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Proteomic Deep Mining the Venom of the Red-Headed Krait, Bungarus flaviceps.
Toxins (Basel). 2018 09 13; 10(9)T

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.

Authors+Show Affiliations

Fundação Oswaldo Cruz-Ceará, Rua São José, 2º Pavimento, Precabura, Eusébio 61760-000, Brazil. alexmueller007@web.de.Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro 21045-900, Brazil. ann-x3@hotmail.com.Computational Mass Spectrometry& Proteomics Group, Carlos Chagas Institute, Fiocruz, Paraná 81350-010, Brazil. paulo@pcarvalho.com.Department of Biology, Stetson University, 421 N. Woodland Blvd, DeLand, FL 32723, USA. rmccleary@stetson.edu.Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore. dbscmm@nus.edu.sg.Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro 21045-900, Brazil. jperales@ioc.fiocruz.br.Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore. dbskinim@nus.edu.sg.School of Biological Sciences, University of Northern Colorado, 501 20th St., CB 92, Greeley, CO 80639-0017, USA. stephen.mackessy@unco.edu.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

30217057

Citation

Chapeaurouge, Alex, et al. "Proteomic Deep Mining the Venom of the Red-Headed Krait, Bungarus Flaviceps." Toxins, vol. 10, no. 9, 2018.
Chapeaurouge A, Silva A, Carvalho P, et al. Proteomic Deep Mining the Venom of the Red-Headed Krait, Bungarus flaviceps. Toxins (Basel). 2018;10(9).
Chapeaurouge, A., Silva, A., Carvalho, P., McCleary, R. J. R., Modahl, C. M., Perales, J., Kini, R. M., & Mackessy, S. P. (2018). Proteomic Deep Mining the Venom of the Red-Headed Krait, Bungarus flaviceps. Toxins, 10(9). https://doi.org/10.3390/toxins10090373
Chapeaurouge A, et al. Proteomic Deep Mining the Venom of the Red-Headed Krait, Bungarus Flaviceps. Toxins (Basel). 2018 09 13;10(9) PubMed PMID: 30217057.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Proteomic Deep Mining the Venom of the Red-Headed Krait, Bungarus flaviceps. AU - Chapeaurouge,Alex, AU - Silva,Andreza, AU - Carvalho,Paulo, AU - McCleary,Ryan J R, AU - Modahl,Cassandra Marie, AU - Perales,Jonas, AU - Kini,R Manjunatha, AU - Mackessy,Stephen P, Y1 - 2018/09/13/ PY - 2018/06/13/received PY - 2018/08/28/revised PY - 2018/09/01/accepted PY - 2018/9/16/entrez PY - 2018/9/16/pubmed PY - 2019/7/19/medline KW - Bungarus flaviceps KW - Red-headed Krait KW - enzymes KW - proteome KW - snake venom KW - toxins JF - Toxins JO - Toxins (Basel) VL - 10 IS - 9 N2 - 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. SN - 2072-6651 UR - https://www.unboundmedicine.com/medline/citation/30217057/Proteomic_Deep_Mining_the_Venom_of_the_Red_Headed_Krait_Bungarus_flaviceps_ L2 - https://www.mdpi.com/resolver?pii=toxins10090373 DB - PRIME DP - Unbound Medicine ER -