Evolution of immunoglobulins

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. 

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. 

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. 

Because of the ready availability of myeloma and Bence Jones proteins, a large amount of amino acid sequence data has been accumulated with mouse as well as human immunoglobulins. Comparisons of data on L chains of the two species have improved our understanding of the evolution of immunoglobulins and the nature of the variability in V regions. 

In this chapter we shall describe properties of immunoglobulins of four mammalian species that have been studied quite extensively the rabbit, mouse, guinea pig, and horse. Human inununoglobulins are considered in Chapter 3 and the pattern of evolution of immunoglobulins in vertebrates in Chapter 7. Allotypy of immunoglobulins is reviewed in Chapter 9 and will not be considered here. Because of the extensive body of information available on amino acid sequences and allotypes a more complete understanding of the structure of the immunoglobulins of these species will require reference to Chapters 4 and 9. 

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. 

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

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. 

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

Van der Stoep N, Van der Linden J, Logtenberg T Molecular evolution of the human immunoglobulin E response high incidence of shared mutations and clonal relatedness among eVH5 transcripts from three unrelated patients with atopic dermatitis. J Exp Med 1993 177 99-107. 

Members of the immunoglobulin superfamily which have been identified at present are sketched in Fig. 2. In this review, I only shall discuss in detail members (other than immunoglobulins) which consist of at least one unit meeting the standard criteria and shall only mention other more distantly related members in the context of the evolution of the whole superfamily. 

In the evolution of the immunoglobulin superfamily (Fig. 12) three critical steps can be discerned (1) the assembly of the primordial V unit. According to one hypothesis [201], the primordial building block was a unit half the size of present day... 

Malek A, Sager R, Kuhn P, Nicholaides KH, Schneider H. Evolution of maternofetal transport of immunoglobulins dnring hnman pregnancy. Am J Reprod Immunol 1996 36 248-255. 

Common Structures - Both the antibodies of the humoral response and the molecules involved in the cellular response contain elements of common structure. The similarity is even greater than Figure 7.35 suggests. The domains in these molecules are built on a common motif, called the immunoglobulin fold, in which two antiparallel sheets lie face to face (Figure 7.36). This structure probably represents the primitive structural element in the evolution of the immune response. The immunoglobulin fold is also found in a number of other proteins. 

Grenningloh, G., Bieber, A.J., Rehm, E.J., Snow, P.M., Traquina, Z.R., Hortsch, M., Patel, N.H. and Goodman, C.S. (1990) Molecular genetics of neuronal recognition in Drosophila - evolution and function of immunoglobulin superfamily cell adhesion molecules. Cold Spring Harbor Symp. Quant. Biol. 55 327-340. 

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