Chickens, more than humans, focus the diversity of their immunoglobulin genes on the complementarity-determining region but utilise amino acids, indicative of a more cross-reactive antibody repertoire

Jessica Mallaby, Joseph Ng, Alex Stewart, Emma Sinclair, Deborah Dunn-Walters, Uri Hershberg

Research output: Contribution to journalArticlepeer-review

Abstract

The mechanisms of B-cell diversification differ greatly between aves and mammals, but both produce B cells and antibodies capable of supporting an effective immune response. To see how differences in the generation of diversity might affect overall repertoire diversity, we have compared the diversity characteristics of immunoglobulin genes from domestic chickens to those from humans. Both use V(D)J gene rearrangement and somatic hypermutation, but only chickens use somatic gene conversion. A range of diversity analysis tools were used to investigate multiple aspects of amino acid diversity at both the germline and repertoire levels. The effect of differing amino acid usages on antibody characteristics was assessed. At both the germline and repertoire levels, chickens exhibited lower amino acid diversity in comparison to the human immunoglobulin genes, especially outside of the complementarity-determining region (CDR). Chickens were also found to possess much larger and more hydrophilic CDR3s with a higher predicted protein binding potential, suggesting that the antigen-binding site in chicken antibodies is more flexible and more polyreactive than that seen in human antibodies.

Original languageEnglish
Article number837246
JournalFrontiers in Immunology
Volume13
DOIs
StatePublished - 8 Dec 2022

Bibliographical note

Publisher Copyright:
Copyright © 2022 Mallaby, Ng, Stewart, Sinclair, Dunn-Walters and Hershberg.

Keywords

  • B cell
  • amino acid
  • avian
  • diversity
  • human
  • immunoglobulin

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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