Proteomic profile, biological activities and antigenic analysis of the venom from Bothriopsis bilineata smaragdina ("loro machaco"), a pitviper snake from Peru

Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas. Departamento de Bioquímica e Imunologia. Belo Horizonte, MG, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil.
Universidad Nacional Jorge Basadre Grohmann. Tacna, Peru.
Fundação Ezequiel Dias. Centro de Pesquisa e Desenvolvimento. Belo Horizonte, MG, Brasil.
Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas. Departamento de Bioquímica e Imunologia. Belo Horizonte, MG, Brasil.
Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas. Departamento de Bioquímica e Imunologia. Belo Horizonte, MG, Brasil.
Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas. Departamento de Bioquímica e Imunologia. Belo Horizonte, MG, Brasil.
Universidade Federal dos Vales do Jequitinhonha e Mucuri. Faculdade de Medicina do Mucuri. Teófilo Otoni, MG, Brasil.
Universidad Nacional Mayor de San Marcos. Lima, Peru.
Instituto Nacional de Salud. Lima, Peru.
Fundação Ezequiel Dias. Centro de Pesquisa e Desenvolvimento. Belo Horizonte, MG, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil.
Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas. Departamento de Bioquímica e Imunologia. Belo Horizonte, MG, Brasil.

Abstract

In order to determine Bothriopsis bilineata smaragdina venom (BbsV) composition, proteomic approaches were performed. Venom components were analyzed by RP-HPLC, SDS- PAGE and nano LC on line with LTQ Orbitrap XL. Results showed a total of 189 identified proteins, grouped into 11 different subgroups, which include snake venom metalloproteinases (SVMPs, 54.67%), snake C-type lectins (Snaclecs, 15.78%), snake venom serine proteinases (SVSPs, 14.69%), cystein-rich secretory proteins (CRISP, 2.61%), phospholipases A2 (PLA2, 1.14%), phosphodiesterase (PDE, 1.17%), venom endothelial growth factor (VEGF, 1.06%) 5'nucleotidases (0.33%), L-amino acid oxidases (LAAOs, 0.28%) and other proteins. In vitro enzymatic activities (SVMP, SVSP, LAAO, Hyal and PLA2) of BbsV were also analyzed. BbsV showed high SVSP activity but low PLA2 activity, when compared to other Bothrops venoms. In vivo, BbsV induced hemorrhage and edema in mice and showed intraperitoneal median lethal dose (LD50) of 92.74 (± 0.15) μg/20 g of mice. Furthermore, BbsV reduced cell viability when incubated with VERO cells. Peruvian and Brazilian bothropic antivenoms recognize BbsV proteins, as detected by ELISA and Western Blotting. Both antivenoms were able to neutralize in vivo edema and hemorrhage.

Keywords in Portuguese

Proteômica de veneno
Caracterização de veneno
Cobra peruana
Bothriopsis bilineata smaragdina

Keywords

Bothriopsis bilineata smaragdina
Venom proteomics
Peruvian snake
Venom characterization

Publisher

Elsevier

Citation

RODRIGUES, Carolina Rego et al. Proteomic profile, biological activities and antigenic analysis of the venom from Bothriopsis bilineata smaragdina (“loro machaco”), a pitviper snake from Peru. Journal of Proteomics, v. 187, p.171-181, July 2018.

DOI

10.1016/j.jprot.2018.07.016

ISSN

1874-3919

Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/32974

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Copyright

Restricted access

Embargo date

2022-01-01

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