Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/31951
Title: Proteomic deep mining the venom of the Red-Headed Krait, Bungarus flaviceps
Authors: Chapeaurouge, Alex
Silva, Andreza
Carvalho, Paulo Costa
McCleary, Ryan J. R.
Modahl, Cassandra Marie
Perales, Jonas
Kini, R. Manjunatha
Mackessy, Stephen P.
Affilliation: Fundação Oswaldo Cruz. Ceará, CE, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Carlos Chagas. Grupo de Espectrometria de Massas Computacional e Proteômica. Curitiba, PR, Brasil.
Departamento of Biology. Stetson University. Florida, United States of America.
Departamento of Biological Sciences. National University of Singapore. Singapore.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ, Brasil.
Departamento of Biological Sciences. National University of Singapore. Singapore.
School of Biological Sciences. University of Northern Colorado. Greeley, CO, United States of America.
Abstract: The use of -omics technologies allows for the characterization of snake venom composition at a fast rate and at high levels of detail. In the present study, we investigated the protein content of Red-headed Krait (Bungarus flaviceps) venom. This analysis revealed a high diversity of snake venom protein families, as evidenced by high-throughput mass spectrometric analysis. We found all six venom protein families previously reported in a transcriptome study of the venom gland of B. flaviceps, including phospholipases A₂ (PLA₂s), Kunitz-type serine proteinase inhibitors (KSPIs), three-finger toxins (3FTxs), cysteine-rich secretory proteins (CRISPs), snaclecs, and natriuretic peptides. A combined approach of automated database searches and de novo sequencing of tandem mass spectra, followed by sequence similarity searches, revealed the presence of 12 additional toxin families. De novo sequencing alone was able to identify 58 additional peptides, and this approach contributed significantly to the comprehensive description of the venom. Abundant protein families comprise 3FTxs (22.3%), KSPIs (19%), acetylcholinesterases (12.6%), PLA₂s (11.9%), venom endothelial growth factors (VEGFs, 8.4%), nucleotidases (4.3%), and C-type lectin-like proteins (snaclecs, 3.3%); an additional 11 toxin families are present at significantly lower concentrations, including complement depleting factors, a family not previously detected in Bungarus venoms. The utility of a multifaceted approach toward unraveling the proteome of snake venoms, employed here, allowed detection of even minor venom components. This more in-depth knowledge of the composition of B. flaviceps venom facilitates a better understanding of snake venom molecular evolution, in turn contributing to more effective treatment of krait bites.
Keywords: Bungarotoxins
Snake Venoms
Enzymes
Proteome
Keywords in spanish: Venenos de Serpiente
keywords: Bungarus
DeCS: Bungarotoxinas
Venenos de Serpentes
Enzimas
Proteoma
Issue Date: 2018
Publisher: MDPI
Citation: CHAPEAUROUGE, Alex. Proteomic deep mining the venom of the Red-Headed Krait, Bungarus flaviceps.Toxins, v. 10, n. 373, 2018.
DOI: 10.3390/toxins10090373
ISSN: 2072-6651
Copyright: open access
Appears in Collections:PR - ICC - Artigos de Periódicos

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