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一种来自硬骨鱼的新型嵌合免疫球蛋白重链与免疫球蛋白D有相似之处。

A novel chimeric Ig heavy chain from a teleost fish shares similarities to IgD.

作者信息

Wilson M, Bengtén E, Miller N W, Clem L W, Du Pasquier L, Warr G W

机构信息

Department of Microbiology, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS 39216, USA.

出版信息

Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4593-7. doi: 10.1073/pnas.94.9.4593.

Abstract

IgD is considered to be a recently evolved Ig, being previously found only in primates and rodents. Here we describe, from a teleost fish (the channel catfish, Ictalurus punctatus), a novel complex chimeric Ig heavy chain, homologous, in part, to the heavy chain (delta) of IgD. In addition to alternative secretory or membrane-associated C termini, this chimeric molecule contains a rearranged variable domain, the first constant domain of mu, and seven constant domains encoded by a delta gene homolog. Identification of the catfish gene as delta is based on the following properties: sequence relatedness to mammalian delta; a location within the IgH locus that is immediately downstream of the mu gene; separate terminal exons for the secretory and membrane forms; coexpression with the complete mu chain in some but not all B cells. These results (i) suggest that IgD is an ancient immunoglobulin that was present in vertebrates ancestral to both the mammals and the ray-finned fishes, and (ii) raise the possibility that this Ig isotype may have served an as yet unidentified important function early in the evolution of the immune system.

摘要

IgD被认为是一种最近才进化出来的免疫球蛋白,此前仅在灵长类动物和啮齿动物中发现。在此,我们描述了一种来自硬骨鱼(斑点叉尾鮰,Ictalurus punctatus)的新型复合嵌合免疫球蛋白重链,它部分同源于IgD的重链(δ)。除了可选择的分泌型或膜结合型C末端外,这种嵌合分子还包含一个重排的可变结构域、μ的第一个恒定结构域,以及由一个δ基因同源物编码的七个恒定结构域。将鲶鱼基因鉴定为δ基于以下特性:与哺乳动物δ的序列相关性;位于IgH基因座中μ基因下游紧邻的位置;分泌型和膜型的独立末端外显子;在一些但并非所有B细胞中与完整的μ链共表达。这些结果(i)表明IgD是一种古老的免疫球蛋白,在哺乳动物和硬骨鱼的共同祖先脊椎动物中就已存在,(ii)增加了这种免疫球蛋白同种型在免疫系统进化早期可能发挥了尚未确定的重要功能的可能性。

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