Publication

Evolutionary Genomics of Immunoglobulin-Encoding Loci in Vertebrates

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Last modified
  • 03/05/2025
Type of Material
Authors
    Sabyasachi Das, Emory UniversityMasayuki Hirano, Emory UniversityRea Tako, California State University FullertonChelsea McCallister, California State University FullertonNikolas Nikolaidis, California State University Fullerton
Language
  • English
Date
  • 2012-04-01
Publisher
  • Bentham Science Publishers
Publication Version
Copyright Statement
  • © 2012 Bentham Science Publishers.
License
Final Published Version (URL)
Title of Journal or Parent Work
ISSN
  • 1389-2029
Volume
  • 13
Issue
  • 2
Start Page
  • 95
End Page
  • 102
Grant/Funding Information
  • CM is supported by the Bradshaw Scholarship in Immunology and a grant from the FDC at California State University Fullerton (CSUF).
  • NN is supported by start-up funds from CSUF, a Faculty-Student research Grant from CSUPERB, and a state-mini grant from CSUF.
  • RT is supported by a grant from FDC at CSUF.
  • SD and MH are supported by a grant from the National Institute of Health (NIH) to Max D. Cooper.
Abstract
  • Immunoglobulins (or antibodies) are an essential element of the jawed vertebrate adaptive immune response system. These molecules have evolved over the past 500 million years and generated highly specialized proteins that recognize an extraordinarily large number of diverse substances, collectively known as antigens. During vertebrate evolution the diversification of the immunoglobulin-encoding loci resulted in differences in the genomic organization, gene content, and ratio of functional genes and pseudogenes. The tinkering process in the immunoglobulin-encoding loci often gave rise to lineage-specific characteristics that were formed by selection to increase species adaptation and fitness. Immunoglobulin loci and their encoded antibodies have been shaped repeatedly by contrasting evolutionary forces, either to conserve the prototypic structure and mechanism of action or to generate alternative and diversified structures and modes of function. Moreover, evolution favored the development of multiple mechanisms of primary and secondary antibody diversification, which are used by different species to effectively generate an almost infinite collection of diverse antibody types. This review summarizes our current knowledge on the genomics and evolution of the immunoglobulin-encoding loci and their protein products in jawed vertebrates.
Author Notes
  • Address correspondence to Nikolas Nikolaidis at the 800 North State College Blvd, Department of Biological Science, California State University Fullerton, Fullerton, CA 92834, USA; Tel: 657-278-4526, 657-278-5045; Fax: 657-278-3426; E-mail: nnikolaidis@fullerton.edu
Keywords
Research Categories
  • Biology, General
  • Health Sciences, Pathology

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