Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/31090
Title: Crotalid snake venom subproteomes unraveled by the antiophidic protein DM43
Authors: Rocha, Surza L. G.
Ferreira, Ana G. C. Neves
Trugilho, Monique R. O.
Chapeaurouge, Alex
León, Ileana R.
Valente, Richard H.
Domont, Gilberto B.
Perales, Jonas
Affilliation: Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil / Universidade Federal do Rio de Janeiro. Rio de Janeiro, RJ, Brasil / Rede Proteômica do Rio de Janeiro. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil / Rede Proteômica do Rio de Janeiro. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil / Rede Proteômica do Rio de Janeiro. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil / Rede Proteômica do Rio de Janeiro. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil / Rede Proteômica do Rio de Janeiro. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil / Rede Proteômica do Rio de Janeiro. Rio de Janeiro, RJ, Brasil.
Universidade Federal do Rio de Janeiro. Rio de Janeiro, RJ, Brasil / Rede Proteômica do Rio de Janeiro. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil / Rede Proteômica do Rio de Janeiro. Rio de Janeiro, RJ, Brasil.
Abstract: Snake venoms are mixtures of proteins and peptides with different biological activities, many of which are very toxic. Several animals, including the opossum Didelphis aurita, are resistant to snake venoms due to the presence of neutralizing factors in their blood. An antihemorrhagic protein named DM43 was isolated from opossum serum. It inhibits snake venom metalloproteinases through noncovalent complex formation with these enzymes. In this study, we have used DM43 and proteomic techniques to explore snake venom subproteomes. Four crotalid venoms were chromatographed through an affinity column containing immobilized DM43. Bound fractions were analyzed by one- and two-dimensional gel electrophoresis, followed by identification by MALDI-TOF/TOF mass spectrometry. With this approach, we could easily visualize and compare the metalloproteinase compositions of Bothrops atrox, Bothrops jararaca, Bothrops insularis, and Crotalus atrox snake venoms. The important contribution of proteolytic processing to the complexity of this particular subproteome was demonstrated. Fractions not bound to DM43 column were similarly analyzed and were composed mainly of serine proteinases, C-type lectins, C-type lectin-like proteins, l-amino acid oxidases, nerve growth factor, cysteine-rich secretory protein, a few metalloproteinases (and their fragments), and some unidentified spots. Although very few toxin families were represented in the crotalid venoms analyzed, the number of protein spots detected was in the hundreds, indicating an important protein variability in these natural secretions. DM43 affinity chromatography and associated proteomic techniques proved to be useful tools to separate and identify proteins from snake venoms, contributing to a better comprehension of venom heterogeneity.
Keywords: Snake
venom
toxin
metalloproteinase
inhibitor
proteomics
mass spectrometry
keywords: Serpente
veneno
toxina
metaloproteinase
inibidor
proteômica
espectometria de massa
Issue Date: 2009
Publisher: American Chemical Society
Citation: ROCHA, Surza L. G. et al. Crotalid Snake Venom Subproteomes Unraveled by the Antiophidic Protein DM43. Journal of Proteome Research, v.8, p.2351–2360 2351, 2009.
DOI: 10.1021/pr800977s
ISSN: 1535-3893
Copyright: restricted access
Appears in Collections:IOC - Artigos de Periódicos

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