Identification of cathelicidin gene from Hoplobatrachus rugulosus and the antioxidant capacity of PC29 peptide

Abstract

Cathelicidins, a group of vertebrate multifunctional molecules, play a role in innate immunity. In this study, a cathelicidin was identified from the lungs of frogs, Hoplobatrachus rugulosus. A 474 base pairs (bp) complementary DNA (cDNA) sequence encoded a 157 amino acid residue prepropeptide of H. rugulosus cathelicidin (cathelicidin-HR), which consisting of a 20-residue signal peptide sequence, a 108-residue cathelin region, and a 29-residue cathelicidin-HR peptide. Amino acid sequence alignment and cladogram analysis illustrated that cathelicidin-HR have a high degree of similarity to further amphibian cathelicidins. The cathelicidin-HR peptide displays very low antimicrobial activity but exhibits dose-dependent antioxidant activity. Moreover, this peptide expresses DNA damage inhibition against UV/H2O2-induction. The molecular docking indicated that DNA damage protection of cathelicidin-HR might occur via DNA-peptide complex formation. This is the first amphibian cathelicidin peptide that possesses DNA damage inhibitory activity which might play a crucial role in oxidative stress.