Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/68727
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dc.creatorCaroline Fabri Bittencourt Rodriguespt_BR
dc.creatorCaroline Serino-Silvapt_BR
dc.creatorKaren de Morais-Zanipt_BR
dc.creatorVictor Koiti Kavazoipt_BR
dc.creatorMarcelo Pires Nogueira de Carvalhopt_BR
dc.creatorKathleen Fernandes Gregopt_BR
dc.creatorTassia Chiarellipt_BR
dc.creatorAlexandre Keiji Tashimapt_BR
dc.creatorMarcos Hikari Toyamapt_BR
dc.creatorAnita Mitico Tanaka-Azevedopt_BR
dc.date.accessioned2024-05-28T14:55:55Z-
dc.date.available2024-05-28T14:55:55Z-
dc.date.issued2020-
dc.citation.volume15pt_BR
dc.citation.issue2pt_BR
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0229657pt_BR
dc.identifier.issn1932-6203pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/68727-
dc.description.resumoPlasma in several organisms has components that promote resistance to envenomation by inhibiting specific proteins from snake venoms, such as phospholipases A2 (PLA2s). The major hypothesis for inhibitor’s presence would be the protection against self-envenomation in venomous snakes, but the occurrence of inhibitors in non-venomous snakes and other animals has opened new perspectives for this molecule. Thus, this study showed for the first time the structural and functional characterization of the PLA2 inhibitor from the Boa constrictor serum (BoaγPLI), a non-venomous snake that dwells extensively the Brazilian territory. Therefore, the inhibitor was isolated from B. constrictor serum, with 0.63% of recovery. SDS-PAGE showed a band at ~25 kDa under reducing conditions and ~20 kDa under non-reducing conditions. Chromatographic analyses showed the presence of oligomers formed by BoaγPLI. Primary structure of BoaγPLI suggested an estimated molecular mass of 22 kDa. When BoaγPLI was incubated with Asp-49 and Lys-49 PLA2 there was no severe change in its dichroism spectrum, suggesting a non-covalent interaction. The enzymatic assay showed a dose-dependent inhibition, up to 48.2%, when BoaγPLI was incubated with Asp-49 PLA2, since Lys-49 PLA2 has a lack of enzymatic activity. The edematogenic and myotoxic effects of PLA2s were also inhibited by BoaγPLI. In summary, the present work provides new insights into inhibitors from non-venomous snakes, which possess PLIs in their plasma, although the contact with venom is unlikely.pt_BR
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_BR
dc.description.sponsorshipFAPESP - Fundação de Amparo à Pesquisa do Estado de São Paulopt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentVET - DEPARTAMENTO DE CLÍNICA E CIRURGIApt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofPLoS ONEpt_BR
dc.rightsAcesso Abertopt_BR
dc.subjectPhospholipase C gammapt_BR
dc.subjectBoa constrictorpt_BR
dc.subjectPlasmapt_BR
dc.subjectEnvenomationpt_BR
dc.subject.otherFosfolipase C gamapt_BR
dc.subject.otherBoa constrictorpt_BR
dc.subject.otherPlasmapt_BR
dc.subject.otherEnvenenamentopt_BR
dc.titleBoaγPLI: Structural and functional characterization of the gamma phospholipase A2 plasma inhibitor from the non-venomous Brazilian snake Boa constrictorpt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0229657pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0003-4244-7268pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-9363-3752pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-9900-8384pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-5978-8718pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-0210-8352pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-2998-8556pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-1332-8895pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-6836-3084pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-4694-4475pt_BR
Appears in Collections:Artigo de Periódico



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