Abstract
The existence of a well-developed immune system is restricted to the vertebrates. Foreign substances are recognized by antibodies that exhibit an almost endless variety of antigen-combining sites. Although some of the antibody variability may be due to somatic mutations, the vertebrate genome contains substantial numbers of genes coding for immunoglobulin variable regions (see Scidman et al., 1978). It appears possible that these sets of genes evolved under environmental selection by a gradual expansion of duplicated and mutated genes. At some time during the course of this development, the gene products may have occurred as a family of proteins displaying a restricted genetic polymorphism. These ancestral proteins may have participated in recognitive processes such as the discrimination between self and nonself wherein genetic polymorphism should have provided a selective advantage. Assuming that the evolution of the variable regions included organisms lacking a circulatory system, it can be envisaged that the predecessors of the immunoglobulins were cell-surface proteins.
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Peterson, P.A., Kämpe, O. (1981). Are the Classic Transplantation Antigens Primitive Cell-Surface Antibodies?. In: Reisfeld, R.A., Ferrone, S. (eds) Current Trends in Histocompatibility. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3758-4_18
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DOI: https://doi.org/10.1007/978-1-4684-3758-4_18
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