Characterization of a novel LTA/LPS-binding antimicrobial and anti-inflammatory temporin peptide from the skin of Fejervary limnocharis (Anura: Ranidae)

Septic shock caused by Gram-positive bacteria continues to be a major cause of morbidity and mortality in intensive care units globally. Most Temporins are excellent growth inhibitors of gram-positive bacteria and candidates for developing antimicrobial treatments due to their biological action and small molecular weight. In this study, a novel Temporin peptide from the skin of Fejervarya limnocharis frog, named as Temporin-FL, was characterized. Temporin-FL was found to adopt typical alpha-helical conformation in SDS solution and to exhibit selective antibacterial activity against Gram-positive bacteria through a membrane destruction mechanism. Accordingly, Temporin-FL showed protective effects against Staphylococcus aureus-induced sepsis in mice. Finally, Temporin-FL was demonstrated to exert anti-inflammatory effects by neutralizing the action of LPS/LTA and by inhibiting MAPK pathway activation. Therefore, Temporin-FL represents a novel candidate for molecular therapy of Gram-positive bacterial sepsis.

Automated summary

In this study, a novel Temporin peptide, named Temporin-FL, was found in the skin of Fejervarya limnocharis frog. Temporin-FL showed selective antibacterial activity against Gram-positive bacteria through a membrane destruction mechanism. It also demonstrated protective effects against Staphylococcus aureus-induced sepsis and exhibited anti-inflammatory effects by neutralizing the action of LPS/LTA and inhibiting MAPK pathway activation.