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Varied redox forms of teleost IgM: an alternative to isotypic diversity?
Author(s) -
Kaattari Stephen,
Evans David,
Klemer John,
Kaattari Stephen,
Evans David,
Kieraer John
Publication year - 1998
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1111/j.1600-065x.1998.tb01258.x
Subject(s) - biology , antibody , immunoglobulin light chain , catfish , immunoglobulin m , redox , immunoglobulin heavy chain , disulfide bond , fish <actinopterygii> , biochemistry , immunoglobulin g , genetics , chemistry , organic chemistry , fishery
Summary: Teleosts (bony fish) are thought to primarily or exclusively possess a single, structural form of immunoglobulin (Ig), a tetrameric IgM. However, in species wherein intact Ig has been electrophoretically analyzed under denaturing, non‐reducing conditions, a significato degree of structural diversity has been revealed. This IgM molecule appears to be assembled with great latitude in the degree of disulfide crosslinking between monomeric or hallmark subunits composing the complete IgM molecule. This heterogeneity in the basic structure (herein referred to as redox forms) is not due to isotopic differences as each B cell produces this heterogeneity within its immunoglobulin product. Additionally, in the case of the catfish, a single fish/mouse chimeric Ig H gene is capable of producing IgM with a comparable amount of structural heterogeneity within the mouse cell. Thus, the piscine B lymphocyte routinely assembles a variety of redox forms from one IgM H chain. This has both profound biosynthetic implications for macromolecular assembly processes as well as intriguing possibilities for the generation of teleost Ig functional diversity.