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dc.creatorSantamaría Quesada, Carlos Manuel
dc.creatorLarios Ramos, Silda
dc.creatorAngulo Ugalde, Yamileth
dc.creatorPizarro Cerdá, Javier
dc.creatorGorvel, Jean Pierre
dc.creatorMoreno Robles, Edgardo
dc.creatorLomonte, Bruno
dc.date.accessioned2018-02-27T15:39:45Z
dc.date.available2018-02-27T15:39:45Z
dc.date.issued2005
dc.identifier.citationhttps://www.sciencedirect.com/science/article/pii/S0041010104003885
dc.identifier.urihttps://hdl.handle.net/10669/74163
dc.description.abstractA short peptide derived from the C-terminal region of Bothrops asper myotoxin II, a Lys49 phospholipase A2 (PLA2), was previously found to reproduce the bactericidal activity of its parent molecule. In this study, a panel of eight PLA2 myotoxins purified from crotalid snake venoms, including both Lys49 and Asp49-type isoforms, were all found to express bactericidal activity, indicating that this may be a common action of the group IIA PLA2 protein family. A series of 10 synthetic peptide variants, based on the original C-terminal sequence 115–129 of myotoxin II and its triple Tyr/Trp substituted peptide p115- W3, were characterized. In vitro assays for bactericidal, cytolytic and anti-endotoxic activities of these peptides suggest a general correlation between the number of tryptophan substitutions introduced and microbicidal potency, both against Gramnegative (Salmonella typhimurium) and Gram-positive (Staphylococcus aureus) bacteria. Peptide variants with high bactericidal activity also tended to be more cytolytic towards skeletal muscle C2C12 myoblasts, thus limiting their potential in vivo use. However, the peptide variant pEM-2 (KKWRWWLKALAKK) showed reduced toxicity towards muscle cells, while retaining high bactericidal potency. This peptide also showed the highest endotoxin-neutralizing activity in vitro, and was shown to functionally interact with lipopolysaccharide (LPS) using a chimeric bacteria model. The bactericidal and antiendotoxic properties of pEM-2, combined with its relatively low toxicity towards eukaryotic cells, highlight it as a promising candidate for further evaluation of its antimicrobial potential in vivo.es_ES
dc.description.sponsorshipNeTropica Sweden-Central America network/[01-R-2003]//Sueciaes_ES
dc.description.sponsorshipAmerican Society for Microbiology-MIRCEN/[]//Estados Unidoses_ES
dc.description.sponsorshipLindbergh Foundation/[]//Estados Unidoses_ES
dc.description.sponsorshipCRUSA Foundation/[]//Estados Unidoses_ES
dc.description.sponsorshipFlorida, Ice and Farm Company/[]//Costa Ricaes_ES
dc.description.sponsorshipEmbassy of France/[]//Costa Ricaes_ES
dc.description.sponsorshipEmbassy of Japan/[]//Costa Ricaes_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-99-269]/UCR/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.sourceToxicon 45, 807-815 (2005)es_ES
dc.subjectmyotoxines_ES
dc.subjectantimicrobiales_ES
dc.subjectSnake venomes_ES
dc.titleAntimicrobial activity of myotoxic phospholipases A2 from crotalid snake venoms and synthetic peptide variants derived from their C-terminal regiones_ES
dc.typeartículo original
dc.identifier.doi10.1016/j.toxicon.2004.09.012
dc.identifier.doi0041-0101
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.description.procedenceUCR::Vicerrectoría de Docencia::Salud::Facultad de Medicina::Escuela de Medicinaes_ES
dc.identifier.codproyecto741-99-269
dc.identifier.pmid15904676


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