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Toxins 2017, 9(3), 81; doi:10.3390/toxins9030081

Electrophysiological Characterization of the Antarease Metalloprotease from Tityus serrulatus Venom

1
Dipartimento di Scienze Biomediche and Istituto CNR di Neuroscienze, Università di Padova, Via Ugo Bassi 58/B, 35121 Padova, Italy
2
Laboratório de Venenos e Toxinas Animais, Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte 31270-901, MG, Brazil
*
Authors to whom correspondence should be addressed.
Academic Editor: Bryan Grieg Fry
Received: 4 November 2016 / Revised: 15 February 2017 / Accepted: 20 February 2017 / Published: 27 February 2017
(This article belongs to the Section Animal Venoms)
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Abstract

Scorpions are among the oldest venomous living organisms and the family Buthidae is the largest and most medically relevant one. Scorpion venoms include many toxic peptides, but recently, a metalloprotease from Tityus serrulatus called antarease was reported to be capable of cleaving VAMP2, a protein involved in the neuroparalytic syndromes of tetanus and botulism. We have produced antarease and an inactive metalloprotease mutant in a recombinant form and analyzed their enzymatic activity on recombinant VAMP2 in vitro and on mammalian and insect neuromuscular junction. The purified recombinant antarease paralyzed the neuromuscular junctions of mice and of Drosophila melanogaster whilst the mutant was inactive. We were unable to demonstrate any cleavage of VAMP2 under conditions which leads to VAMP proteolysis by botulinum neurotoxin type B. Antarease caused a reduced release probability, mainly due to defects upstream of the synaptic vesicles fusion process. Paired pulse experiments indicate that antarease might proteolytically inactivate a voltage-gated calcium channel. View Full-Text
Keywords: antarease; scorpion; Zn-metalloprotease; vesicle associated membrane protein 2 (VAMP2); botulinum neurotoxins antarease; scorpion; Zn-metalloprotease; vesicle associated membrane protein 2 (VAMP2); botulinum neurotoxins
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Zornetta, I.; Scorzeto, M.; Mendes Dos Reis, P.V.; De Lima, M.E.; Montecucco, C.; Megighian, A.; Rossetto, O. Electrophysiological Characterization of the Antarease Metalloprotease from Tityus serrulatus Venom. Toxins 2017, 9, 81.

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