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dc.creatorLina Massimino, Maria
dc.creatorSimonato, Morena
dc.creatorSpolaore, Barbara
dc.creatorFranchin, Cinzia
dc.creatorArrigoni, Giorgio
dc.creatorMarin, Oriano
dc.creatorMonturiol Gross, Laura
dc.creatorFernández Ulate, Julián
dc.creatorLomonte, Bruno
dc.creatorTonello, Fiorella
dc.date.accessioned2019-01-15T16:14:37Z
dc.date.available2019-01-15T16:14:37Z
dc.date.issued2018
dc.identifier.citationhttps://www.nature.com/articles/s41598-018-28846-4
dc.identifier.issn2045-2322
dc.identifier.urihttps://hdl.handle.net/10669/76390
dc.description.abstractPhospholipases A2 are a major component of snake venoms. Some of them cause severe muscle necrosis through an unknown mechanism. Phospholipid hydrolysis is a possible explanation of their toxic action, but catalytic and toxic properties of PLA2s are not directly connected. In addition, viperid venoms contain PLA2-like proteins, which are very toxic even if they lack catalytic activity due to a critical mutation in position 49. In this work, the PLA2-like Bothrops asper myotoxin-II, conjugated with the fluorophore TAMRA, was found to be internalized in mouse myotubes, and in RAW264.7 cells. Through experiments of protein fishing and mass spectrometry analysis, using biotinylated Mt-II as bait, we found fifteen proteins interacting with the toxin and among them nucleolin, a nucleolar protein present also on cell surface. By means of confocal microscopy, Mt-II and nucleolin were shown to colocalise, at 4 °C, on cell membrane where they form Congo-red sensitive assemblies, while at 37 °C, 20 minutes after the intoxication, they colocalise in intracellular spots going from plasmatic membrane to paranuclear and nuclear area. Finally, nucleolin antagonists were found to inhibit the Mt-II internalization and toxic activity and were used to identify the nucleolin regions involved in the interaction with the toxines_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-B4-100]/UCR/Costa Ricaes_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-B5-602]/UCR/Costa Ricaes_ES
dc.description.sponsorshipInternational Center for Genetic Engineering and Biotechnology/[CRP/13/006]/ICGEB/Indiaes_ES
dc.language.isoen_USes_ES
dc.rightsCC BY 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.sourceScientific Reports, vol.8(10619), pp. 1-14.es_ES
dc.subjectVenomes_ES
dc.subjectSnakees_ES
dc.subjectMyotoxines_ES
dc.subjectReceptores_ES
dc.subject615.94 Venenos animaleses_ES
dc.titleCell surface nucleolin interacts with and internalizes Bothrops asper Lys49 phospholipase A2 and mediates its toxic activityes_ES
dc.typeartículo original
dc.identifier.doi10.1038/s41598-018-28846-4
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 Microbiologíaes_ES
dc.identifier.codproyecto741-B4-100
dc.identifier.codproyecto741-B5- 602


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CC BY 4.0 International
Excepto si se señala otra cosa, la licencia del ítem se describe como CC BY 4.0 International