Immunoglobulin evolution

Hooper JA. Intravenous immunoglobulins evolution of commercial IVIG preparations. Immunol Allergy Clin North Am 2008 28(4) 765-78, viii. 

From the results reported to date, it seems that the manner in which haptens are attached to carrier proteins leads to significant differences in certain cases. Clearly, haptens designed with aromatic moieties between the linkage to the immunogenic carrier protein and the TSA motif often have better antibody recognition. Recently, Hilvert pointed out that on both micro and macro levels, mechanistic improvements arise as a function of time. The differences in time scales for the evolution of natural enzymes and antibodies — millions of years versus weeks or months — also appear to be an explanation of the low efficiency of antibody catalysts. He also highlighted that the unique immunoglobulin fold has not been adopted by nature as one of the common scaffolds on which to build enzyme catalytic machinery. Therefore, antibody structure itself places limitations on the kind of reactions amenable to catalysis. 

Kodaira, M., Kinashi, T., Umemura, I., et al. (1986). Organization and evolution of variable region genes of the human immunoglobulin heavy chain. J. Mol. Biol., 190,529-541. 

Structural domains of proteins are sometimes encoded by a single coding segment of DNA i.e., by a single exon in a split gene. Domains of this type may have served as evolutionarily mobile modules that have spread to new proteins and multiplied during evolution. For example, the immunoglobulin structural domain is found not only in antibodies but also in a variety of cell surface proteins.229 252... 

Bentley, D.L. Rabbitts, T.H. (1983). Evolution of immunoglobulin V genes evidence indicating that recently duplicated human VK sequences have diverged by gene conversion. Cell 32, 181-189. 

Blankenstein, T., Bonhomme, F., Krawinkel, U. (1987). Evolution of pseudogenes in the immunoglobulin Vjj-gene family of the mouse. Immunogenetics 26,237-248. 

Hinds-Frey, K.R., Nishikata, H., Litman, R.T., Litman, G.W. (1993). Somatic variation precedes extensive diversification of germline sequences and combinatorial joining in the evolution of immunoglobulin heavy chain diversity. J. Exp. Med. 178, 815-824. 

Seising, E., Miller, J., Wilson, R., Storb, U. (1982). Evolution of mouse immunoglobulin X genes. Proc. Natl. Acad. Sci. USA 79,4681-4685. 

Takahashi, N., Ueda, S., Obata, M., Nikaido, T., Nakai, S., Honjo, T. (1982). Structure of human immunoglobulin gamma genes implications for evolution of a gene family. Cell 29,671-679. 

Tucker, P.W., Slightom, J.L., Blattner, F.R. (1981). Mouse IgA heavy chain gene sequence implications for evolution of immunoglobulin hinge exons. Proc. Natl. Acad. Sci USA 78,7684-7688. 

Peroxidasins (in humans also designated vascular peroxidases [18]) represent peculiar multidomain peroxidases. In PeroxiBase, 37 sequences are described. During later steps of evolution, the peroxidase domain was fused with immunoglobulin... 

Evolution of taste receptor mRNA Section 32.2.5 Photoreceptor evolution Section 32.3.4 The immunoglobulin fold Section 33.2... 

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