Host defense peptides from Lithobates forreri, Hylarana luctuosa, and Hylarana signata (Ranidae): Phylogenetic relationships inferred from primary structures of ranatuerin-2 and brevinin-2 peptides

J. Michael Conlon, Jolanta Kolodziejek, Milena Mechkarska, Laurent Coquet, Jérôme Leprince, Thierry Jouenne, Hubert Vaudry, Per F. Nielsen, Norbert Nowotny, Jay D. King

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The primary structures of host-defense peptides present in frog skin secretions constitute useful molecular markers for establishing taxonomic classifications and investigating phylogenetic relationships between species within a particular genus. Peptidomic analysis has led to the characterization of multiple host-defense peptides in norepinephrine-stimulated skin secretions of three species of frogs from the family Ranidae: Lithobates forreri (Boulenger, 1883), Hylarana luctuosa (Peters, 1871), and Hylarana signata (Günther, 1872). The L. forreri secretions contain ranatuerin-2 (2 peptides), brevinin-1 (4 peptides), and temporin (1 peptide). The H. luctuosa secretions contain brevinin-2 (4 peptides), esculentin-1 (1 peptide), esculentin-2 (1 peptide), palustrin-2 (2 peptides), and temporin (2 peptides). The H. signata secretions contain brevinin-2 (4 peptides), brevinin-1 (5 peptides), palustrin-2 (1 peptide), and temporin (2 peptides). Cladistic analysis based upon the primary structures of 44 ranatuerin-2 peptides from 20 Lithobates species indicates a close phylogenetic relationship between L. forreri, Lithobates onca, and Lithobates yavapaiensis. A similar cladistic analysis based upon the primary structures of 27 brevinin-2 peptides from 8 Hylarana species provides support for a close phylogenetic relationship between H. signata and Hylarana picturata, while showing that the species are not conspecific, with H. luctuosa more distantly related.

Original languageEnglish
Pages (from-to)49-57
Number of pages9
JournalComparative Biochemistry and Physiology - Part D: Genomics and Proteomics
Volume9
Issue number1
DOIs
Publication statusPublished - Mar 2014

Fingerprint

Ranidae
Peptides
ranatuerin
esculentin steroid
Anura
Skin

Keywords

  • Antimicrobial peptide Lithobates
  • Brevinin-2
  • Hylarana
  • Phylogeny
  • Ranatuerin-2

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology
  • Physiology

Cite this

Host defense peptides from Lithobates forreri, Hylarana luctuosa, and Hylarana signata (Ranidae) : Phylogenetic relationships inferred from primary structures of ranatuerin-2 and brevinin-2 peptides. / Conlon, J. Michael; Kolodziejek, Jolanta; Mechkarska, Milena; Coquet, Laurent; Leprince, Jérôme; Jouenne, Thierry; Vaudry, Hubert; Nielsen, Per F.; Nowotny, Norbert; King, Jay D.

In: Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics, Vol. 9, No. 1, 03.2014, p. 49-57.

Research output: Contribution to journalArticle

Conlon, J. Michael ; Kolodziejek, Jolanta ; Mechkarska, Milena ; Coquet, Laurent ; Leprince, Jérôme ; Jouenne, Thierry ; Vaudry, Hubert ; Nielsen, Per F. ; Nowotny, Norbert ; King, Jay D. / Host defense peptides from Lithobates forreri, Hylarana luctuosa, and Hylarana signata (Ranidae) : Phylogenetic relationships inferred from primary structures of ranatuerin-2 and brevinin-2 peptides. In: Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics. 2014 ; Vol. 9, No. 1. pp. 49-57.
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