Abstract
Temporins are antimicrobial peptides secreted by the granular glands of the European red frog (Rana temporaria). They are 10–14 amino acid long polypeptides active prevalently against gram positive bacteria. This study shows that a synthetic temporin B analogue (TB-YK), acquires the capacity to act in synergism with temporin A and to exert antimicrobial and anti-inflammatory activity in vivo against gram positive and gram negative bacteria. Administration of 3.4 mg/Kg of temporin A (TA)+1.6 mg/Kg TB-YK, given to individual mice concurrently with a lethal dose of bacteria (gram positive or negative), rescued 100% of the animals. More importantly, the same doses of temporins, administered one week after experimental infection with a sub lethal dose of bacteria, sterilized 100% of the animals within 3–6 days. Also, it is described an animal model based on the use of sub lethal doses of bacteria, which closely mimics bacterial infection in humans. The model offers the possibility to test in a preclinical setting the true potential of TA and TB-YK in combination as antimicrobial and anti-inflammatory agents.
Highlights
Antimicrobial peptides (AMP) are essential components of the innate immune system of plants and animals, including humans [1]
For the in vivo studies peptides need to be labelled with fluorescent dyes; we obtained temporin A derivatized with rhodamine (TA-Rho) and Temporin B derivatized with a fluoresceine (TB-Fluo)
Addition of two extra positive charged lysine residues at the N-terminus conferred to the analogue (TB-YK) a strong synergism with the native temporin A (Table 2)
Summary
Antimicrobial peptides (AMP) are essential components of the innate immune system of plants and animals, including humans [1]. Temporins are AMPs produced and secreted by the granular glands of the European red frog (Rana temporaria) [6,7]. They are amphipathic ahelical polypeptides, 10–14 amino acid long, containing only 1 or 2 positively charged amino acids (R or K). These peptides are amidated at the C-terminus as a result of an enzymatic posttranslational reaction [8]. Temporins A and B, in combination with Temporin L, show anti-bacterial activity against
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