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Erin Bromage, Jianmin Ye, Stephen Kaattari, Unique processes of antibody assembly and systemic regulation enhance affinity maturation in salmonids (90.15), The Journal of Immunology, Volume 178, Issue 1_Supplement, April 2007, Page S159, https://doi.org/10.4049/jimmunol.178.Supp.90.15
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Abstract
The salmonid humoral immune response is mediated primarily by the induction of a single antibody isotype, an 800 kDa tetrameric molecule. However, this antibody molecule possesses considerable structural diversity due to non-uniform disulfide cross-linking of its monomeric subunits. The potential association of antibody affinity with the degree of inter-monomeric disulfide bonding was examined. Three distinctly different routes were taken to examine this relationship; 1) fractionation and analysis of high and low affinity antibodies from individual immune sera by differential immunoadsorption, 2) selective induction of high vs. mixed affinity antibodies in vitro from the same population of cells, and 3) analysis of total serum antibodies undergoing affinity maturation in vivo. All three methods demonstrated a direct relationship between affinity and the degree of disulfide polymerization, with the most cross-linked forms possessing the highest affinity. Utilizing the transfer of labeled immunopurified antibody to naive hosts we have discovered that the persistence of these structural isomers in vivo is also regulated, with the preferential removal of the more reduced forms from circulation. Thus it appears that control of intramolecular disulfide polymerization of the antibody molecule combined with the selective removal of lower affinity antibodies from the circulation, is critical to achieve a mature antibody response in salmonid species.
