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dc.creatorPáramo Aguilera, Leandro Alberto
dc.creatorLomonte, Bruno
dc.creatorPizarro Cerdá, Javier
dc.creatorBengoechea, José Antonio
dc.creatorGorvel, Jean Pierre
dc.creatorMoreno Robles, Edgardo
dc.date.accessioned2017-11-29T21:47:57Z
dc.date.available2017-11-29T21:47:57Z
dc.date.issued1998
dc.identifier.citationhttp://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.1998.2530452.x/fulles_ES
dc.identifier.issn1742-4658
dc.identifier.urihttp://hdl.handle.net/10669/73477
dc.description.abstractMammalian group-II phospholipases A2 (PLA2) of inflammatory fluids display bactericidal properties, which are dependent on their enzymatic activity. This study shows that myotoxins II (Lys49) and III (Asp49), two group-II PLA2 isoforms from the venom of Bothrops asper, are lethal to a broad spectrum of bacteria. Since the catalytically inactive Lys49 myotoxin II isoform has similar bactericidal effects to its catalytically active Asp49 counterpart, a bactericidal mechanism that is independent of an intrinsic PLA2 activity is demonstrated. Moreover, a synthetic 13-residue peptide of myotoxin II, comprising residues 1152129 (common numbering system) near the C-terminal loop, reproduced the bactericidal effect of the intact protein. Following exposure to the peptide or the protein, accelerated uptake of the hydrophobic probe N-phenyl-N-naphthylamine was observed in susceptible but not in resistant bacteria, indicating that the lethal effect was initiated on the bacterial membrane. The outer membrane, isolated lipopolysaccharide (LPS), and lipid A of susceptible bacteria showed higher binding to the myotoxin II- (1152129)-peptide than the corresponding moieties of resistant strains. Bacterial LPS chimeras indicated that LPS is a relevant target for myotoxin II-(1152129)-peptide. When heterologous LPS of the resistant strain was present in the context of susceptible bacteria, the chimera became resistant, and vice versa. Myotoxin II represents a group-II PLA2 with a direct bactericidal effect that is independent of an intrinsic enzymatic activity, but adscribed to the presence of a short cluster of basic/hydrophobic amino acids near its C-terminal loop.es_ES
dc.description.sponsorshipInstitut National de la Santé et de la Recherche Médicale [94NS2]/INSERM/Francees_ES
dc.description.sponsorshipEusko Jaurlaritza and the Universidad de Navarra of Spain/[PM92-0140-CO2]/UNAV/Spaines_ES
dc.description.sponsorshipInternational Foundation for Science/[F/1388-3F]/IFS/ Swedenes_ES
dc.description.sponsorshipVicerrectoría de Investigación Universidad de Costa Rica/[741-95-264]/UCR/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.rightsCC0 1.0 Universal*
dc.rights.urihttp://creativecommons.org/publicdomain/zero/1.0/*
dc.sourceEuropean Journal of Biochemistry; Vol. 253, pp. 452-461es_ES
dc.subjectPhospholipase A2es_ES
dc.subjectMyotoxines_ES
dc.subjectBactericidales_ES
dc.subjectSynthetic peptidees_ES
dc.subjectSnake venomes_ES
dc.titleBactericidal activity of Lys49 and Asp49 myotoxic phospholipases A2 from Bothrops asper snake venom: synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal regiones_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1046/j.1432-1327.1998.2530452.x
dc.description.procedenceUCR::Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid9654096


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