2. Academic Validation
  3. Peptidomic analysis of the host-defense peptides in skin secretions of the Amazon River frog Lithobates palmipes (Ranidae)

Peptidomic analysis of the host-defense peptides in skin secretions of the Amazon River frog Lithobates palmipes (Ranidae)

  • Comp Biochem Physiol Part D Genomics Proteomics. 2023 Jun:46:101069. doi: 10.1016/j.cbd.2023.101069.
Milena Mechkarska 1,  Gervonne Barran 1,  Jolanta Kolodziejek 2,  Laurent Coquet 3,  Jérôme Leprince 3,  Thierry Jouenne 4,  Norbert Nowotny 5,  J Michael Conlon 6
Affiliations

Affiliations

  • 1 Department of Life Sciences, The University of the West Indies, St Augustine, Trinidad and Tobago.
  • 2 Viral Zoonoses, Emerging and Vector-Borne Infections Group, Institute of Virology, University of Veterinary Medicine, A-1210 Vienna, Austria.
  • 3 Université Rouen Normandie, CNRS UAR2026, HeRacLeS-PISSARO PBS UMR 6270, F-76000 Rouen, France; Université Rouen Normandie, INSERM US51, NorDiC U1239, PRIMACEN, F-76000 Rouen, France.
  • 4 Université Rouen Normandie, CNRS UAR2026, HeRacLeS-PISSARO PBS UMR 6270, F-76000 Rouen, France.
  • 5 Viral Zoonoses, Emerging and Vector-Borne Infections Group, Institute of Virology, University of Veterinary Medicine, A-1210 Vienna, Austria; Department of Basic Medical Sciences, College of Medicine, Mohammed Bin Rashid University of Medicine and Health Sciences, P.O. Box 505055, Dubai Healthcare City, Dubai, United Arab Emirates.
  • 6 Diabetes Research Centre, School of Biomedical Sciences, Ulster University, Coleraine BT52 1SA, N. Ireland, UK. Electronic address: m.conlon@ulster.ac.uk.
PMID: 36868141 DOI: 10.1016/j.cbd.2023.101069
Abstract

Skin secretions of certain frog species represent a source of host-defense Peptides (HDPs) with therapeutic potential and their primary structures provide insight into taxonomic and phylogenetic relationships. Peptidomic analysis was used to characterize the HDPs in norepinephrine-stimulated skin secretions from the Amazon River frog Lithobates palmipes (Ranidae) collected in Trinidad. A total of ten Peptides were purified and identified on the basis of amino acid similarity as belonging to the ranatuerin-2 family (ranatuerin-2PMa, -2PMb, -2PMc, and-2PMd), the brevinin-1 family (brevinin-1PMa, -1PMb, -1PMc and des(8-14)brevinin-1PMa) and the temporin family (temporin-PMa in C-terminally amidated and non-amidated forms). Deletion of the sequence VAAKVLP from brevinin-1PMa (FLPLIAGVAAKVLPKIFCAISKKC) in des[(8-14)brevinin-1PMa resulted in a 10-fold decrease in potency against Staphylococcus aureus (MIC = 31 μM compared with 3 μM) and a > 50-fold decrease in hemolytic activity but potency against Echerichia coli was maintained (MIC = 62.5 μM compared with 50 μM). Temporin-PMa (FLPFLGKLLSGIF.NH2) inhibited growth of S. aureus (MIC = 16 μM) but the non-amidated form of the peptide lacked antimicrobial activity. Cladistic analysis based upon the primary structures of ranaturerin-2 Peptides supports the division of New World frogs of the family Ranidae into the genera Lithobates and Rana. A sister-group relationship between L. palmipes and Warszewitsch's frog Lithobates warszewitschii is indicated within a clade that includes the Tarahumara frog Lithobates tarahumarae. The study has provided further evidence that peptidomic analysis of HDPs in frog skin secretions is a valuable approach to elucidation of the evolutionary history of species within a particular genus.

Keywords

Antimicrobial; Brevinin-1; Frog skin; Host-defense peptide; Ranatuerin-2; Temporin.

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