Abstract
The phylogenetic relationship between the relict leopard frog Lithobates (Rana) onca (Cope, 1875) and the lowland leopard frog Lithobates (Rana) yavapaiensis (Platz and Frost, 1984) is unclear. Chromatographic analysis of norepinephrine-stimulated skin secretions from L. onca led to the identification of six peptides with antimicrobial activity. Determination of their primary structures indicated that four of the peptides were identical to brevinin-1Ya, brevinin-1Yb, brevinin-1Yc and ranatuerin-2Ya previously isolated from skin secretions of L. yavapaiensis. However, a peptide belonging to the temporin family (temporin-ONa: FLPTFGKILSGLF.NH2) and an atypical member of the ranatuerin-2 family containing a C-terminal cyclic heptapeptide domain (ranatuerin-2ONa: GLMDTVKNAAKNLAGQMLDKLKCKITGSC) were isolated from the L. onca secretions but were not present in the L. yavapaiensis secretions. Ranatuerin-2ONa inhibited the growth of Escherichia coli (MIC = 50 μM) and Candida albicans (MIC = 100 μM ) and showed hemolytic activity (LC50 = 90 μM) but was inactive against Staphylococcus aureus. The data indicate a close phylogenetic relationship between L. onca and L. yavapaiensis but suggest that they are not conspecific species.
Original language | English |
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Pages (from-to) | 313-317 |
Number of pages | 5 |
Journal | Comparative Biochemistry and Physiology - C Toxicology and Pharmacology |
Volume | 151 |
Issue number | 3 |
DOIs | |
Publication status | Published - Apr 2010 |
Externally published | Yes |
Keywords
- Antimicrobial peptide
- Brevinin-1
- Frog skin
- Ranatuerin-2
- Temporin
ASJC Scopus subject areas
- Biochemistry
- Physiology
- Aquatic Science
- Animal Science and Zoology
- Toxicology
- Cell Biology
- Health, Toxicology and Mutagenesis