Identification and characterization of an antimicrobial peptide of Hypsiboas semilineatus (Spix, 1824) (Amphibia, Hylidae).
Toxicon
; 99: 16-22, 2015 Jun 01.
Article
in En
| 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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Anura
/
Skin
/
Antimicrobial Cationic Peptides
/
Amphibian Proteins
/
Drug Discovery
/
Gram-Positive Bacteria
/
Anti-Infective Agents
Type of study:
Diagnostic_studies
Limits:
Animals
/
Humans
Country/Region as subject:
America do sul
/
Brasil
Language:
En
Journal:
Toxicon
Year:
2015
Document type:
Article
Affiliation country:
Brazil