BoaγPLI: Structural and functional characterization of the gamma phospholipase A2 plasma inhibitor from the non-venomous Brazilian snake Boa constrictor

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dc.creatorCaroline Fabri Bittencourt Rodrigues
dc.creatorCaroline Serino-Silva
dc.creatorKaren de Morais-Zani
dc.creatorVictor Koiti Kavazoi
dc.creatorMarcelo Pires Nogueira de Carvalho
dc.creatorKathleen Fernandes Grego
dc.creatorTassia Chiarelli
dc.creatorAlexandre Keiji Tashima
dc.creatorMarcos Hikari Toyama
dc.creatorAnita Mitico Tanaka-Azevedo
dc.date.accessioned2024-05-28T14:55:55Z
dc.date.accessioned2025-09-09T01:23:47Z
dc.date.available2024-05-28T14:55:55Z
dc.date.issued2020
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
dc.description.sponsorshipFAPESP - Fundação de Amparo à Pesquisa do Estado de São Paulo
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0229657
dc.identifier.issn1932-6203
dc.identifier.urihttps://hdl.handle.net/1843/68727
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofPLoS ONE
dc.rightsAcesso Aberto
dc.subjectFosfolipase C gama
dc.subjectBoa constrictor
dc.subjectPlasma
dc.subjectEnvenenamento
dc.subject.otherPhospholipase C gamma
dc.subject.otherBoa constrictor
dc.subject.otherPlasma
dc.subject.otherEnvenomation
dc.titleBoaγPLI: Structural and functional characterization of the gamma phospholipase A2 plasma inhibitor from the non-venomous Brazilian snake Boa constrictor
dc.typeArtigo de periódico
local.citation.issue2
local.citation.volume15
local.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.
local.identifier.orcidhttps://orcid.org/0000-0003-4244-7268
local.identifier.orcidhttps://orcid.org/0000-0001-9363-3752
local.identifier.orcidhttps://orcid.org/0000-0001-9900-8384
local.identifier.orcidhttps://orcid.org/0000-0001-5978-8718
local.identifier.orcidhttps://orcid.org/0000-0002-0210-8352
local.identifier.orcidhttps://orcid.org/0000-0002-2998-8556
local.identifier.orcidhttps://orcid.org/0000-0002-1332-8895
local.identifier.orcidhttps://orcid.org/0000-0001-6836-3084
local.identifier.orcidhttps://orcid.org/0000-0002-4694-4475
local.publisher.countryBrasil
local.publisher.departmentVET - DEPARTAMENTO DE CLÍNICA E CIRURGIA
local.publisher.initialsUFMG
local.url.externahttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0229657

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