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Toxins 2016, 8(10), 292; doi:10.3390/toxins8100292

Novel Catalytically-Inactive PII Metalloproteinases from a Viperid Snake Venom with Substitutions in the Canonical Zinc-Binding Motif

1
Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José 11501, Costa Rica
2
Instituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas, Valencia 46010, Spain
3
Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro 21040-900, Brazil
4
Departamento de Biotecnología, Universidad Politécnica de Valencia, Valencia 46022, Spain
*
Author to whom correspondence should be addressed.
Academic Editor: Nicholas R. Casewell
Received: 12 September 2016 / Revised: 28 September 2016 / Accepted: 30 September 2016 / Published: 12 October 2016
(This article belongs to the Special Issue Snake Venom Metalloproteinases)
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Abstract

Snake venom metalloproteinases (SVMPs) play key biological roles in prey immobilization and digestion. The majority of these activities depend on the hydrolysis of relevant protein substrates in the tissues. Hereby, we describe several isoforms and a cDNA clone sequence, corresponding to PII SVMP homologues from the venom of the Central American pit viper Bothriechis lateralis, which have modifications in the residues of the canonical sequence of the zinc-binding motif HEXXHXXGXXH. As a consequence, the proteolytic activity of the isolated proteins was undetectable when tested on azocasein and gelatin. These PII isoforms comprise metalloproteinase and disintegrin domains in the mature protein, thus belonging to the subclass PIIb of SVMPs. PII SVMP homologues were devoid of hemorrhagic and in vitro coagulant activities, effects attributed to the enzymatic activity of SVMPs, but induced a mild edema. One of the isoforms presents the characteristic RGD sequence in the disintegrin domain and inhibits ADP- and collagen-induced platelet aggregation. Catalytically-inactive SVMP homologues may have been hitherto missed in the characterization of snake venoms. The presence of such enzymatically-inactive homologues in snake venoms and their possible toxic and adaptive roles deserve further investigation. View Full-Text
Keywords: snake venom metalloproteinases; PII SVMP homologues; disintegrin domain; zinc-binding motif; hemorrhagic activity; platelet aggregation; proteinase activity snake venom metalloproteinases; PII SVMP homologues; disintegrin domain; zinc-binding motif; hemorrhagic activity; platelet aggregation; proteinase activity
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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

Camacho, E.; Sanz, L.; Escalante, T.; Pérez, A.; Villalta, F.; Lomonte, B.; Neves-Ferreira, A.G.C.; Feoli, A.; Calvete, J.J.; Gutiérrez, J.M.; Rucavado, A. Novel Catalytically-Inactive PII Metalloproteinases from a Viperid Snake Venom with Substitutions in the Canonical Zinc-Binding Motif. Toxins 2016, 8, 292.

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