INVESTIGADORES
MARANI mariela Mirta
congresos y reuniones científicas
Título:
Novel Antimicrobial Peptides Identified From the Skin of Patagonian Frog Pleurodema Somuncurense (Anura: Leptodactylidae: Leiuperinae)
Autor/es:
CANCELARICH NATALIA L.; PÉREZ LUIS O.; MOREIRA, DANIEL C.; BARBOSA, EDER; BASSO NÉSTOR G.; LEITE JOSÉ R. S. A.; MARANI MARIELA M.
Lugar:
Brasilia
Reunión:
Encuentro; Encontro Internacional de Inovação em Saúde do Distrito Federal. Encuentro; 2018
Institución organizadora:
Facultad de Medicina, Campus Universitario Darcy Ribeiro
Resumen:
The emergence of several multi-resistant pathogenic bacteria strains has become a serious problem for public health, requiring the search for novel therapeutic molecules. The potential of antimicrobial peptides (AMPs) is known as an alternative to the conventional therapies. These molecules have shown broad-spectrum antimicrobial activities against various microorganisms, including Gram-positive and Gram-negative bacteria, fungi, and viruses [Zasloff et al., 2002]. A huge number of AMPs has been identified and isolated from amphibian skin [Patocka et al., 2018]. The aim of this work was the identification of AMPs from the skin of the Patagonian frog Pleurodema somuncurense. Adult specimen of P. somuncurense was collected at Meseta Somuncurá, Río Negro, Argentina. Total RNA from dorsal skin region was isolated using Trizol reagent. 3′RACE reactions were performed for cDNA synthesis using degenerate primers based on preserved signal peptide sequences [Vanhoye et al., 2003]. Purified PCR products were linked to the pCR?4-TOPO vector to transform E.coli DH5α competent cells. Positive clones were sequenced obtaining 11 prepropeptides. Eight sequences were synthesized and purified using F-moc chemistry and RP-HPLC, respectively. The antimicrobial activity was established against strains Escherichia coli and Staphylococcus aureus. Eight new peptides were identified, showing positive net charge, and α-helix structure with an amphipathic arrangement. Two peptides were similar to the thaulins, a family peptide previously described by our group from the skin of the Patagonian frog Pleurodema thaul [Marani et al., 2017], while the remaining showed 32-53 % of similarity to other families of amphibian AMPs. The isolates exhibited moderate antimicrobial activity against E. coli (125 ? 250 ug/ml) and S. aureus (250 ? 500 ug/ml).The discovery of these novel peptides is a step forward in the search for active molecules and contribute to the knowledge of the defense mechanisms of Patagonian amphibians.