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Toxicon ; 99: 16-22, 2015 Jun 01.
Article in English | MEDLINE | ID: mdl-25772860

ABSTRACT

The multidrug-resistant bacteria have become a serious problem to public health. In this scenery the antimicrobial peptides (AMPs) derived from animals and plants emerge as a novel therapeutic modality, substituting or in addition to the conventional antimicrobial. The anurans are one of the richest natural sources of AMPs. In this work several cycles of cDNA cloning of the skin of the Brazilian treefrog Hypsiboas semilineatus led to isolation of a precursor sequence that encodes a new AMP. The sequence comprises a 27 residue signal peptide, followed by an acidic intervening sequence that ends in the mature peptide at the carboxy terminal. The AMP, named Hs-1, has 20 amino acids residues, mostly arranged in an alpha helix and with a molecular weight of 2144.6 Da. The chemically synthesized Hs-1 showed an antimicrobial activity against all Gram-positive bacteria tested, with a range of 11-46 µM, but it did not show any effect against Gram-negative bacteria, which suggest that Hs-1 may have a selective action for Gram-positive bacteria. The effects of Hs-1 on bacterial cells were also demonstrated by transmission electron microscopy. Hs-1 is the first AMP to be described from H. semilineatus.


Subject(s)
Amphibian Proteins/pharmacology , Anti-Infective Agents/pharmacology , Antimicrobial Cationic Peptides/pharmacology , Anura/metabolism , Drug Discovery , Gram-Positive Bacteria/drug effects , Skin/chemistry , Amino Acid Sequence , Amphibian Proteins/adverse effects , Amphibian Proteins/chemistry , Amphibian Proteins/genetics , Animals , Anti-Infective Agents/adverse effects , Anti-Infective Agents/chemistry , Anti-Infective Agents/isolation & purification , Antimicrobial Cationic Peptides/adverse effects , Antimicrobial Cationic Peptides/chemistry , Antimicrobial Cationic Peptides/genetics , Base Sequence , Blood Cells/drug effects , Brazil , DNA, Complementary/chemistry , Forests , Gram-Positive Bacteria/growth & development , Gram-Positive Bacteria/ultrastructure , Humans , Microbial Sensitivity Tests , Microscopy, Electron, Transmission , Molecular Sequence Data , Molecular Weight , Protein Stability , Protein Structure, Secondary , Recombinant Proteins/adverse effects , Recombinant Proteins/chemistry , Recombinant Proteins/isolation & purification , Recombinant Proteins/pharmacology
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