公司。保留所有权利。
Folding and assembly of MHC molecules in mammals occurs in the endoplasmic reticulum (ER), but has not been studied in teleosts. Calnexin (CNX) is an ER chaperone that associates with glycoproteins bearing a monoglucosylated N-linked oligosaccharide side chain. Here we report the first identification and characterization of a full-length CNX cDNA clone in a teleost, and the association of the CNX chaperone with MHC class II in a channel catfish T cell line. The 1.8 kb CNX clone encodes a protein of 607 amino acids that is 72% identical to the consensus sequence of mammalian CNXs. The association of CNX with class II is of particular interest because the native MHC class II alpha chain of Ictalurus punctatus does not bear any N-linked oligosaccharide consensus glycosylation sequences. Thus the assembly of class II molecules in the catfish probably proceeds via different steps than occurs in mammals. (C) 2003 Elsevier Ltd. All rights reserved.