Evolutionary Development of the Immunoglobulin Family

Purchase on Springer.com

$39.95 / €34.95 / £29.95*

Rent the article at a discount

Rent now

* Final gross prices may vary according to local VAT.

Get Access

Abstract

The origin of the ability of immunoglobulins (Ig) and T-cell receptors (TCRs) to specifically recognize antigens is related to the evolutionary development of proteins of the immunoglobulin superfamily (IgSF). The IgSF proteins are characterized by specific domain organization of molecules and statistically significant homology with known Ig. Four types of Ig domains (V1, V2, C1, and C2), differing from one another both in variations of their spatial organization and in the number of amino acid residues have been distinguished. Immunoglobulin superfamily comprises Ig; TCRs; class I and II major histocompatibility complex (MHC) molecules; one-domain proteins of thymocytes and T-cells (Thy-1); myelin protein P0; β2-microglobulin; two-domain proteins, such as sponge receptor tyrosine kinase (RTK), sponge adhesive protein (SAP), Drosophila tyrosine-kinase receptor (DTCR), Xenopus and human cortical-thymocyte receptors (CTX and CTH), etc.; and a large group of adhesins, coreceptors, and Ig receptors with varying number of domains. Evolutionary development of IgSF began with the evolvement of chaperones, Thy-1, and P0 of prokaryotes and unicellular eukaryotes. Mutations, duplications, and translocations of the genes controlling both V and C domains yielded proteins with different numbers and combinations of these domains. All IgSF proteins are divided into two groups. The first group includes the proteins with nonrearranging V2 domains and homophilic mode of interaction; the second, the proteins with rearranging V1 domains and heterophilic mode of interaction (Ig, TCRs). The ability for heterophilic antigen-binding mode of interaction was apparently acquired due to the introduction of recombination-activating retroviral genes (RAG1 and RAG2) into the genome of Gnathostomata ancestors.