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

Author:

Wilson Melanie1,Bengtén Eva1,Miller Norman W.1,Clem L. William1,Du Pasquier Louis1,Warr Gregory W.1

Affiliation:

1. Department of Microbiology, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS 39216; Basel Institute for Immunology, Grenzacherstrasse 487, CH-4058 Basel, Switzerland; and Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425

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 (δ) 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 μ, and seven constant domains encoded by a δ gene homolog. Identification of the catfish gene as δ is based on the following properties: sequence relatedness to mammalian δ; a location within the IgH locus that is immediately downstream of the μ gene; separate terminal exons for the secretory and membrane forms; coexpression with the complete μ 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.

Publisher

Proceedings of the National Academy of Sciences

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