Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/23195
Title: An in-depth snake venom proteopeptidome characterization: Benchmarking Bothrops jararaca
Authors: Nicolau, Carolina A.
Carvalho, Paulo C.
Azevedo, Inácio L. M. Junqueira de
Ferreira, André Teixeira
Junqueira, Magno
Perales, Jonas
Ferreira, Ana Gisele C. Neves
Valente, Richard H.
Affilliation: Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil / Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil / Fundação Oswaldo Cruz. Instituto Carlos Chagas. Laboratório para Proteomica e Engenharia de Proteínas. Paraná, Brasil
Înstituto Butantan. Laboratório Especial de Toxinologia. São Paulo, SP, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil / Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil.
Universidade Federal do Rio de Janeiro. Departamento de Bioquímica. Rede de Proteômica do Rio de Janeiro. Rio de Janeiro, RJ, Brasil / .Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil / Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil / Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil / Instituto Nacional de Ciência e Tecnologia em Toxinas, CNPq. Brasília, DF, Brasil.
Abstract: A large-scale proteomic approach was devised to advance the understanding of venom composition. Bothrops jararaca venom was fractionated by OFFGEL followed by chromatography, generating peptidic and proteic fractions. The latter was submitted to trypsin digestion. Both fractions were separately analyzed by reversed-phase nanochromatography coupled to high resolution mass spectrometry. This strategy allowed deeper and joint characterizations of the peptidome and proteome (proteopeptidome) of this venom. Our results lead to the identification of 46 protein classes (with several uniquely assigned proteins per class) comprising eight high-abundance bona fide venom components, and 38 additional classes in smaller quantities. This last category included previously described B. jararaca venom proteins, common Elapidae venom constituents (cobra venom factor and three-finger toxin), and proteins typically encountered in lysosomes, cellular membranes and blood plasma. Furthermore, this report is the most complete snake venom peptidome described so far, both in number of peptides and in variety of unique proteins that could have originated them. It is hypothesized that such diversity could enclose cryptides, whose bioactivities would contribute to envenomation in yet undetermined ways. Finally, we propose that the broad range screening of B. jararaca peptidome will facilitate the discovery of bioactive molecules, eventually leading to valuable therapeutical agents.
Keywords: Bothrops jararaca
Cryptome
OFFGEL
Proteopeptidome
Proteomics
Snake venomics
keywords: Bothrops
Proteômica
Venenos de Serpentes
Issue Date: 2017
Publisher: Elsevier
Citation: NICOLAU, Carolina A. et al. An in-depth snake venom proteopeptidome characterization: Benchmarking Bothrops jararaca. Journal of Proteomicsv. v.151, p.214–231, June 2017.
DOI: 10.1016/j.jprot.2016.06.029
ISSN: 1874-3919
Copyright: restricted access
Appears in Collections:PR - ICC - Artigos de Periódicos
IOC - Artigos de Periódicos

Files in This Item:
File Description SizeFormat 
jonas2_perales_etal_IOC_2017.pdf1.65 MBAdobe PDF    Request a copy


FacebookTwitterDeliciousLinkedInGoogle BookmarksBibTex Format mendeley Endnote DiggMySpace

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.