Origin and Functional Diversification of an Amphibian Defense Peptide Arsenal

Roelants, Kim, Fry, Bryan G., Ye, Lumeng, Stijlemans, Benoit, Brys, Lea, Kok, Philippe, Clynen, Elke, Schoofs, Liliane, Cornelis, Pierre and Bossuyt, Franky (2014) Origin and Functional Diversification of an Amphibian Defense Peptide Arsenal. Plos Genetics, 9 8: e1003662.1-e1003662.15. doi:10.1371/journal.pgen.1003662

Author Roelants, Kim
Fry, Bryan G.
Ye, Lumeng
Stijlemans, Benoit
Brys, Lea
Kok, Philippe
Clynen, Elke
Schoofs, Liliane
Cornelis, Pierre
Bossuyt, Franky
Title Origin and Functional Diversification of an Amphibian Defense Peptide Arsenal
Journal name Plos Genetics   Check publisher's open access policy
ISSN 1553-7390
Publication date 2014-01-01
Year available 2013
Sub-type Article (original research)
DOI 10.1371/journal.pgen.1003662
Open Access Status DOI
Volume 9
Issue 8
Start page e1003662.1
End page e1003662.15
Total pages 16
Place of publication San Francisco, CA United States
Publisher Public Library of Science
Language eng
Formatted abstract
The skin secretion of many amphibians contains an arsenal of bioactive molecules, including hormone-like peptides (HLPs) acting as defense toxins against predators, and antimicrobial peptides (AMPs) providing protection against infectious microorganisms. Several amphibian taxa seem to have independently acquired the genes to produce skin-secreted peptide arsenals, but it remains unknown how these originated from a non-defensive ancestral gene and evolved diverse defense functions against predators and pathogens. We conducted transcriptome, genome, peptidome and phylogenetic analyses to chart the full gene repertoire underlying the defense peptide arsenal of the frog Silurana tropicalis and reconstruct its evolutionary history. Our study uncovers a cluster of 13 transcriptionally active genes, together encoding up to 19 peptides, including diverse HLP homologues and AMPs. This gene cluster arose from a duplicated gastrointestinal hormone gene that attained a HLP-like defense function after major remodeling of its promoter region. Instead, new defense functions, including antimicrobial activity, arose by mutation of the precursor proteins, resulting in the proteolytic processing of secondary peptides alongside the original ones.Although gene duplication did not trigger functional innovation, it may have subsequently facilitated the convergent loss of the original function in multiple gene lineages (subfunctionalization), completing their transformation from HLP gene to AMP gene. The processing of multiple peptides from a single precursor entails a mechanism through which peptide-encoding genes may establish new functions without the need for gene duplication to avoid adaptive conflicts with older ones.
Keyword Xenopus Muelleri Pipidae
Antimicrobial Peptides
Skin Secretions
Clawed Frogs
Batrachochytrium dendrobatidis
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Biological Sciences Publications
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Citation counts: TR Web of Science Citation Count  Cited 16 times in Thomson Reuters Web of Science Article | Citations
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