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

AutorCamacho, Erika; Sanz, Libia ; Escalante, Teresa; Pérez, Alicia ; Villalta, Fabián; Lomonte, Bruno; Neves-Ferreira, Ana Gisele C.; Feoli, Andrés; Calvete, Juan J. ; Gutiérrez, José María; Rucavado, Alexandra
Palabras claveSsnake venom metalloproteinases
PII SVMP homologues
disintegrin domain
zinc-binding motif
hemorrhagic activity
platelet aggregation
proteinase activity
Fecha de publicación30-sep-2016
EditorMolecular Diversity Preservation International
CitaciónToxins; 8(10): E292 (2016)
ResumenSnake 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.
DescripciónArtículo electrónico, 18 páginas, 6 figuras, 1 tabla
URIhttp://hdl.handle.net/10261/139962
DOIhttp://dx.doi.org/10.3390/toxins8100292
E-ISSN2072-6651
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