Antimicrobial peptides in the skin secretions of anurans constitute a component of the innate immunity that protects the organism against invading pathogens. Four peptides with antimicrobial activity were isolated in high yield from norepinephrine-stimulated skin secretions of the Northern red-legged frog Rana aurora aurora and their primary structures determined. Ranatuerin-2AUa (GILSSFKGVAKGVAKNLAGKLLDELKCKITGC) showed potent growth-inhibitory activity against a range of Gram-positive and Gram-negative bacteria (minimum inhibitory concentrations <20 μM) but low hemolytic activity against human erythrocytes (50% hemolysis at 290 μM). Brevinin-1AUa (FLPILAGLAAKLVPKVFCSITKKC) and brevinin-1AUb (FLPILAGLAANILPKVFCSITKKC) also showed potent antimicrobial activity but were strongly hemolytic (HC 50<10 μM). Temporin-1AUa (FLPIIGQLLSGLL.NH2) atypically lacked a basic amino acid residue and showed very weak antimicrobial and hemolytic activity. Its biological function remains to be established. The primary structures of the antimicrobial peptides are consistent with a close phylogenetic relationship between R. aurora, Rana boylii and Rana luteiventris.
- Antimicrobial peptide
- Frog skin
- HC, concentration producing 50% hemolysis
- MIC, minimum inhibitory concentration
ASJC Scopus subject areas
- Developmental Biology