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Updated: May 30, 2026
08:51
Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
Published on: March 15, 2019
Exploring Antarctic teleost immunoglobulin genes.
Maria Rosaria Coscia1, Umberto Oreste
1CNR, Institute of Protein Biochemistry, Via P. Castellino 111, 80131 Naples, Italy.
Marine Genomics
|July 30, 2011
Summary
Researchers studied immunoglobulin in Antarctic Notothenioidei fish, revealing limited heavy chain diversity and an unusually long hinge peptide. This suggests unique adaptive evolution in these abundant teleost species.
Area of Science:
- * Evolutionary biology
- * Molecular immunology
- * Antarctic marine biology
Background:
- * Notothenioidei are the most abundant teleost fish in the Antarctic Ocean.
- * Immunoglobulin is a key molecule of the immune system, crucial for adaptive immunity.
- * Understanding adaptive evolution in extreme environments like the Antarctic is vital.
Purpose of the Study:
- * To investigate adaptive evolution in Antarctic Notothenioidei.
- * To identify specific features of immunoglobulin in this species.
- * To analyze the immunoglobulin heavy chain (IGH) and light chain (IGL) in Trematomus bernacchii and related species.
Main Methods:
- * Sequencing of genomic DNA and transcripts encoding IGH from 18 notothenioid species.
- * Investigation of T. bernacchii immunoglobulin light chain and identification of three isotypes.
- * Analysis of deduced amino acid sequences and polymorphism in IGH.
Main Results:
- * Identified three isotypes of T. bernacchii immunoglobulin light chain.
- * Found limited diversity in the immunoglobulin heavy chain variable domain, with only two VH gene families in T. bernacchii.
- * Discovered an unexpectedly long hinge peptide in the secreted heavy chain, with high polymorphism.
- * Observed domain-truncated heavy chains due to alternative mRNA splicing in several species, featuring a long extracellular spacer from 39-nt repeat insertions.
Conclusions:
- * The limited VH diversity and unique hinge peptide suggest specific adaptive evolutionary pressures on immunoglobulin in Notothenioidei.
- * The polymorphic hinge peptide may play a significant biological role in the adaptive evolution of Antarctic fish.
- * Alternative splicing leading to domain-truncated IGH forms indicates novel mechanisms in immune system adaptation.
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