CONICET | Buscador de Institutos y Recursos Humanos

Amphibian secretion is an important source of bioactive molecules that naturally protect the skin against noxious microorganisms. Collectively called Antimicrobial Peptides (AMPs), these molecules have a wide spectrum of action, targeting viruses, bacteria and fungi. Like many membrane and secretedproteins, AMPs have cleavable signal sequences that mediate and translocate the nascent polypeptide chains into the endoplasmic reticulum. Although it is accepted that the signal peptides are simple and interchangeable, there is neither sequence nor structure that is conserved among all gene families. Theyderived from a common ancestor but developed different traits as they adapt to distinct environmental pressures. The aim of this study was to provide an overview of the diversity of signal peptides of the frog, taking into account reported cDNA sequences and the evolutionary relationship among them. Weanalysed more than two thousand records, reported the relative abundance, diversity and evolutionary divergence based on the peptide signals of frog antimicrobial peptides. We conclude that the physical properties of the sequence is more important than the specific peptides in AMP signal peptides. Sincethere is significant overlapping among related genera, differences in secretion from different peptides types should be regulated by additional levels, like post-transcriptional modifications or 5´UTR sequences.