Mostrar el registro sencillo del ítem
Unveiling the nature of black mamba (Dendroaspis polylepis) venom through venomics and antivenom immunoprofiling: identification of key toxin targets for antivenom development.
dc.creator | Laustsen, Andreas Hougaard | |
dc.creator | Lomonte, Bruno | |
dc.creator | Lohse, Brian | |
dc.creator | Fernández Ulate, Julián | |
dc.creator | Gutiérrez, José María | |
dc.date.accessioned | 2016-07-07T21:27:17Z | |
dc.date.available | 2016-07-07T21:27:17Z | |
dc.date.issued | 2015-04-24 | |
dc.identifier.citation | http://www.sciencedirect.com/science/article/pii/S1874391915000561 | |
dc.identifier.issn | 1874-3919 | |
dc.identifier.uri | https://hdl.handle.net/10669/28143 | |
dc.description.abstract | The venom proteome of the black mamba, Dendroaspis polylepis, from Eastern Africa, was, for the first time, characterized. Forty- different proteins and one nucleoside were identified or assigned to protein families. The most abundant proteins were Kunitz-type proteinase inhibitors, which include the unique mamba venom components ‘dendrotoxins’, and α-neurotoxins and other representatives of the three-finger toxin family. In addition, the venom contains lower percentages of proteins from other families, including metalloproteinase, hyaluronidase, prokineticin, nerve growth factor, vascular endothelial growth factor, phospholipase A2, 5′-nucleotidase, and phosphodiesterase. Assessment of acute toxicity revealed that the most lethal components were α-neurotoxins and, to a lower extent, dendrotoxins. This venom also contains a relatively high concentration of adenosine, which might contribute to toxicity by influencing the toxin biodistribution. ELISA immunoprofiling and preclinical assessment of neutralization showed that polyspecific antivenoms manufactured in South Africa and India were effective in the neutralization of D. polylepis venom, albeit showing different potencies. Antivenoms had higher antibody titers against α-neurotoxins than against dendrotoxins, and displayed high titers against less toxic proteins of high molecular mass. Our results reveal the complexity of D. polylepis venom, and provide information for the identification of its most relevant toxins to be neutralized by antivenoms. | es_ES |
dc.description.sponsorship | University of Copenhagen, Department of Drug Design and Pharmacology | es_ES |
dc.description.sponsorship | Universidad de Costa Rica, Instituto Clodomiro Picado | es_ES |
dc.description.sponsorship | University of Copenhagen, Drug Research Academy | es_ES |
dc.description.sponsorship | Dansk Tennis Fond Oticon Fonden | es_ES |
dc.description.sponsorship | Knud Højgaards Fond | es_ES |
dc.description.sponsorship | Rudolph Als Fondet | es_ES |
dc.description.sponsorship | Henry Shaws Legat | es_ES |
dc.description.sponsorship | Læge Johannes Nicolai Krigsgaard of Hustru Else Krogsgaards Mindelegat for Medicinsk Forskning og Medicinske Studenter ved Københavns Universitet | es_ES |
dc.description.sponsorship | Lundbeckfonden | es_ES |
dc.description.sponsorship | Torben of Alice Frimodts Fond | es_ES |
dc.description.sponsorship | Frants Allings Legat | es_ES |
dc.description.sponsorship | Christian og Ottilia Brorsons Rejselegat for Yngre Videnskabsmænd- og kvinder | es_ES |
dc.description.sponsorship | Fonden for Lægevidenskabens Fremme | es_ES |
dc.language.iso | en_US | es_ES |
dc.source | Journal of Proteomics 119: 126-142 | es_ES |
dc.subject | Snake venom | es_ES |
dc.subject | Dendroaspis | es_ES |
dc.subject | proteome | es_ES |
dc.title | Unveiling the nature of black mamba (Dendroaspis polylepis) venom through venomics and antivenom immunoprofiling: identification of key toxin targets for antivenom development. | es_ES |
dc.type | artículo original | |
dc.identifier.doi | doi: 10.1016/j.jprot.2015.02.002 | |
dc.description.procedence | UCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP) | es_ES |
Ficheros en el ítem
Este ítem aparece en la(s) siguiente(s) colección(ones)
-
Microbiología [1171]