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Article

Insights into the Hypertensive Effects of Tityus serrulatus Scorpion Venom: Purification of an Angiotensin-Converting Enzyme-Like Peptidase

by
Daniela Cajado-Carvalho
1,
Alexandre Kazuo Kuniyoshi
1,
Bruno Duzzi
1,
Leo Kei Iwai
2,
Úrsula Castro de Oliveira
2,
Inácio De Loiola Meirelles Junqueira de Azevedo
2,
Roberto Tadashi Kodama
1 and
Fernanda Vieira Portaro
1,*
1
Immunochemistry Laboratory, Butantan Institute, São Paulo CEP 05503-900, SP, Brazil
2
Special Laboratory for Applied Toxinology, Butantan Institute/Center of Toxins, Immune-Response and Cell Signaling (CeTICS), São Paulo CEP 05503-900, SP, Brazil
*
Author to whom correspondence should be addressed.
Toxins 2016, 8(12), 348; https://doi.org/10.3390/toxins8120348
Submission received: 7 October 2016 / Revised: 1 November 2016 / Accepted: 16 November 2016 / Published: 24 November 2016
(This article belongs to the Section Animal Venoms)
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Abstract

The number of cases of envenomation by scorpions has grown significantly in Brazil since 2007, with the most severe cases being caused by the Tityus serrulatus scorpion. Although envenomed patients mostly suffer neurotoxic manifestations, other symptoms, such as hypertension, cannot be exclusively attributed to neurotoxins. Omics analyses have detected plentiful amounts of metalloproteases in T. serrulatus venom. However, the roles played by these enzymes in envenomation are still unclear. Endeavoring to investigate the functions of scorpion venom proteases, we describe here for the first time an Angiotensin I-Converting Enzyme-like peptidase (ACE-like) purified from T. serrulatus venom. The crude venom cleaved natural and fluorescent substrates and these activities were inhibited by captopril. Regarding the serum neutralization, the scorpion antivenom was more effective at blocking the ACE-like activity than arachnid antivenom, although neither completely inhibited the venom cleavage action, even at higher doses. ACE-like was purified from the venom after three chromatographic steps and its identity was confirmed by mass spectrometric and transcriptomic analyses. Bioinformatics analysis showed homology between the ACE-like transcript sequences from Tityus spp. and human testis ACE. These findings advance our understanding of T. serrulatus venom components and may improve treatment of envenomation victims, as ACE-like may contribute to envenomation symptoms, especially the resulting hypertension.
Keywords: ACE-like; Tityus serrulatus venom; proteases; antivenom; hypertension ACE-like; Tityus serrulatus venom; proteases; antivenom; hypertension
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MDPI and ACS Style

Cajado-Carvalho, D.; Kuniyoshi, A.K.; Duzzi, B.; Iwai, L.K.; Oliveira, Ú.C.d.; Junqueira de Azevedo, I.D.L.M.; Kodama, R.T.; Portaro, F.V. Insights into the Hypertensive Effects of Tityus serrulatus Scorpion Venom: Purification of an Angiotensin-Converting Enzyme-Like Peptidase. Toxins 2016, 8, 348. https://doi.org/10.3390/toxins8120348

AMA Style

Cajado-Carvalho D, Kuniyoshi AK, Duzzi B, Iwai LK, Oliveira ÚCd, Junqueira de Azevedo IDLM, Kodama RT, Portaro FV. Insights into the Hypertensive Effects of Tityus serrulatus Scorpion Venom: Purification of an Angiotensin-Converting Enzyme-Like Peptidase. Toxins. 2016; 8(12):348. https://doi.org/10.3390/toxins8120348

Chicago/Turabian Style

Cajado-Carvalho, Daniela, Alexandre Kazuo Kuniyoshi, Bruno Duzzi, Leo Kei Iwai, Úrsula Castro de Oliveira, Inácio De Loiola Meirelles Junqueira de Azevedo, Roberto Tadashi Kodama, and Fernanda Vieira Portaro. 2016. "Insights into the Hypertensive Effects of Tityus serrulatus Scorpion Venom: Purification of an Angiotensin-Converting Enzyme-Like Peptidase" Toxins 8, no. 12: 348. https://doi.org/10.3390/toxins8120348

APA Style

Cajado-Carvalho, D., Kuniyoshi, A. K., Duzzi, B., Iwai, L. K., Oliveira, Ú. C. d., Junqueira de Azevedo, I. D. L. M., Kodama, R. T., & Portaro, F. V. (2016). Insights into the Hypertensive Effects of Tityus serrulatus Scorpion Venom: Purification of an Angiotensin-Converting Enzyme-Like Peptidase. Toxins, 8(12), 348. https://doi.org/10.3390/toxins8120348

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