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dc.creatorSantamaría Quesada, Carlos Manuel
dc.creatorLarios Ramos, Silda
dc.creatorQuirós Barrantes, Steve
dc.creatorPizarro Cerdá, Javier
dc.creatorGorvel, Jean Pierre
dc.creatorLomonte, Bruno
dc.creatorMoreno Robles, Edgardo
dc.date.accessioned2018-01-11T20:56:00Z
dc.date.available2018-01-11T20:56:00Z
dc.date.issued2005
dc.identifier.citationhttp://aac.asm.org/content/49/4/1340es_ES
dc.identifier.issn0066-4804
dc.identifier.issn1098-6596
dc.identifier.otherPMC1068596
dc.identifier.urihttps://hdl.handle.net/10669/73832
dc.description.abstractThe activities of short synthetic, nonhemolytic peptides derived from the C-terminal region of myotoxin II, a catalytically inactive phospholipase A2 homologue present in the venom of the snake Bothrops asper, have been shown to reproduce the bactericidal activity of the parent protein. They combine cationic and hydrophobic- aromatic amino acids, thus functionally resembling the antimicrobial peptides of innate defenses. This study evaluated the antimicrobial and antiendotoxic properties of a 13-mer derivative peptide of the C-terminal sequence from positions 115 to 129 of myotoxin II, named pEM-2. This peptide (KKWRWWLKALAKK) showed bactericidal activity against both gram-positive and gram-negative bacteria. In comparison to previously described peptide variants derived from myotoxin II, the toxicity of pEM-2 toward eukaryotic cells in culture was significantly reduced, being similar to that of lactoferricin B but lower than that of polymyxin B. The all-D enantiomer of pEM-2 [pEM-2 (D)] retained the same bactericidal potency of its L-enantiomeric counterpart, but it showed an enhanced ability to counteract the lethal activity of an intraperitoneal lipopolysaccharide challenge in mice, which correlated with a significant reduction of the serum tumor necrosis factor alpha levels triggered by this endotoxin. Lethality induced by intraperitoneal infection of mice with Escherichia coli or Salmonella enterica serovar Typhimurium was reduced by the administration of pEM-2 (D). These results demonstrate that phospholipase A2-derived peptides may have the potential to counteract microbial infections and encourage further evaluations of their actions in vivoes_ES
dc.description.sponsorshipRed para la Investigación y el Entrenamiento en Enfermedades Tropicales/[01-R-2003]/NeTropica/Costa Ricaes_ES
dc.description.sponsorshipThe Lindbergh Foundation/[]//EE.UUes_ES
dc.description.sponsorshipThe AmericanSociety for Microbiology/[]/MIRCEN//EE.UUes_ES
dc.description.sponsorshipThe Florida, Ice & Farm of Costa Rica/[]//Costa Ricaes_ES
dc.description.sponsorshipThe CR-USA Foundation/[]//Costa Ricaes_ES
dc.description.sponsorshipThe University of Costa Rica/[]/UCR/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.rightsCC0 1.0 Universal*
dc.rights.urihttp://creativecommons.org/publicdomain/zero/1.0/*
dc.sourceAntimicrobial Agents and Chemotherapy, vol.49(4), pp.1340-1345es_ES
dc.subjectSnake Venomes_ES
dc.subjectPhospholipase A2es_ES
dc.subjectMyotoxin IIes_ES
dc.titleBactericidal and anti-endotoxic properties of short cationic peptides derived from a snake venom Lys49 phospholipase A2es_ES
dc.typeartículo científicoes_ES
dc.identifier.doi10.1128/AAC.49.4.1340-1345.2005
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid15793109


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CC0 1.0 Universal
Except where otherwise noted, this item's license is described as CC0 1.0 Universal