Show simple item record

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/s41598-018-28846-4es_ES
dc.identifier.issn2045-2322
dc.identifier.urihttp://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.typeinfo:eu-repo/semantics/articlees_ES
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


Files in this item

Thumbnail
Thumbnail

This item appears in the following Collection(s)

Show simple item record

CC BY 4.0 International
Except where otherwise noted, this item's license is described as CC BY 4.0 International