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Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A2 from Bothrops asper snake venom: synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region
dc.creator | Páramo Aguilera, Leandro Alberto | |
dc.creator | Lomonte, Bruno | |
dc.creator | Pizarro Cerdá, Javier | |
dc.creator | Bengoechea, José Antonio | |
dc.creator | Gorvel, Jean Pierre | |
dc.creator | Moreno Robles, Edgardo | |
dc.date.accessioned | 2017-11-29T21:47:57Z | |
dc.date.available | 2017-11-29T21:47:57Z | |
dc.date.issued | 1998 | |
dc.identifier.citation | http://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.1998.2530452.x/full | |
dc.identifier.issn | 1742-4658 | |
dc.identifier.uri | https://hdl.handle.net/10669/73477 | |
dc.description.abstract | Mammalian 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.sponsorship | Institut National de la Santé et de la Recherche Médicale [94NS2]/INSERM/France | es_ES |
dc.description.sponsorship | Eusko Jaurlaritza and the Universidad de Navarra of Spain/[PM92-0140-CO2]/UNAV/Spain | es_ES |
dc.description.sponsorship | International Foundation for Science/[F/1388-3F]/IFS/ Sweden | es_ES |
dc.description.sponsorship | Vicerrectoría de Investigación Universidad de Costa Rica/[741-95-264]/UCR/Costa Rica | es_ES |
dc.language.iso | en_US | es_ES |
dc.rights | CC0 1.0 Universal | * |
dc.rights.uri | http://creativecommons.org/publicdomain/zero/1.0/ | * |
dc.source | European Journal of Biochemistry; Vol. 253, pp. 452-461 | es_ES |
dc.subject | Phospholipase A2 | es_ES |
dc.subject | Myotoxin | es_ES |
dc.subject | Bactericidal | es_ES |
dc.subject | Synthetic peptide | es_ES |
dc.subject | Snake venom | es_ES |
dc.title | Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A2 from Bothrops asper snake venom: synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region | es_ES |
dc.type | artículo original | |
dc.identifier.doi | 10.1046/j.1432-1327.1998.2530452.x | |
dc.description.procedence | UCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP) | es_ES |
dc.identifier.pmid | 9654096 |
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Microbiología [1171]