Universidad de Costa Rica
  • Sobre Kérwá
  • Acceso Abierto
  • Cómo Depositar
  • Políticas
  • Contacto
    • español
    • English
  • English 
    • español
    • English
  • Login
View Item 
  •   Kérwá Home
  • Investigación
  • Salud
  • Microbiología
  • View Item
  •   Kérwá Home
  • Investigación
  • Salud
  • Microbiología
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis

Artículo científico
Thumbnail
View/Open
258_2008_J.Proteomics_Sanz_Lachesis_venomics.pdf (1.158Mb)
Date
2008-04-30
Author
Sanz, Libia
Escolano, José
Ferretti, Massimo
Biscoglio, Mirtha J.
Rivera, Elena
Crescenti, Ernesto J.
Angulo Ugalde, Yamileth
Lomonte, Bruno
Gutiérrez, José María
Calvete Chornet, Juan José
Metadata
Show full item record
Abstract
We 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.
URI
http://hdl.handle.net/10669/29335
External link to the item
10.1016/j.jprot.2007.10.004
http://www.sciencedirect.com/science/article/pii/S1874391907002503
Collections
  • Microbiología [879]



  • Repositorios universitarios

  • Repositorio del SIBDI-UCR
  • Biblioteca Digital del CIICLA
  • Repositorio Documental Rafael Obregón Loría (CIHAC)
  • Biblioteca Digital Carlos Melendez (CIHAC)
  • Repositorio de Fotografías
  • Colección de videos de UPA-VAS
  • Sitios recomendados

  • Buscador regional de LA Referencia
  • Buscador del Open ROAR
  • Scientific Electronic Library Online (SciELO)
  • Directory of Open Access Journals (DOAJ)
  • Redalyc
  • Redes sociales

  • facebook.com/repositoriokerwa
  • @Ciencia_UCR
  • Sobre Kérwá
  • Acceso Abierto
  • Cómo depositar
  • Políticas
Contact Us | Send Feedback
Repositorio Institucional de la Universidad de Costa Rica. Algunos derechos reservados. Este repositorio funciona con DSpace.
Universidad de Costa Rica
 

 

Browse

All of KérwáCommunities & CollectionsTitlesAuthorsSubjectsProcedenceTypeThis CollectionTitlesAuthorsSubjectsProcedenceType

My Account

LoginRegister

  • Repositorios universitarios

  • Repositorio del SIBDI-UCR
  • Biblioteca Digital del CIICLA
  • Repositorio Documental Rafael Obregón Loría (CIHAC)
  • Biblioteca Digital Carlos Melendez (CIHAC)
  • Repositorio de Fotografías
  • Colección de videos de UPA-VAS
  • Sitios recomendados

  • Buscador regional de LA Referencia
  • Buscador del Open ROAR
  • Scientific Electronic Library Online (SciELO)
  • Directory of Open Access Journals (DOAJ)
  • Redalyc
  • Redes sociales

  • facebook.com/repositoriokerwa
  • @Ciencia_UCR
  • Sobre Kérwá
  • Acceso Abierto
  • Cómo depositar
  • Políticas
Contact Us | Send Feedback
Repositorio Institucional de la Universidad de Costa Rica. Algunos derechos reservados. Este repositorio funciona con DSpace.
Universidad de Costa Rica