Show simple item record

dc.creatorSanz, Libia
dc.creatorEscolano, José
dc.creatorFerretti, Massimo
dc.creatorBiscoglio, Mirtha J.
dc.creatorRivera, Elena
dc.creatorCrescenti, Ernesto J.
dc.creatorAngulo Ugalde, Yamileth
dc.creatorLomonte, Bruno
dc.creatorGutiérrez, José María
dc.creatorCalvete Chornet, Juan José
dc.date.accessioned2016-11-29T15:57:47Z
dc.date.available2016-11-29T15:57:47Z
dc.date.issued2008-04-30
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S1874391907002503es_ES
dc.identifier.issn1874-3919
dc.identifier.urihttp://hdl.handle.net/10669/29335
dc.description.abstractWe report the proteomic characterization of the venoms of two closely related pit vipers of the genus Lachesis, L. muta (South American Bushmaster) and L. stenophrys (Central American Bushmaster), and compare the toxin repertoire of the former revealed through a proteomic versus a transcriptomic approach. The protein composition of the venoms of Lachesis muta and L. stenophrys were analyzed by RP-HPLC, N-terminal sequencing, MALDI-TOF peptide mass fingerprinting and CID-MS/MS. Around 30–40 proteins of molecular masses in the range of 13–110 kDa and belonging, respectively, to only 8 and 7 toxin families were identified in L. muta and L. stenophrys venoms. In addition, both venoms contained a large number of bradykinin-potentiating peptides (BPP) and a C-type natriuretic peptide (C-NP). BPPs and C-NP comprised around 15% of the total venom proteins. In both species, the most abundant proteins were Zn2+-metalloproteinases (32–38%) and serine proteinases (25–31%), followed by PLA2s (9–12%), galactose-specific C-type lectin (4–8%), l-amino acid oxidase (LAO, 3–5%), CRISP (1.8%; found in L. muta but not in L. stenophrys), and NGF (0.6%). On the other hand, only six L. muta venom-secreted proteins matched any of the previously reported 11 partial or full-length venom gland transcripts, and venom proteome and transcriptome depart in their relative abundances of different toxin families. As expected from their close phylogenetic relationship, the venoms of L. muta and L. stenophrys share (or contain highly similar) proteins, in particular BPPs, serine proteinases, a galactose-specific C-type lectin, and LAO. However, they dramatically depart in their respective PLA2 complement. Intraspecific quantitative and qualitative differences in the expression of PLA2 molecules were found when the venoms of five L. muta specimens (3 from Bolivia and 2 from Peru) and the venom of the same species purchased from Sigma were compared. These observations indicate that these class of toxins represents a rapidly-evolving gene family, and suggests that functional differences due to structural changes in PLA2s molecules among these snakes may have been a hallmark during speciation and adaptation of diverging snake populations to new ecological niches, or competition for resources in existing ones. Our data may contribute to a deeper understanding of the biology and ecology of these snakes, and may also serve as a starting point for studying structure–function correlations of individual toxins.es_ES
dc.description.sponsorshipMinisterio de Educación y Ciencia/[BFU2004-01432/BMC]//Españaes_ES
dc.description.sponsorshipConsejo Superior de Investigaciones Científicas/[CSIC-UCR 2006CR0010]/CSIC-UCR/Españaes_ES
dc.language.isoen_USes_ES
dc.sourceJournal of Proteomics; Volumen 71, Número 1. 2008es_ES
dc.subjectSnake venomicses_ES
dc.subjectVenom proteomicses_ES
dc.subjectSnake toxines_ES
dc.subjectLachesis Mutaes_ES
dc.subjectLachesis Stenophryses_ES
dc.subjectBushmasteres_ES
dc.subjectPit viperes_ES
dc.subjectMass spectrometryes_ES
dc.subjectSnake venomes_ES
dc.titleSnake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysises_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/j.jprot.2007.10.004
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record