Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/18016
Title: Novel Catalytically-Inactive PII Metalloproteinases from a Viperid Snake Venom with Substitutions in the Canonical Zinc-Binding Motif
Authors: Camacho, Erika
Sanz, Libia
Escalante, Teresa
Pérez, Alicia
Villalta, Fabián
Lomonte, Bruno
Ferreira, Ana Gisele C. Neves
Feoli, Andrés
Calvete, Juan J.
Gutiérrez, José María
Rucavado, Alexandra
Affilliation: Universidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
Instituto de Biomedicina de Valencia. Consejo Superior de Investigaciones Científicas. Valencia, Spain.
Universidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
Instituto de Biomedicina de Valencia. Consejo Superior de Investigaciones Científicas. Valencia, Spain.
Universidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
Universidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil.
Universidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
Instituto de Biomedicina de Valencia. Consejo Superior de Investigaciones Científicas. Valencia, Spain / Universidad Politécnica de Valencia. Departamento de Biotecnologia. Valencia, Spain.
Universidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
Universidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
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.
Keywords: snake venom metalloproteinases
PII SVMP homologues
disintegrin domain
zinc-binding motif
hemorrhagic activity
platelet aggregation
proteinase activity
keywords: Metaloproteinases de veneno de cobra
Domínio da desintegração
Motivo de ligação ao zinco
Atividade hemorrágica
Agregação de plaquetas
Atividade de proteinase
Issue Date: 2016
Publisher: MDPI
Citation: CAMACHO, Erika; et al. Novel Catalytically-Inactive PII Metalloproteinases from a Viperid Snake Venom with Substitutions in the Canonical Zinc-Binding Motif. Toxins (Basel), v.8, n.10:292,18 p, 2016.
DOI: 10.3390/toxins8100292
ISSN: 2072-6651
Copyright: open access
Appears in Collections:IOC - Artigos de Periódicos

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