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Structural and functional characterization of myotoxin I, a Lys49 phospholipase A2 homologue from the venom of the snake Bothrops atrox
dc.creator | Núñez Rangel, Vitelbina | |
dc.creator | Arce, Viviana | |
dc.creator | Gutiérrez, José María | |
dc.creator | Lomonte, Bruno | |
dc.date.accessioned | 2017-02-07T20:23:52Z | |
dc.date.available | 2017-02-07T20:23:52Z | |
dc.date.issued | 2004-07 | |
dc.identifier.citation | http://www.sciencedirect.com/science/article/pii/S0041010104001837 | |
dc.identifier.issn | 0041-0101 | |
dc.identifier.uri | https://hdl.handle.net/10669/29513 | |
dc.description.abstract | A new myotoxin was isolated from the venom of Bothrops atrox from Colombia. B. atrox myotoxin I is a homodimer, with a subunit molecular mass of 13,826, and a pI of 8.9. Its complete nucleotide sequence was obtained by cDNA cloning, indicating a mature product of 122 residues that belongs to the family of Lys49 phospholipase A2 (PLA2) homologues, a subgroup of catalytically inactive proteins within the group IIA. Accordingly, the toxin was devoid of phospholipase and anticoagulant activities, in vitro. In mice, it induced conspicuous local myonecrosis, edema, and a systemic interleukin-6 response. In vitro, it was cytolytic upon myoblasts, and weakly bactericidal. The toxin showed highest homology with other Lys49 PLA2s, both in its primary and three-dimensional modeled structure, although with an evident difference in the C-terminal region. Unlike Lys49 proteins of American crotalids having 121 residues, this toxin presents an insertion (Asn) between positions 118 and 119. Despite several substitutions within the C-terminal region 115–129 between B. atrox myotoxin I and B. asper myotoxin II, antibodies against synthetic peptide 115–129 of the latter were strongly cross-reactive to the former, indicating the antigenic conservation of this site, known to be critical for the membrane-damaging activities of Lys49 myotoxins. | es_ES |
dc.description.sponsorship | Universidad de Costa Rica/[741-99-269]/UCR/Costa Rica | es_ES |
dc.description.sponsorship | United Nations Educational, Scientific and Cultural Organization/[883.701-3]/UNESCO/ | es_ES |
dc.description.sponsorship | Embassy of Japan///Costa Rica | es_ES |
dc.language.iso | en_US | es_ES |
dc.source | Toxicon; Volumen 44, Número 1. 2004 | es_ES |
dc.subject | Myotoxin | es_ES |
dc.subject | Phospholipase A2 | es_ES |
dc.subject | Lys49 | es_ES |
dc.subject | Bothrops | es_ES |
dc.subject | Snake venom | es_ES |
dc.title | Structural and functional characterization of myotoxin I, a Lys49 phospholipase A2 homologue from the venom of the snake Bothrops atrox | es_ES |
dc.type | artículo original | |
dc.identifier.doi | 10.1016/j.toxicon.2004.04.013 | |
dc.description.procedence | UCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP) | es_ES |
dc.identifier.codproyecto | 741-99-269 | |
dc.identifier.pmid | 15225567 |
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Microbiología [1171]