Proteomic and toxinological characterization of Peruvian pitviper Bothrops brazili (“jergón shushupe”), venom

Carolina Rego Rodrigues; Denis Alexis Molina Molina; Thamyres C. Silva de Assis; Camila Liberato; Marcella N. Melo-Braga; César Bonilla Ferreyra; Javier Cárdenas; Fernanda Costal-Oliveira; Clara Guerra-Duarte; Carlos Chávez-Olórtegui

doi:10.1016/j.toxicon.2020.05.016

Proteomic and toxinological characterization of Peruvian pitviper Bothrops brazili (“jergón shushupe”), venom

Carolina Rego Rodrigues, Denis Alexis Molina Molina, Thamyres C. Silva de Assis, Camila Liberato, Marcella N. Melo-Braga, César Bonilla Ferreyra, Javier Cárdenas, Fernanda Costal-Oliveira, Clara Guerra-Duarte, Carlos Chávez-Olórtegui

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Bothrops brazili is a pitviper from Amazonian region, responsible for many accidents in Peru. Despite its relevance, its venom has not been extensively characterized. In the present work, Bothrops brazili venom (BbV) components were analyzed by RP-HPLC, SDS-PAGE and MALDI-TOF/TOF. Approximately 37 proteins were identified, belonging to 7 families. Snake venom metalloproteinases (SVMPs) were the most abundant proteins of the venom (33.05%), followed by snake venom serine proteinases (SVSPs, 26.11%), phospholipases A₂ (PLA₂, 25.57%), snake C-type lectins (CTLs, 9.61%), L-aminoacid oxidase (LAAO, 3.80%), cystein-rich secretory proteins (CRISP, 1.67%) and Bradykinin-potentiating peptide (BPP, 0.20%). In vitro enzymatic activities of BbV showed high levels of SVMP activity and reduced Hyal activity in comparison with other bothropic venoms. Furthermore, BbV reduced VERO cells viability. ELISA and Western Blotting showed that both Peruvian and Brazilian bothropic antivenoms were able to recognize BbV components. This work provides an overview of BbV venom content and indicates a potential efficiency of Peruvian and Brazilian antivenoms to treat accidents with this species.

Original language	English
Pages (from-to)	19-27
Number of pages	9
Journal	Toxicon
Volume	184
DOIs	https://doi.org/10.1016/j.toxicon.2020.05.016
State	Published - Sep 2020

Bibliographical note

Funding Information:
This research was supported by the Conselho Nacional de Desenvolvimento Cientíﬁco e Tecnológico , Brazil ( CNPq ) (Process: 406163/2018-9 ), Coordenação de Aperfeiçoamento de Pessoal de Nível Superior , Brazil - CAPES (Program COFECUB; Process: 88881.191812/2018-01 ) and by Fundação de Amparo à Pesquisa do Estado de Minas Gerais, Brazil ( FAPEMIG; Process: PPM-00270-16 ).

Publisher Copyright:
© 2020 Elsevier Ltd

Keywords

Amazonian region
Bothropic venoms
Bothrops brazili
MALDI-TOF/TOF
Proteomic analyses

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10.1016/j.toxicon.2020.05.016

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Rodrigues, C. R., Molina, D. A. M., Silva de Assis, T. C., Liberato, C., Melo-Braga, M. N., Ferreyra, C. B., Cárdenas, J., Costal-Oliveira, F., Guerra-Duarte, C., & Chávez-Olórtegui, C. (2020). Proteomic and toxinological characterization of Peruvian pitviper Bothrops brazili (“jergón shushupe”), venom. Toxicon, 184, 19-27. https://doi.org/10.1016/j.toxicon.2020.05.016

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title = "Proteomic and toxinological characterization of Peruvian pitviper Bothrops brazili (“jerg{\'o}n shushupe”), venom",

abstract = "Bothrops brazili is a pitviper from Amazonian region, responsible for many accidents in Peru. Despite its relevance, its venom has not been extensively characterized. In the present work, Bothrops brazili venom (BbV) components were analyzed by RP-HPLC, SDS-PAGE and MALDI-TOF/TOF. Approximately 37 proteins were identified, belonging to 7 families. Snake venom metalloproteinases (SVMPs) were the most abundant proteins of the venom (33.05%), followed by snake venom serine proteinases (SVSPs, 26.11%), phospholipases A2 (PLA2, 25.57%), snake C-type lectins (CTLs, 9.61%), L-aminoacid oxidase (LAAO, 3.80%), cystein-rich secretory proteins (CRISP, 1.67%) and Bradykinin-potentiating peptide (BPP, 0.20%). In vitro enzymatic activities of BbV showed high levels of SVMP activity and reduced Hyal activity in comparison with other bothropic venoms. Furthermore, BbV reduced VERO cells viability. ELISA and Western Blotting showed that both Peruvian and Brazilian bothropic antivenoms were able to recognize BbV components. This work provides an overview of BbV venom content and indicates a potential efficiency of Peruvian and Brazilian antivenoms to treat accidents with this species.",

keywords = "Amazonian region, Bothropic venoms, Bothrops brazili, MALDI-TOF/TOF, Proteomic analyses",

author = "Rodrigues, {Carolina Rego} and Molina, {Denis Alexis Molina} and {Silva de Assis}, {Thamyres C.} and Camila Liberato and Melo-Braga, {Marcella N.} and Ferreyra, {C{\'e}sar Bonilla} and Javier C{\'a}rdenas and Fernanda Costal-Oliveira and Clara Guerra-Duarte and Carlos Ch{\'a}vez-Ol{\'o}rtegui",

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doi = "10.1016/j.toxicon.2020.05.016",

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T1 - Proteomic and toxinological characterization of Peruvian pitviper Bothrops brazili (“jergón shushupe”), venom

AU - Rodrigues, Carolina Rego

AU - Molina, Denis Alexis Molina

AU - Silva de Assis, Thamyres C.

AU - Liberato, Camila

AU - Melo-Braga, Marcella N.

AU - Ferreyra, César Bonilla

AU - Cárdenas, Javier

AU - Costal-Oliveira, Fernanda

AU - Guerra-Duarte, Clara

AU - Chávez-Olórtegui, Carlos

PY - 2020/9

Y1 - 2020/9

N2 - Bothrops brazili is a pitviper from Amazonian region, responsible for many accidents in Peru. Despite its relevance, its venom has not been extensively characterized. In the present work, Bothrops brazili venom (BbV) components were analyzed by RP-HPLC, SDS-PAGE and MALDI-TOF/TOF. Approximately 37 proteins were identified, belonging to 7 families. Snake venom metalloproteinases (SVMPs) were the most abundant proteins of the venom (33.05%), followed by snake venom serine proteinases (SVSPs, 26.11%), phospholipases A2 (PLA2, 25.57%), snake C-type lectins (CTLs, 9.61%), L-aminoacid oxidase (LAAO, 3.80%), cystein-rich secretory proteins (CRISP, 1.67%) and Bradykinin-potentiating peptide (BPP, 0.20%). In vitro enzymatic activities of BbV showed high levels of SVMP activity and reduced Hyal activity in comparison with other bothropic venoms. Furthermore, BbV reduced VERO cells viability. ELISA and Western Blotting showed that both Peruvian and Brazilian bothropic antivenoms were able to recognize BbV components. This work provides an overview of BbV venom content and indicates a potential efficiency of Peruvian and Brazilian antivenoms to treat accidents with this species.

AB - Bothrops brazili is a pitviper from Amazonian region, responsible for many accidents in Peru. Despite its relevance, its venom has not been extensively characterized. In the present work, Bothrops brazili venom (BbV) components were analyzed by RP-HPLC, SDS-PAGE and MALDI-TOF/TOF. Approximately 37 proteins were identified, belonging to 7 families. Snake venom metalloproteinases (SVMPs) were the most abundant proteins of the venom (33.05%), followed by snake venom serine proteinases (SVSPs, 26.11%), phospholipases A2 (PLA2, 25.57%), snake C-type lectins (CTLs, 9.61%), L-aminoacid oxidase (LAAO, 3.80%), cystein-rich secretory proteins (CRISP, 1.67%) and Bradykinin-potentiating peptide (BPP, 0.20%). In vitro enzymatic activities of BbV showed high levels of SVMP activity and reduced Hyal activity in comparison with other bothropic venoms. Furthermore, BbV reduced VERO cells viability. ELISA and Western Blotting showed that both Peruvian and Brazilian bothropic antivenoms were able to recognize BbV components. This work provides an overview of BbV venom content and indicates a potential efficiency of Peruvian and Brazilian antivenoms to treat accidents with this species.

KW - Amazonian region

KW - Bothropic venoms

KW - Bothrops brazili

KW - MALDI-TOF/TOF

KW - Proteomic analyses

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DO - 10.1016/j.toxicon.2020.05.016

M3 - Artículo

C2 - 32479836

AN - SCOPUS:85085936197

SN - 0041-0101

VL - 184

SP - 19

EP - 27

JO - Toxicon

JF - Toxicon

ER -

Proteomic and toxinological characterization of Peruvian pitviper Bothrops brazili (“jergón shushupe”), venom

Abstract

Bibliographical note

Keywords

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