Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/18016
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dc.contributor.authorCamacho, Erika
dc.contributor.authorSanz, Libia
dc.contributor.authorEscalante, Teresa
dc.contributor.authorPérez, Alicia
dc.contributor.authorVillalta, Fabián
dc.contributor.authorLomonte, Bruno
dc.contributor.authorFerreira, Ana Gisele C. Neves
dc.contributor.authorFeoli, Andrés
dc.contributor.authorCalvete, Juan J.
dc.contributor.authorGutiérrez, José María
dc.contributor.authorRucavado, Alexandra
dc.date.accessioned2017-03-13T13:26:02Z
dc.date.available2017-03-13T13:26:02Z
dc.date.issued2016
dc.identifier.citationCAMACHO, 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.
dc.identifier.issn2072-6651
dc.identifier.urihttps://www.arca.fiocruz.br/handle/icict/18016
dc.language.isoeng
dc.publisherMDPI
dc.rightsopen access
dc.subject.otherMetaloproteinases de veneno de cobra
dc.subject.otherDomínio da desintegração
dc.subject.otherMotivo de ligação ao zinco
dc.subject.otherAtividade hemorrágica
dc.subject.otherAgregação de plaquetas
dc.subject.otherAtividade de proteinase
dc.titleNovel Catalytically-Inactive PII Metalloproteinases from a Viperid Snake Venom with Substitutions in the Canonical Zinc-Binding Motif
dc.typeArticle
dc.identifier.doi10.3390/toxins8100292
dc.description.abstractenSnake 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.
dc.creator.affilliationUniversidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
dc.creator.affilliationInstituto de Biomedicina de Valencia. Consejo Superior de Investigaciones Científicas. Valencia, Spain.
dc.creator.affilliationUniversidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
dc.creator.affilliationInstituto de Biomedicina de Valencia. Consejo Superior de Investigaciones Científicas. Valencia, Spain.
dc.creator.affilliationUniversidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
dc.creator.affilliationUniversidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
dc.creator.affilliationFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxinologia. Rio de Janeiro, RJ. Brasil.
dc.creator.affilliationUniversidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
dc.creator.affilliationInstituto de Biomedicina de Valencia. Consejo Superior de Investigaciones Científicas. Valencia, Spain / Universidad Politécnica de Valencia. Departamento de Biotecnologia. Valencia, Spain.
dc.creator.affilliationUniversidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
dc.creator.affilliationUniversidad de Costa Rica. Instituto Clodomiro Picado. Facultad de Microbiologia. San Jose, Costa, Rica.
dc.subject.ensnake venom metalloproteinases
dc.subject.enPII SVMP homologues
dc.subject.endisintegrin domain
dc.subject.enzinc-binding motif
dc.subject.enhemorrhagic activity
dc.subject.enplatelet aggregation
dc.subject.enproteinase activity
dc.identifier.eissn2072-6651
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