TY - JOUR
T1 - Exploring the biological activities and proteome of Brazilian scorpion Rhopalurus agamemnon venom
AU - Magalhães, Ana Carolina Martins
AU - de Santana, Carlos José Correia
AU - Melani, Rafael D.
AU - Domont, Gilberto B.
AU - Castro, Mariana S.
AU - Fontes, Wagner
AU - Roepstorff, Peter
AU - Júnior, Osmindo Rodrigues Pires
N1 - Funding Information:
This work was funded by National Council for Scientific and technological Development (CNPq) and The Brazilian Federal Agency for Support and Assessment of Post-Graduate Education (CAPES) for granting the PhD scholarship. and the University of Brasilia for financial support Grant ID 1/2019 ans 1/2020 .
Publisher Copyright:
© 2021 Elsevier B.V.
PY - 2021/4/15
Y1 - 2021/4/15
N2 - Scorpion venoms are formed by toxins harmful to various organisms, including humans. Several techniques have been developed to understand the role of proteins in animal venoms, including proteomics approach. Rhopalurus agamemnon (Koch, 1839) is the largest scorpion in the Buthidae family in the Brazilian Cerrado, measuring up to 110 mm in total length. The accident with R. agamemnon is painful and causes some systemic reactions, but the specie's venom remains uninvestigated. We explore the venom protein composition using a proteomic and a biological-directed approach identifying 230 protein compounds including enzymes like Hyaluronidase, metalloproteinase, L-amino acid oxidase and amylase, the last two are first reported for scorpion venoms. Some of those new reports are important to demonstrate how distant we are from a total comprehension of the diversity about venoms in general, due to their diversity in composition and function. Biological significance: In this study, we explored the composition of venom proteins from the scorpion Rhopalurus agamemnon. We identified 230 proteins from the venom including new enzyme reports. These data highlight the unique diversity of the venom proteins from the scorpion R. agamemnon, provide insights into new mechanisms of envenomation and enlarge the protein database of scorpion venoms. The discovery of new proteins provides a new scenario for the development of new drugs and suggests molecular targets to venom components.
AB - Scorpion venoms are formed by toxins harmful to various organisms, including humans. Several techniques have been developed to understand the role of proteins in animal venoms, including proteomics approach. Rhopalurus agamemnon (Koch, 1839) is the largest scorpion in the Buthidae family in the Brazilian Cerrado, measuring up to 110 mm in total length. The accident with R. agamemnon is painful and causes some systemic reactions, but the specie's venom remains uninvestigated. We explore the venom protein composition using a proteomic and a biological-directed approach identifying 230 protein compounds including enzymes like Hyaluronidase, metalloproteinase, L-amino acid oxidase and amylase, the last two are first reported for scorpion venoms. Some of those new reports are important to demonstrate how distant we are from a total comprehension of the diversity about venoms in general, due to their diversity in composition and function. Biological significance: In this study, we explored the composition of venom proteins from the scorpion Rhopalurus agamemnon. We identified 230 proteins from the venom including new enzyme reports. These data highlight the unique diversity of the venom proteins from the scorpion R. agamemnon, provide insights into new mechanisms of envenomation and enlarge the protein database of scorpion venoms. The discovery of new proteins provides a new scenario for the development of new drugs and suggests molecular targets to venom components.
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U2 - 10.1016/j.jprot.2021.104119
DO - 10.1016/j.jprot.2021.104119
M3 - Article
C2 - 33540062
AN - SCOPUS:85100883864
SN - 1874-3919
VL - 237
JO - Journal of Proteomics
JF - Journal of Proteomics
M1 - 104119
ER -